Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.
A single-pass transmembrane glycoproteins that mediate CALCIUM-dependent CELL ADHESION and are core components of DESMOSOMES.
A group of desmosomal cadherins with cytoplasmic tails that resemble those of classical CADHERINS.
Desmoplakins are cytoskeletal linker proteins that anchor INTERMEDIATE FILAMENTS to the PLASMA MEMBRANE at DESMOSOMES.
A group of desmosomal cadherins with cytoplasmic tails that are divergent from those of classical CADHERINS. Their intracytoplasmic domains bind PLAKOGLOBIN; PLAKOPHILINS; and DESMOPLAKINS.
A family of cytoskeletal proteins that play essential roles in CELL ADHESION at ADHERENS JUNCTIONS by linking CADHERINS to the ACTIN FILAMENTS of the CYTOSKELETON.
A multi-functional catenin that is highly homologous to BETA CATENIN. Gamma catenin binds CADHERINS and helps link their cytoplasmic tails to ACTIN in the CYTOSKELETON via ALPHA CATENIN. It is also found in DESMOSOMES where it mediates the link between DESMOSOMAL CADHERINS and DESMOPLAKIN.
A type of junction that attaches one cell to its neighbor. One of a number of differentiated regions which occur, for example, where the cytoplasmic membranes of adjacent epithelial cells are closely apposed. It consists of a circular region of each membrane together with associated intracellular microfilaments and an intercellular material which may include, for example, mucopolysaccharides. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990; Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
A catenin that binds F-ACTIN and links the CYTOSKELETON with BETA CATENIN and GAMMA CATENIN.
A CALCIUM-dependent adhesion molecule of DESMOSOMES that also plays a role in embryonic STEM CELL proliferation.
Adherence of cells to surfaces or to other cells.
Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.
A desmosomal cadherin that is an autoantigen in the acquired skin disorder PEMPHIGUS FOLIACEUS.
Direct contact of a cell with a neighboring cell. Most such junctions are too small to be resolved by light microscopy, but they can be visualized by conventional or freeze-fracture electron microscopy, both of which show that the interacting CELL MEMBRANE and often the underlying CYTOPLASM and the intervening EXTRACELLULAR SPACE are highly specialized in these regions. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p792)
A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.
Anchoring points where the CYTOSKELETON of neighboring cells are connected to each other. They are composed of specialized areas of the plasma membrane where bundles of the ACTIN CYTOSKELETON attach to the membrane through the transmembrane linkers, CADHERINS, which in turn attach through their extracellular domains to cadherins in the neighboring cell membranes. In sheets of cells, they form into adhesion belts (zonula adherens) that go all the way around a cell.
Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.
The phenomenon by which dissociated cells intermixed in vitro tend to group themselves with cells of their own type.
A desmosomal cadherin that is an autoantigen in the acquired skin disorder PEMPHIGUS VULGARIS.
A family of proteins that contain several 42-amino acid repeat domains and are homologous to the Drosophila armadillo protein. They bind to other proteins through their armadillo domains and play a variety of roles in the CELL including SIGNAL TRANSDUCTION, regulation of DESMOSOME assembly, and CELL ADHESION.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.
Members of the armadillo family of proteins that are found in DESMOSOMES and interact with various proteins including desmocadherins; DESMOPLAKIN; ACTIN FILAMENTS; and KERATINS.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Any of several ways in which living cells of an organism communicate with one another, whether by direct contact between cells or by means of chemical signals carried by neurotransmitter substances, hormones, and cyclic AMP.
The measurement of frequency or oscillation changes.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Group of chronic blistering diseases characterized histologically by ACANTHOLYSIS and blister formation within the EPIDERMIS.
A subclass of receptor-like protein tryosine phosphatases that contain multiple extracellular immunoglobulin G-like domains and fibronectin type III-like domains. An additional memprin-A5-mu domain is found on some members of this subclass.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action during the developmental stages of an organism.
Proteins obtained from various species of Xenopus. Included here are proteins from the African clawed frog (XENOPUS LAEVIS). Many of these proteins have been the subject of scientific investigations in the area of MORPHOGENESIS and development.
A cytoskeletal protein associated with cell-cell and cell-matrix interactions. The amino acid sequence of human vinculin has been determined. The protein consists of 1066 amino acid residues and its gene has been assigned to chromosome 10.
A subclass of receptor-like protein tryosine phosphatases that contain an extracellular RDGS-adhesion recognition motif and a single cytosolic protein tyrosine phosphate domain.
Epidermal cells which synthesize keratin and undergo characteristic changes as they move upward from the basal layers of the epidermis to the cornified (horny) layer of the skin. Successive stages of differentiation of the keratinocytes forming the epidermal layers are basal cell, spinous or prickle cell, and the granular cell.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Specialized areas at the CELL MEMBRANE where a cell attaches to the EXTRACELLULAR MATRIX or other substratum.
A technique that localizes specific nucleic acid sequences within intact chromosomes, eukaryotic cells, or bacterial cells through the use of specific nucleic acid-labeled probes.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.
Established cell cultures that have the potential to propagate indefinitely.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.
Infections of the nervous system caused by bacteria of the genus HAEMOPHILUS, and marked by prominent inflammation of the MENINGES. HAEMOPHILUS INFLUENZAE TYPE B is the most common causative organism. The condition primarily affects children under 6 years of age but may occur in adults.
A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A rac GTP-binding protein involved in regulating actin filaments at the plasma membrane. It controls the development of filopodia and lamellipodia in cells and thereby influences cellular motility and adhesion. It is also involved in activation of NADPH OXIDASE. This enzyme was formerly listed as EC 3.6.1.47.
The external, nonvascular layer of the skin. It is made up, from within outward, of five layers of EPITHELIUM: (1) basal layer (stratum basale epidermidis); (2) spinous layer (stratum spinosum epidermidis); (3) granular layer (stratum granulosum epidermidis); (4) clear layer (stratum lucidum epidermidis); and (5) horny layer (stratum corneum epidermidis).
Separation of the prickle cells of the stratum spinosum of the epidermis, resulting in atrophy of the prickle cell layer. It is seen in diseases such as pemphigus vulgaris (see PEMPHIGUS) and DARIER DISEASE.
A process of complicated morphogenetic cell movements that reorganizes a bilayer embryo into one with three GERM LAYERS and specific orientation (dorsal/ventral; anterior/posterior). Gastrulation describes the germ layer development of a non-mammalian BLASTULA or that of a mammalian BLASTOCYST.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A sequential pattern of amino acids occurring more than once in the same protein sequence.
Microscopy in which the samples are first stained immunocytochemically and then examined using an electron microscope. Immunoelectron microscopy is used extensively in diagnostic virology as part of very sensitive immunoassays.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The process by which cells convert mechanical stimuli into a chemical response. It can occur in both cells specialized for sensing mechanical cues such as MECHANORECEPTORS, and in parenchymal cells whose primary function is not mechanosensory.
A MARVEL domain-containing protein found in the presynaptic vesicles of NEURONS and NEUROENDOCRINE CELLS. It is commonly used as an immunocytochemical marker for neuroendocrine differentiation.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
Photographic techniques used in ORTHODONTICS; DENTAL ESTHETICS; and patient education.
Money owed to creditors outside of a country.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The developmental entity of a fertilized egg (ZYGOTE) in animal species other than MAMMALS. For chickens, use CHICK EMBRYO.
A member of the Rho family of MONOMERIC GTP-BINDING PROTEINS. It is associated with a diverse array of cellular functions including cytoskeletal changes, filopodia formation and transport through the GOLGI APPARATUS. This enzyme was formerly listed as EC 3.6.1.47.
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
Cytoplasmic filaments intermediate in diameter (about 10 nanometers) between the microfilaments and the microtubules. They may be composed of any of a number of different proteins and form a ring around the cell nucleus.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.

Explanations for the clinical and microscopic localization of lesions in pemphigus foliaceus and vulgaris. (1/6757)

Patients with pemphigus foliaceus (PF) have blisters on skin, but not mucous membranes, whereas patients with pemphigus vulgaris (PV) develop blisters on mucous membranes and/or skin. PF and PV blisters are due to loss of keratinocyte cell-cell adhesion in the superficial and deep epidermis, respectively. PF autoantibodies are directed against desmoglein (Dsg) 1; PV autoantibodies bind Dsg3 or both Dsg3 and Dsg1. In this study, we test the hypothesis that coexpression of Dsg1 and Dsg3 in keratinocytes protects against pathology due to antibody-induced dysfunction of either one alone. Using passive transfer of pemphigus IgG to normal and DSG3(null) neonatal mice, we show that in the areas of epidermis and mucous membrane that coexpress Dsg1 and Dsg3, antibodies against either desmoglein alone do not cause spontaneous blisters, but antibodies against both do. In areas (such as superficial epidermis of normal mice) where Dsg1 without Dsg3 is expressed, anti-Dsg1 antibodies alone can cause blisters. Thus, the anti-desmoglein antibody profiles in pemphigus sera and the normal tissue distributions of Dsg1 and Dsg3 determine the sites of blister formation. These studies suggest that pemphigus autoantibodies inhibit the adhesive function of desmoglein proteins, and demonstrate that either Dsg1 or Dsg3 alone is sufficient to maintain keratinocyte adhesion.  (+info)

p27 is involved in N-cadherin-mediated contact inhibition of cell growth and S-phase entry. (2/6757)

In this study the direct involvement of cadherins in adhesion-mediated growth inhibition was investigated. It is shown here that overexpression of N-cadherin in CHO cells significantly suppresses their growth rate. Interaction of these cells and two additional fibroblastic lines with synthetic beads coated with N-cadherin ligands (recombinant N-cadherin ectodomain or specific antibodies) leads to growth arrest at the G1 phase of the cell cycle. The cadherin-reactive beads inhibit the entry into S phase and the reduction in the levels of cyclin-dependent kinase (cdk) inhibitors p21 and p27, following serum-stimulation of starved cells. In exponentially growing cells these beads induce G1 arrest accompanied by elevation in p27 only. We propose that cadherin-mediated signaling is involved in contact inhibition of growth by inducing cell cycle arrest at the G1 phase and elevation of p27 levels.  (+info)

Tracing cellular and molecular mechanisms involved in endometriosis. (3/6757)

The aetiology and pathogenesis of endometriosis, defined as the presence of endometrium-like tissue outside the uterine cavity, is largely unknown. In this paper we present and discuss possibilities to study the putative pathogenic properties of endometriotic cells in vitro. The current focus of our investigations is on the invasive phenotype of the disease, assuming that this might contribute to the pathogenesis of endometriosis. So far, we have shown that: (i) cytokeratin-positive and E-cadherin-negative endometriotic cells have an invasive phenotype in a collagen invasion assay in vitro similar to metastatic carcinoma cells; (ii) the invasiveness of endometriotic but not of eutopic endometrial cells can be stimulated by a heat-stable protein present in peritoneal fluid; and (iii) the endometriotic cell line EEC145T, which we established, may be a useful tool for the identification of gene products which are, positively or negatively, invasion-related. Finally, our studies suggest that the invasive phenotype in endometriosis shares aspects with tumour metastasis, but might also have unique mechanisms.  (+info)

Cadherin-11 is expressed in invasive breast cancer cell lines. (4/6757)

In several cancers, including breast cancer, loss of E-cadherin expression is correlated with a loss of the epithelial phenotype and with a gain of invasiveness. Cells that have lost E-cadherin expression are either poorly invasive with a rounded phenotype, or highly invasive, with a mesenchymal phenotype. Most cells lacking E-cadherin still retain weak calcium-dependent adhesion, indicating the presence of another cadherin family member. We have now examined the expression of the mesenchymal cadherin, cadherin-11, in breast cancer cell lines. Cadherin-11 mRNA and protein, as well as a variant form, are expressed in the most invasive cell lines but not in any of the noninvasive cell lines. Cadherin-11 is localized to a detergent-soluble pool and is associated with both alpha- and beta-catenin. Immunocytochemistry shows that cadherin-11 is localized to the cell membrane at sites of cell-cell contact as well as at lamellipodia-like projections, which do not interact with other cells. These results suggest that cadherin-11 expression may be well correlated with the invasive phenotype in cancer cells and may serve as a molecular marker for the more aggressive, invasive subset of tumors. Cadherin-11 may mediate the interaction between malignant tumor cells and other cell types that normally express cadherin-11, such as stromal cells or osteoblasts or perhaps even with the surrounding extracellular matrix, thus facilitating tumor cell invasion and metastasis.  (+info)

Coupling assembly of the E-cadherin/beta-catenin complex to efficient endoplasmic reticulum exit and basal-lateral membrane targeting of E-cadherin in polarized MDCK cells. (5/6757)

The E-cadherin/catenin complex regulates Ca++-dependent cell-cell adhesion and is localized to the basal-lateral membrane of polarized epithelial cells. Little is known about mechanisms of complex assembly or intracellular trafficking, or how these processes might ultimately regulate adhesion functions of the complex at the cell surface. The cytoplasmic domain of E-cadherin contains two putative basal-lateral sorting motifs, which are homologous to sorting signals in the low density lipoprotein receptor, but an alanine scan across tyrosine residues in these motifs did not affect the fidelity of newly synthesized E-cadherin delivery to the basal-lateral membrane of MDCK cells. Nevertheless, sorting signals are located in the cytoplasmic domain since a chimeric protein (GP2CAD1), comprising the extracellular domain of GP2 (an apical membrane protein) and the transmembrane and cytoplasmic domains of E-cadherin, was efficiently and specifically delivered to the basal-lateral membrane. Systematic deletion and recombination of specific regions of the cytoplasmic domain of GP2CAD1 resulted in delivery of <10% of these newly synthesized proteins to both apical and basal-lateral membrane domains. Significantly, >90% of each mutant protein was retained in the ER. None of these mutants formed a strong interaction with beta-catenin, which normally occurs shortly after E-cadherin synthesis. In addition, a simple deletion mutation of E-cadherin that lacks beta-catenin binding is also localized intracellularly. Thus, beta-catenin binding to the whole cytoplasmic domain of E-cadherin correlates with efficient and targeted delivery of E-cadherin to the lateral plasma membrane. In this capacity, we suggest that beta-catenin acts as a chauffeur, to facilitate transport of E-cadherin out of the ER and the plasma membrane.  (+info)

Mutated epithelial cadherin is associated with increased tumorigenicity and loss of adhesion and of responsiveness to the motogenic trefoil factor 2 in colon carcinoma cells. (6/6757)

Epithelial (E)-cadherin and its associated cytoplasmic proteins (alpha-, beta-, and gamma-catenins) are important mediators of epithelial cell-cell adhesion and intracellular signaling. Much evidence exists suggesting a tumor/invasion suppressor role for E-cadherin, and loss of expression, as well as mutations, has been described in a number of epithelial cancers. To investigate whether E-cadherin gene (CDH1) mutations occur in colorectal cancer, we screened 49 human colon carcinoma cell lines from 43 patients by single-strand conformation polymorphism (SSCP) analysis and direct sequencing. In addition to silent changes, polymorphisms, and intronic variants in a number of the cell lines, we detected frameshift single-base deletions in repeat regions of exon 3 (codons 120 and 126) causing premature truncations at codon 216 in four replication-error-positive (RER+) cell lines (LS174T, HCT116, GP2d, and GP5d) derived from 3 patients. In LS174T such a mutation inevitably contributes to its lack of E-cadherin protein expression and function. Transfection of full-length E-cadherin cDNA into LS174T cells enhanced intercellular adhesion, induced differentiation, retarded proliferation, inhibited tumorigenicity, and restored responsiveness to the migratory effects induced by the motogenic trefoil factor 2 (human spasmolytic polypeptide). These results indicate that, although inactivating E-cadherin mutations occur relatively infrequently in colorectal cancer cell lines overall (3/43 = 7%), they are more common in cells with an RER+ phenotype (3/10 = 30%) and may contribute to the dysfunction of the E-cadherin-catenin-mediated adhesion/signaling system commonly seen in these tumors. These results also indicate that normal E-cadherin-mediated cell adhesion can restore the ability of colonic tumor cells to respond to trefoil factor 2.  (+info)

Misexpression of the catenin p120(ctn)1A perturbs Xenopus gastrulation but does not elicit Wnt-directed axis specification. (7/6757)

Modulators of cadherin function are of great interest given that the cadherin complex actively contributes to the morphogenesis of virtually all tissues. The catenin p120(ctn) (formerly p120cas) was first identified as a src- and receptor-protein tyrosine kinase substrate and later shown to interact directly with cadherins. In common with beta-catenin and plakoglobin (gamma-catenin), p120(ctn) contains a central Armadillo repeat region by which it binds cadherin cytoplasmic domains. However, little is known about the function of p120(ctn) within the cadherin complex. We examined the role of p120(ctn)1A in early vertebrate development via its exogenous expression in Xenopus. Ventral overexpression of p120(ctn)1A, in contrast to beta-catenin, did not induce the formation of duplicate axial structures resulting from the activation of the Wnt signaling pathway, nor did p120(ctn) affect mesoderm induction. Rather, dorsal misexpression of p120(ctn) specifically perturbed gastrulation. Lineage tracing of cells expressing exogenous p120(ctn) indicated that cell movements were disrupted, while in vitro studies suggested that this may have been a consequence of reduced adhesion between blastomeres. Thus, while cadherin-binding proteins beta-catenin, plakoglobin, and p120(ctn) are members of the Armadillo protein family, it is clear that these proteins have distinct biological functions in early vertebrate development. This work indicates that p120(ctn) has a role in cadherin function and that heightened expression of p120(ctn) interferes with appropriate cell-cell interactions necessary for morphogenesis.  (+info)

The expression of beta-catenin in non-small-cell lung cancer: a clinicopathological study. (8/6757)

AIMS: To investigate the expression of beta-catenin in non-small-cell lung cancer (NSCLC) and its clinical significance. METHODS: 101 patients were surgically treated for NSCLC by lobectomy or pneumectomy with systematic lymph node dissection. Follow up was available in all patients, ranging from 24 to 110 months. Immunostaining of tissue sections from primary tumours and (when present) their lymph node metastases was performed and evaluated using a monoclonal antibody against beta-catenin. Correlations were investigated between beta-catenin immunostaining in primary tumours and E-cadherin immunostaining (data available from a previous study), lymph node stage, and survival. RESULTS: There were significant correlations between scores for beta-catenin immunostaining and E-cadherin immunostaining in primary tumours (p = 0.007), and between the beta-catenin immunostaining score in primary tumours and in their lymph node metastases (p = 0.006). An inverse correlation was found between the beta-catenin immunostaining score in primary tumours and lymph node stage N0, N1, or N2 (p = 0.03). According to the Kaplan-Meier survival estimate, the level of beta-catenin expression in primary tumours was a statistically significant prognostic factor (p = 0.01). CONCLUSIONS: Reduced beta-catenin expression in surgically treated NSCLC is clearly associated with lymph node metastasis and an infavourable prognosis. The existence of a functional relation between E-cadherin and beta-catenin is supported by the results of this clinicopathological study.  (+info)

Classic cadherins are transmembrane receptors involved in cell type-specific calcium-dependent intercellular adhesion. The specificity of adhesion is mediated by homophilic interactions between cadherins extending from opposing cell surfaces. In addition, classic cadherins can self-associate forming lateral dimers. Whereas it is widely excepted that lateral dimerization of cadherins is critical for adhesion, details of this process are not known. Yet, no evidence for physical association between different classic cadherins in cells expressing complex cadherin patterns has been reported. To study lateral and adhesive intercadherin interactions, we examined interactions between two classic cadherins, E- and P-cadherins, in epithelial A-431 cells co-producing both proteins. We showed that these cells exhibited heterocomplexes consisting of laterally assembled E- and P-cadherins. These complexes were formed by a mechanism involving Trp(156) of E-cadherin. Removal of calcium ions from the culture ...
Cadherins are a family of transmembrane proteins formed from multiple repeats of cadherin-specific motif (a recurrent molecular sequence) and also share a large extracellular domain. Cadherins are classified into two groups: Classical Cadherins and Protocadherins. The main difference between the two groups of cadherins is the classical cadherins contain five cadherin repeats with the third (EC3) and the fifth (EC5) repeat having very specific features. The protocadherins do not share the same features of the EC3 and EC5 units; are longer than five repeats long; and the sequences are very similar to each other. As a result of these differences, the classical cadherins are very specific and do not adhere to a large number of different ECM proteins, whereas protocadherins are much more flexible in their attachments. Classical cadherins are known to only be found in vertebrates so far, while protocadherins are found in planaria, hydra, Drosophila, and various mammals. Cadherins rely heavily on ...
P-cadherin is a subclass of Ca2+-dependent cell-cell adhesion molecules present in mouse placenta, where its localization suggests a function of connecting the embryo to the uterus (Nose, A., and M. Takeichi. 1986. J. Cell Biol. 103:2649-2658). We recently identified a human cadherin detected by an mAb capable of disrupting cell-cell adhesion of A-431 cells, and found that it was closely related immunochemically to mouse P-cadherin. Curiously, this cadherin was undetectable in human placenta by immunohistochemical examination (Shimoyama, Y., S. Hirohashi, S. Hirano, M. Noguchi, Y. Shimosato, M. Takeichi, and O. Abe. 1989. Cancer Res. 49:2128-2133). We here report the cloning and sequencing of cDNA clone encoding the human homologue of mouse P-cadherin. The deduced amino acid sequence of the human P-cadherin consists of 829 amino acid and shows striking homology with mouse P-cadherin. On Northern blot analysis, human P-cadherin was scarcely expressed in human placenta in contrast to mouse ...
Clustered protocadherins (PCDHs) map in tandem at human chromosome 5q31 and comprise three multi-genes clusters: α-, β- and γ-PCDH. The expression of this cluster consists of a complex mechanism involving DNA hub formation through DNA-CCTC binding factor (CTCF) interaction. Methylation alterations can affect this interaction, leading to transcriptional dysregulation. In cancer, clustered PCDHs undergo a mechanism of long-range epigenetic silencing by hypermethylation. In this study, we detected frequent methylation alterations at CpG islands associated to these clustered PCDHs in all the solid tumours analysed (colorectal, gastric and biliary tract cancers, pilocytic astrocytoma), but not hematologic neoplasms such as chronic lymphocytic leukemia. Importantly, several altered CpG islands were associated with CTCF binding sites. Interestingly, our analysis revealed a hypomethylation event in pilocytic astrocytoma, suggesting that in neuronal tissue, where PCDHs are highly expressed, these genes become
Clustered protocadherins (PCDHs) map in tandem at human chromosome 5q31 and comprise three multi-genes clusters: α-, β- and γ-PCDH. The expression of this cluster consists of a complex mechanism involving DNA hub formation through DNA-CCTC binding factor (CTCF) interaction. Methylation alterations can affect this interaction, leading to transcriptional dysregulation. In cancer, clustered PCDHs undergo a mechanism of long-range epigenetic silencing by hypermethylation. In this study, we detected frequent methylation alterations at CpG islands associated to these clustered PCDHs in all the solid tumours analysed (colorectal, gastric and biliary tract cancers, pilocytic astrocytoma), but not hematologic neoplasms such as chronic lymphocytic leukemia. Importantly, several altered CpG islands were associated with CTCF binding sites. Interestingly, our analysis revealed a hypomethylation event in pilocytic astrocytoma, suggesting that in neuronal tissue, where PCDHs are highly expressed, these genes become
E-cadherin is a Ca2+-dependent cell adhesion molecule which plays an important role in normal growth and development via mediation of homotypic, homophilic cell-cell interaction. Recent studies suggest that E-cadherin may be important in neoplastic progression as well, particularly as a suppressor of invasion. We have previously demonstrated that the invasive phenotype of rat prostate cancer cells is associated with the decreased expression of E-cadherin (M. J. G. Bussemakers, R. J. A. Van Moorselaar, L. A. Giroldi, T. Ichikawa, J. T. Isaacs, F. M. J. Debruyne, and J. A. Schalken, Cancer Res., 52: 2916-2922, 1992). This is of particular interest, since the locus to which the human E-cadherin gene is mapped is frequently involved in allelic loss in prostate cancer (B. S. Carter, C. M. Ewing, W. S. Ward, B. F. Treiger, T. W. Aalders, J. A. Schalken, J. I. Epstein, and W. B. Isaacs, Proc. Natl. Acad. Sci. USA, 87: 8751-8755, 1990; U. S. Bergerheim, K. Kunimi, V. P. Collins, and P. Ekman, Genes, ...
Detachment of cell-cell adhesion is indispensable for the first step of invasion and metastasis of cancer. This mechanism is frequently associated with the impairment of either E-cadherin expression or function. However, mechanisms of such abnormalities have not been fully elucidated. In this study, we demonstrated that the function of E-cadherin was completely abolished in the human gastric cancer cell line HSC-39, despite the high expression of E-cadherin, because of mutations in one of the E-cadherin-associated cytoplasmic proteins, beta-catenin. Although immunofluorescence staining of HSC-39 cells by using an anti-E-cadherin antibody (HECD-1) revealed the strong and uniform expression of E-cadherin on the cell surface, cell compaction and cell aggregation were not observed in this cell. Western blotting (immunoblotting) using HECD-1 exhibited a 120-kDa band which is equivalent to normal E-cadherin. Northern (RNA) blotting demonstrated a 4.7-kb band, the same as mature E-cadherin mRNA. ...
TY - JOUR. T1 - Calcium-dependent dynamics of cadherin interactions at cell-cell junctions. AU - Kim, Sally A.. AU - Tai, Chin Yin. AU - Mok, Lee Peng. AU - Mosser, Eric A.. AU - Schuman, Erin M.. PY - 2011/6/14. Y1 - 2011/6/14. N2 - Cadherins play a key role in the dynamics of cell-cell contact formation and remodeling of junctions and tissues. Cadherin-cadherin interactions are gated by extracellular Ca2+, which serves to rigidify the cadherin extracellular domains and promote trans junctional interactions. Here we describe the direct visualization and quantification of spatiotemporal dynamics of N-cadherin interactions across intercellular junctions in living cells using a genetically encodable FRET reporter system. Direct measurements of transjunctional cadherin interactions revealed a sudden, but partial, loss of homophilic interactions (τ = 1.17 ± 0.06 s-1) upon chelation of extracellular Ca2+. A cadherin mutant with reduced adhesive activity (W2A) exhibited a faster, more substantial ...
Classical cadherins mediate Ca2+-dependent intercellular adhesion and are essential for tissue morphogenesis and maintenance. They are key components of adherens junctions (AJs). In vitro studies in simple epithelial cells indicated an essential role for E-cadherin not only in the formation of AJs but also other intercellular contacts, such as desmosomes and tight junctions. In contrast, in vivo tissue specific knockout studies did not reveal a necessity of E-cadherin in the formation of intercellular junctions, raising the question if classical cadherins are necessary or if other classical cadherins can compensate for the loss of E-cadherin. Therefore, the aim of this thesis was to ask how E-cadherin regulates tight junctions and if E-cadherin has a specific function in the formation of tight junctions. In addition, the question was asked if classical cadherin function is necessary for the formation of other intercellular contacts, such as desmosomes. Using primary keratinocytes as a model for ...
Loss of the epithelial adhesion molecule E-cadherin is thought to enable metastasis by disrupting intercellular contacts-an early step in metastatic dissemination. To further investigate the molecular basis of this notion, we use two methods to inhibit E-cadherin function that distinguish between E-cadherins cell-cell adhesion and intracellular signaling functions. Whereas the disruption of cell-cell contacts alone does not enable metastasis, the loss of E-cadherin protein does, through induction of an epithelial-to-mesenchymal transition, invasiveness, and anoikis resistance. We find the E-cadherin binding partner beta-catenin to be necessary, but not sufficient, for induction of these phenotypes. In addition, gene expression analysis shows that E-cadherin loss results in the induction of multiple transcription factors, at least one of which, Twist, is necessary for E-cadherin loss-induced metastasis. These findings indicate that E-cadherin loss in tumors contributes to metastatic ...
This gene is a type II classical cadherin from the cadherin superfamily and one of three cadherin 7-like genes located in a cluster on chromosome 18. The encoded membrane protein is a calcium dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. Since disturbance of intracellular adhesion is a prerequisite for invasion and metastasis of tumor cells, cadherins are considered prime candidates for tumor suppressor genes.
This gene is a type II classical cadherin from the cadherin superfamily and one of three cadherin 7-like genes located in a cluster on chromosome 18. The encoded membrane protein is a calcium dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. Since disturbance of intracellular adhesion is a prerequisite for invasion and metastasis of tumor cells, cadherins are considered prime candidates for tumor suppressor genes. [provided by RefSeq, Jul 2008 ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene is a type II classical cadherin from the cadherin superfamily and one of three cadherin 7-like genes located in a cluster on chromosome 18. The encoded membrane protein is a calcium dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. Since disturbance of intracellular adhesion is a prerequisite for invasion and metastasis of tumor cells, cadherins are considered prime candidates for tumor suppressor genes. [provided by RefSeq, Jul 2008 ...
This gene encodes a classical cadherin of the cadherin superfamily. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate the mature glycoprotein. This calcium-dependent cell-cell adhesion protein is comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. This gene is located in a gene cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. In addition, aberrant expression of this protein is observed in cervical adenocarcinomas. Mutations in this gene are associated with hypotrichosis with juvenile macular dystrophy and ectodermal dysplasia, ectrodactyly, and macular dystrophy syndrome (EEMS). [provided by RefSeq, Nov 2015 ...
Because AQP3 but not AQP5 was delivered to cell-cell contacts, we directly tested whether a targeting patch specific for basolateral vesicles is assembled upon E-cadherin-mediated cell-cell adhesion. Our data indicate that microtubules, the exocyst, and t-SNAREs are essential components of this lateral targeting patch. We showed that the exocyst and the t-SNARE syntaxin 4 colocalized with E-cadherin at early cell-cell contacts, and it has been shown by others that microtubule plus ends extend radially into cell-cell contacts (Stehbens et al., 2006; Shaw et al., 2007). Functional disruption of any one of these components did not interfere with the establishment of cell-cell adhesion or the localization of other components to cell-cell contact. Because there is a large amount of E-cadherin on the cell surface before cell adhesion (Adams et al. 1998), it is therefore likely that initial cell-cell adhesion does not require the delivery of E-cadherin from intracellular compartments. However, ...
One of the genes in our body is called CDH1. It is located on chromosome 16, and when it is functioning properly it provides instructions for our cells to make the e-cadherin protein, and allows cells to adhere to one another in an orderly manner. A pathogenic variant in this gene interferes with the normal function of the e-cadherin protein and can result in cancer. Another gene, CTNNA1, is found on chromosome 5 and has a similar function to the CDH1 gene.. Hereditary Diffuse Gastric Cancer syndrome (HDGC) is defined by the presence of a pathogenic germline CDH1 or CTNNA1 variant in an individual with diffuse gastric cancer (DGC) or in a family with one or more DGC cases in first or second degree relatives.. Hereditary Lobular Breast Cancer (HLBC) is defined by the presence of a pathogenic germline CDH1 variant in an individual with lobular breast cancer (LBC) or in a family with one or more LBC cases in first or second degree relatives, having no known DGC in either situation. If someone in an ...
Cadherin cell adhesion molecules play crucial tasks in vertebrate development including the development of the retina. of embryonic zebrafish resulted in similar eye problems. Our results suggest that protocadherin-17 plays an important part in the normal formation of the zebrafish retina. ((MO (MOs sequences showed no significant similarities to any sequences (using BLAST) other than zebrafish (GenBank accession quantity: XM 684743). MOs were microinjected into one- to four-cell stage embryos (1.5-3 ng/embryo) in Daneau buffer (58 mM NaCl, 0.7 mM KCl, 0.4 mM MgSO4, 0.6 mM Ca(NO3)2, 5.0 mM HEPES pH 7.6). The zebrafish coding region was amplified with primers comprising EcoRI (5) and XbaI (3) restriction sites and cloned 1st into pCR2.1-TOPO vector (Existence Systems, Carlsbad, CA), followed by cloning into pCS2+MT vector (Dr. Pamela Raymond, the University of Michigan). The pCS2+MT/pcdh17 was verified by restriction digestion and sequencing (Macrogen, Rockville, MD). Capped mRNA was synthesized ...
Advisor: Andrés J. García, PhD (Georgia Institute of Technology). Committee: Thomas H. Barker, PhD (Georgia Institute of Technology). Andrew P. Kowalczyk, PhD (Emory University). Susan N. Thomas, PhD (Georgia Institute of Technology). Cheng Zhu, PhD (Georgia Institute of Technology). Quantitative Analyses for Cadherin-Based Cell-Cell Adhesive Force. Cell adhesion is a critical determinant of tissue architecture and tissue organization. Cadherin proteins mediate cell-cell adhesion in a calcium-dependent manner. The functional roles for cadherin proteins early in development and in adults, as well as the multiple disease phenotypes resulting from cadherin dysregulation, underscore the importance of cadherin proteins. Quantitative assessment of cadherin interaction structure, force, and interaction dynamics is not yet completely understood because of lack of experimental platforms to study cadherin proteins as well as their often-conflicting roles in a tissue-specific manner. Adhesive force ...
This gene encodes a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Mature cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small, highly conserved C-terminal cytoplasmic domain. The extracellular domain consists of 5 subdomains, each containing a cadherin motif, and appears to determine the specificity of the proteins homophilic cell adhesion activity. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. This particular cadherin is expressed in brain and is putatively involved in synaptic adhesion, axon outgrowth and guidance.[7] ...
Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation [ (PUBMED:3061804) ]. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the binding that it is mediated by cadherins is the juxtamembrane region of the cadherin. This region induces clustering and also binds to the protein p120ctn [ (PUBMED:9566976) ]. The cytoplasmic region is highly conserved in sequence and has been shown experimentally to regulate the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton [ (PUBMED:3061804) ]. This domain is found upstream of the cadherin domain IPR002126 . ...
My work examines the role of a conserved tryptophan residue, Trp2, in the adhesive domain of cadherins that has been shown to be essential for their adhesive function. Structural studies have shown Trp2 to be integrated into its own cadherin domain, integrated into the domain an opposing cadherin molecule, or freed from the domain and exposed to solvent. Until now, the physiological relevance of these structures has been controversial. Using conformation specific antibodies I show that Trp2 integrates into the domain fold of its own cadherin molecule in physiological conditions, but that this integration is not stable owing to structural constraints imposed by calcium binding to the cadherin. This raises the possibility that Trp2 could participate in intermolecular interactions during adhesion by inserting into opposing cadherins in what is referred to as the strand exchange model of cadherin adhesion. This model is tested directly by introducing cysteine substitutions into opposing cadherins ...
Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
p,The hair-cell tip link, a fine filament directly conveying force to mechanosensitive transduction channels, is composed of two proteins, protocadherin-15 and cadherin-23, whose mutation causes deafness. However, their molecular structure, elasticity, and deafness-related structural defects are unknown. We present crystal structures of the first and second extracellular cadherin repeats of cadherin-23. Overall, structures show typical cadherin folds, but reveal an elongated N terminus that precludes classical cadherin interactions and contributes to an N-terminal Ca(2+)-binding site. The deafness mutation D101G, in the linker region between the repeats, causes a slight bend between repeats and decreases Ca(2+) affinity. Molecular dynamics simulations suggest that cadherin-23 repeats are stiff and that either removing Ca(2+) or mutating Ca(2+)-binding residues reduces rigidity and unfolding strength. The structures define an uncharacterized cadherin family and, with simulations, suggest ...
Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the cadherin-mediated adhesion may be by the juxtamembrane region in cadherins. This region induces clus
Sideridou M, Zakopoulou R, Evangelou K, Liontos M, Kotsinas A, Rampakakis E, Gagos S, Kahata K, Grabusic K, Gkouskou K, Trougakos IP, Kolettas E, Georgakilas AG, Volarevic S, Eliopoulos AG, Zannis-Hadjopoulos M, Moustakas A, Gorgoulis VG J. Cell Biol. 195 (7) 1123-1140 [2011-12-26; online 2011-12-28] E-cadherin (CDH1) loss occurs frequently in carcinogenesis, contributing to invasion and metastasis. We observed that mouse and human epithelial cell lines overexpressing the replication licensing factor Cdc6 underwent phenotypic changes with mesenchymal features and loss of E-cadherin. Analysis in various types of human cancer revealed a strong correlation between increased Cdc6 expression and reduced E-cadherin levels. Prompted by these findings, we discovered that Cdc6 repressed CDH1 transcription by binding to the E-boxes of its promoter, leading to dissociation of the chromosomal insulator CTCF, displacement of the histone variant H2A.Z, and promoter heterochromatinization. Mutational analysis ...
TY - JOUR. T1 - Similarities between heterophilic and homophilic cadherin adhesion. AU - Prakasam, A. K.. AU - Maruthamuthu, V.. AU - Leckband, D. E.. PY - 2006/10/17. Y1 - 2006/10/17. N2 - The mechanism that drives the segregation of cells into tissue-specific subpopulations during development is largely attributed to differences in intercellular adhesion. This process requires the cadherin family of calcium-dependent glycoproteins. A widely held view is that protein-level discrimination between different cadherins on cell surfaces drives this sorting process. Despite this postulated molecular selectivity, adhesion selectivity has not been quantitatively verified at the protein level. In this work, molecular force measurements and bead aggregation assays tested whether differences in cadherin bond strengths could account for cell sorting in vivo and in vitro. Studies were conducted with chicken N-cadherin, canine E-cadherin, and Xenopus C-cadherin. Both qualitative bead aggregation and ...
TY - JOUR. T1 - Expression of cadherins and catenins in paired tumor and non-neoplastic primary prostate cultures and corresponding prostatectomy specimens. AU - Wang, J.. AU - Krill, D.. AU - Torbenson, Michael. AU - Wang, Q.. AU - Bisceglia, M.. AU - Stoner, J.. AU - Thomas, A.. AU - DeFlavia, P.. AU - Dhir, R.. AU - Becich, M. J.. PY - 2000/1/1. Y1 - 2000/1/1. N2 - Cadherins are a family of transmembrane proteins that play a crucial role in cell differentiation, cell migration, and intercellular adhesion. Cadherins are associated with catenins through their highly conserved cytoplasmic domain. Down-regulation of E-cadherin protein has been shown in various human cancers. This study examined the expression of cadherins and associated catenins at the mRNA level. Paired tumor and non-neoplastic primary prostate cultures were obtained from surgical specimens. Quantitative multiplex fluorescence reverse transcriptase-polymerase chain reaction (QMF RT-PCR) and quantitative analysis were performed ...
We show in this paper that this can indeed occur, in a cell culture system in which Wg signaling can be controlled and its response be measured over time. We found two contrasting effects: Wg initially lowers the amount of the cadherin-catenin complex at cell-cell contacts, most probably by reducing the Arm pool interacting with E-cadherin, but later, Wg signaling leads to elevated DE-cadherin transcription. This later increase in DE cadherin may titrate the pool of Arm available for Wg signaling and therefore attenuate the transcriptional response to Wg. We have shown by metabolic labeling experiments that the reduction in E-cadherin levels was caused by a posttranscriptional mechanism that affected the stability of the E-cadherin protein. Although levels of E-cadherin precursors were similar in the absence or presence of Wg signaling, very little mature E-cadherin was detectable in cells with an activated Wg pathway, indicating that the majority of E-cadherin was either degraded before arrival ...
E-Cadherin is calcium-dependent cell adhesion molecule encoded by CDH1 gene at chromosome 16q22.1. Ecadherin regulates cell-cell adhesions and controls mobility and proli..
E-cadherin (epithelial cadherin, CDH1, OMIM# 192090) is a member of the cadherin family of adhesion molecules, which are transmembrane glycoproteins mediating calcium-dependent cell-cell adhesion1. Germline mutations in the CDH1 gene have been demonstrated to underlie in diffuse gastric cancer (DGC) in various ethnic backgrounds 2, 3, 4. CDH1 germ line mutations have also been identified in a small portion of early onset DGC patients without a family history 5, 6, 12. Associations between CDH1 germ line mutations and both lobular breast cancer and signet ring carcinoma of the colon have been reported in DGC families 7, 8, 9. DGC is a highly penetrant autosomal dominant disorder that has been reported to occur in many ethnicities. The offspring of an affected individual has a 50% risk of also being affected. The estimated cumulative risk of gastric cancer by age 80 years is 67% (95% CI: 39-99) for men and 83% (95% CI: 58-99) for women10. Women also have a 39% risk for lobular breast cancer10. ...
Our laboratory is interested in understanding fundamental mechanisms of transcription and RNA splicing in the nervous system, and how these mechanisms bear on neuronal connectivity and neurodegenerative diseases. Interest in neuronal connectivity arose from our discovery of a remarkable organization of a large cluster of genes encoding cell surface cadherin-like proteins called protocadherins. This unusual gene organization leads to the generation of enormous individual cell surface diversity at the synapse through a mechanism that involves stochastic promoter choice and alternative RNA splicing. We are studying the detailed mechanisms of promoter choice, and are using gene knock out methods to investigate the function of protocadherins. We are also using embryonic stem cell differentiation and deep sequencing methods to study transcription, RNA splicing, protein-RNA interactions, and microRNAs in ALS disease models. This involves studies of SOD1, FUS and TDP43 mouse models, and human patient ...
This gene is a member of the protocadherin family, which represents a subset of the larger cadherin superfamily. The members of the protocadherin family encode non-classical cadherins that function as calcium-dependent cell-cell adhesion molecules. This protocadherin represents a new candidate for tumor suppression. Alternatively spliced transcript variants that encode the same protein have been identified.
Our results show that NFPC and TAF1 are expressed in RGCs and that inhibition of either NFPC or TAF1 function in vivo severely impairs axon and dendrite extension. These findings, together with recent reports showing that γ-protocadherins regulate synaptic development in spinal cord neurons (Weiner et al., 2005), and OL-protocadherin controls striatal axon elongation in the ventral telencephalon (Uemura et al., 2007), implicate protocadherins as general players in axonogenesis and dendritogenesis.. Although it is apparent that NFPC plays an integral role in RGC axon and dendrite elongation, its precise function at the level of the growth cone is unclear. NFPC was first identified as a regulator of embryonic ectodermal formation in Xenopus. In vivo inhibition of NFPC with NFΔE resulted in a failure of the nascent ectodermal layers to juxtapose, indicating a failure of adhesion in those NFΔE-expressing regions (Bradley et al., 1998). NFPC has also been implicated in the regulation of neural ...
Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.
Title:Cadherins: The Superfamily Critically Involved in Breast Cancer. VOLUME: 22 ISSUE: 5. Author(s):Maeirah Afzal Ashaie and Ezharul Hoque Chowdhury. Affiliation:Faculty of Medicine, Nursing and Health Sciences, Monash University, Australia.. Keywords:Breast cancer, cell adhesion, cadherins, CDH1, CDH2, epigenetic silencing, EMT, tumor repressor, transcriptional factors, signaling pathways.. Abstract:Breast cancer, one of the leading causes of mortality and morbidity among females, is regulated in part by diverse classes of adhesion molecules one of which is known as cadherins. Located at adherens junctions, the members of this superfamily are responsible for upholding proper cell-cell adhesion. Cadherins possess diverse structures and functions and any alteration in their structures or functions causes impeding of normal mammary cells development and maintenance, thus leading to breast malignancy. E-, N-, P-, VE-, Proto-, desmosomal and FAT cadherins have been found to regulate breast cancer ...
Epithelial (E)-cadherin and its associated cytoplasmic proteins (alpha-, beta-, and gamma-catenins) are important mediators of epithelial cell-cell adhesion and intracellular signaling. Much evidence exists suggesting a tumor/invasion suppressor role for E-cadherin, and loss of expression, as well as mutations, has been described in a number of epithelial cancers. To investigate whether E-cadherin gene (CDH1) mutations occur in colorectal cancer, we screened 49 human colon carcinoma cell lines from 43 patients by single-strand conformation polymorphism (SSCP) analysis and direct sequencing. In addition to silent changes, polymorphisms, and intronic variants in a number of the cell lines, we detected frameshift single-base deletions in repeat regions of exon 3 (codons 120 and 126) causing premature truncations at codon 216 in four replication-error-positive (RER+) cell lines (LS174T, HCT116, GP2d, and GP5d) derived from 3 patients. In LS174T such a mutation inevitably contributes to its lack of E
It has long been known that cell-cell adhesiveness is generally reduced in human cancers. Tumor cells are dissociated throughout the entire tumor masses of diffuse-type cancers, whereas those of solid tumors with high metastatic potentials are often focally dissociated or dedifferentiated at the inv …
E-cadherin interacts with other E-cadherin molecules on neighboring cells to form cell-cell adhesions. E-cadherin that is not involved in these trans interactions is removed from the cell surface and replaced with newly synthesized molecules to maintain dynamic adhesions. Now, Izumi et al. (page 237) show that E-cadherins that are involved in trans interactions are excused from this endocytosis by small GTPases. Disruption of this system may free cells for migration.. By reconstituting endocytosis in membrane bilayers, the group shows that clathrin-dependent endocytosis removes E-cadherin that is not interacting in trans with other E-cadherins. E-cadherins engaged in trans interactions, however, activated Rac and Cdc42, which blocked their internalization. So far it is unclear how the trans interactions activate the G proteins.. The endocytic block is enhanced by IQGAP1, an effector of Rac and Cdc42. IQGAP1 cross-links actin filaments into bundles, and the group shows that F-actin is needed to ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene is a member of the cadherin superfamily whose members encode calcium-dependent cell-cell adhesion molecules. The encoded protein has a signal peptide, 27 cadherin repeat domains and a unique cytoplasmic region. This particular cadherin family member is expressed in fibroblasts but not in melanocytes or keratinocytes. The cell-cell adhesion of fibroblasts is thought to be necessary for wound healing. [provided by RefSeq, Jul 2008 ...
Known proteins from the cell-adhesion protein E-cadherin include proteins and catenins involved with signaling trafficking and actin organization. catenins and almost 40 others that were previously reported to influence cadherin function. Many others could be rationalized as novel candidates for regulating the adherens junction Isovitexin cytoskeleton trafficking or signaling. We further characterized lipoma desired partner (LPP) which is present at both cell contacts and focal adhesions. Knockdown of LPP shown its requirement for E-cadherin-dependent adhesion and suggested that it plays a role in coordination of the cell-cell and cell-substrate cytoskeletal relationships. The analysis of LPP function demonstrates proof of principle the proteomic analysis of E-cadherin proximal proteins expands the inventory of parts and tools for understanding the function of E-cadherin. proximity ligation assay (PLA); this assay results in the production of a fluorescent transmission when antibodies to two ...
TY - JOUR. T1 - Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion. AU - Yamada, Soichiro. AU - Nelson, W. James. PY - 2007/7/30. Y1 - 2007/7/30. N2 - Spatiotemporal coordination of cell-cell adhesion involving lamellipodial interactions, cadherin engagement, and the lateral expansion of the contact is poorly understood. Using high-resolution live-cell imaging, biosensors, and small molecule inhibitors, we investigate how Rac1 and RhoA regulate actin dynamics during de novo contact formation between pairs of epithelial cells. Active Rac1, the Arp2/3 complex, and lamellipodia are initially localized to de novo contacts but rapidly diminish as E-cadherin accumulates; further rounds of activation and down-regulation of Rac1 and Arp2/3 occur at the contacting membrane periphery, and this cycle repeats as a restricted membrane zone that moves outward with the expanding contact. The cortical bundle of actin filaments dissolves beneath the ...
This gene encodes a member of the protocadherin family, and cadherin superfamily, of transmembrane proteins containing cadherin domains. These proteins mediate cell adhesion in neural tissues in the presence of calcium. The encoded protein may be involved in signaling at neuronal synaptic junctions. Sharing a characteristic with other protocadherin genes, this gene has a notably large exon that encodes multiple cadherin domains and a transmembrane region. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Nov 2012 ...
Several events during the normal development of the mammalian neocortex depend on N-cadherin, including the radial migration of immature projection neurons into the cortical plate. Remarkably, radial migration requires the N-cadherin extracellular domain but not N-cadherin-dependent homophilic cell-cell adhesion, suggesting that other N-cadherin-binding proteins may be involved. We used proximity ligation and affinity purification proteomics to identify N-cadherin-binding proteins. Both screens detected MycBP2 and SPRY domain protein Fbxo45, two components of an intracellular E3 ubiquitin ligase. Fbxo45 appears to be secreted by a nonclassical mechanism, not involving a signal peptide and not requiring transport from the endoplasmic reticulum to the Golgi apparatus. Fbxo45 binding requires N-cadherin SPRY motifs that are not involved in cell-cell adhesion. SPRY mutant N-cadherin does not support radial migration in vivo. Radial migration was similarly inhibited when Fbxo45 expression was ...
Cadherins are a family of glycoproteins involved in the Ca2+-dependent cell-cell adhesion mechanism which is detected in most kinds of tissues. Inhibition of the cadherin activity with antibodies induces dissociation of cell layers, indicating a fundamental importance of these molecules in maintaining the multicellular structure. Cadherins are divided into subclasses, including E-, N- and P-cadherins. While all subclasses are similar in molecular weight, Ca2+- and protease-sensitivity, each subclass is characterized by a unique tissue distribution pattern and immunological specificity. Analysis of amino acid sequences deduced from cDNA encoding these molecules showed that they are integral membrane proteins of 723-748 amino acids long and share common sequences; similarity in the sequences between subclasses is in a range of 50-60% when compared within a single animal species. L cells, with very little endogenous cadherin activity, transfected with the cadherin cDNA acquired high ...
TY - JOUR. T1 - Ras farnesylation inhibitor FTI-277 restores the E-cadherin/catenin cell adhesion system in human cancer cells and reduces cancer metastasis. AU - Nam, Jeong Seok. AU - Ino, Yoshinori. AU - Sakamoto, Michiie. AU - Hirohashi, Setsuo. PY - 2002/9/1. Y1 - 2002/9/1. N2 - The E-cadherin/catenin cell adhesion system is often down-regulated in epithelial tumors. This is thought to play an important role in cancer invasion and metastasis, and restoration of this system may suppress metastatic spread of cancer. In this study, the effects of a Ras farnesylation inhibitor (FTI-277) on E-cadherin-mediated cell-cell adhesion and metastatic potential were examined. In cell aggregation assays, FTI-277 stimulated aggregation of colon, liver and breast cancer cells. In vitro cultures of cancer cells showed that FTI-277 induced strong cell-cell contact. Immunoblotting analysis showed that FTI-277 increased E-cadherin/catenin (α, β and γ) expression and strongly stabilized E-cadherin/catenin ...
Objective: The present study aimed to investigate the possible role of IL-6 and 1α,25-dihydroxyvitamin D3 (1,25D)signaling in epithelial-mesenchymal transition (EMT) and stemness in triple-negative breast cancer (TNBC) cell line.Methods: TNBC cell line, HCC 1806, was treated with IL-6 and 1,25D for three and six days. Also, the role of vitaminD receptor (VDR) was studied by transfection of TNBC cell line with VDR gene and transfection efficiency was assessedusing Human VDR enzyme-linked immunosorbent assay (ELISA). Changes in E-cadherin gene expression wereanalyzed by quantitative real-time PCR (qRT-PCR). Also, changes in CD44+ cells were analyzed by flow cytometry.Finally, morphological changes were investigated by light microscopy after 6 days. Results: Treatment of HCC1806cells with IL-6 has no significant effect either on E-cadherin gene expression or CD44+ cells, (p | 0.05). However,E-cadherin gene expression was significantly up-regulated after treatment with 1,25D for 6 days, (p | 0.05). Also,
TY - JOUR. T1 - E-cadherin germline mutations define an inherited cancer syndrome dominated by diffuse gastric cancer. AU - Guilford, Parry J.. AU - Hopkins, Justin B.W.. AU - Grady, William M.. AU - Markowitz, Sanford D.. AU - Willis, Joseph. AU - Lynch, Henry. AU - Rajput, Ashwani. AU - Wiesner, Georgia L.. AU - Lindor, Noralane M.. AU - Burgart, Lawrence J.. AU - Toro, Tumi T.. AU - Lee, Don. AU - Limacher, Jean Marc. AU - Shaw, David W.. AU - Findlay, Michael P.N.. AU - Reeve, Anthony E.. N1 - Copyright: Copyright 2007 Elsevier B.V., All rights reserved.. PY - 1999. Y1 - 1999. N2 - To extend earlier observations of germline E-cadherin mutations in kindreds with an inherited susceptibility to diffuse gastric cancer, we searched for germline E-cadherin mutations in five further families affected predominantly by diffuse gastric cancer and one family with a history of diffuse gastric cancer and early-onset breast cancer. Heterozygous inactivating mutations were found in the E-cadherin gene in ...
TY - JOUR. T1 - Effects of non-protein-type amino acids of fine particulate matter on E-cadherin and inflammatory responses in mice. AU - Chuang, Hsiao Chi. AU - Ho, Kin Fai. AU - Cao, Jun Ji. AU - Chuang, Kai Jen. AU - Ho, Steven Sai Hang. AU - Feng, Po Hao. AU - Tian, Linwei. AU - Lee, Chii Hong. AU - Han, Yong Ming. AU - Lee, Chun-Nin. AU - Cheng, Tsun Jen. PY - 2015/9/7. Y1 - 2015/9/7. N2 - Exposure to particulate matter less than 2.5μm (PM2.5) in size is an urgent issue for the protection of human health. Chemicals with PM2.5 collected during a period of intensive haze episodes in Beijing (BJ), Xian (XA) and Hong Kong (HK) were characterised for organic carbon (OC), elemental carbon (EC), total carbon (TC) and free amino acids. BALB/c mice underwent aspiration exposure of 50 or 150μg of PM2.5/mouse (BJ, XA and HK) on days 1 and 7 and were euthanised on day 14. The effects of these exposures on E-cadherin and inflammatory responses in the mouse lungs were analysed. The PM2.5 chemicals ...
Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells. The first two catenins that were identified became known as α-catenin and β-catenin. A-catenin can bind to β-catenin and can also bind actin. B-catenin binds the cytoplasmic domain of some cadherins. Additional catenins such as γ-catenin and δ-catenin have been identified. The name catenin was originally selected (catena means chain in Latin) because it was suspected that catenins might link cadherins to the cytoskeleton. α-catenin β-catenin δ-catenin γ-catenin All but α-catenin contain armadillo repeats. Several types of catenins work with N-cadherins to play an important role in learning and memory (For full article, see Cadherin-catenin complex in learning and memory). Cell-cell adhesion complexes are required for simple epithelia in higher organisms to maintain structure, function and polarity. These complexes, which help regulate cell growth in addition to creating and ...
E-CADHERIN MEDIATED HOMOTYPIC CELL-CELL INTERACTION CONFERS CYTOKINE INDEPENDENCE IN HUMAN LEUKEMIA UT-7 CELL LINE A Thesis by SIRISHA CHAKKAPALLI Submitted to the Office of Graduate Studies of Texas A&M University-Commerce in partial fulfillment of the requirements For the degree of MASTERS OF SCIENCE December 2017E-CADHERIN MEDIATED HOMOTYPIC CELL-CELL INTERACTION CONFERS CYTOKINE INDEPENDENCE IN HUMAN LEUKEMIA UT-7 CELL LINE A Thesis by SIRISHA CHAKKAPALLI Approved by: Advisor: Venu Cheriyath Committee Members: Larry Lemanski Izhar Khan Head of the Department: Judith Ball Dean of the College: Brent L. Donham Interim Dean of Graduate Studies: Mary Beth Sampsoniii Copyright © 2017 Sirisha Chakkapalli iv ABSTRACT E-CADHERIN MEDIATED HOMOTYPIC CELL-CELL INTERACTION CONFERS CYTOKINE INDEPENDENCE IN HUMAN LEUKEMIA UT-7 CELL LINE Sirisha Chakkapalli, MS Texas A&M University-Commerce, 2017 Advisor: Venugopalan Cheriyath.PhD Acute myeloid leukemia (AML) is an aggressive hematopoietic stem cell cancer ...
Looking for online definition of OB-cadherin in the Medical Dictionary? OB-cadherin explanation free. What is OB-cadherin? Meaning of OB-cadherin medical term. What does OB-cadherin mean?
Epithelial-mesenchymal transition is an important mechanism in cancer invasiveness and metastasis. We had previously reported that cancer cells expressing Epstein-Barr virus (EBV) latent viral antigens EBV nuclear antigen EBNA3C and/ or EBNA1 showed higher motility and migration potential and had a propensity for increased metastases when tested in nude mice model. We now show that both EBNA3C and EBNA1 can modulate cellular pathways critical for epithelial to mesenchymal transition of cancer cells. Our data confirms that presence of EBNA3C or EBNA1 result in upregulation of transcriptional repressor Slug and Snail, upregulation of intermediate filament of mesenchymal origin vimentin, upregulation of transcription factor TCF8/ZEB1, downregulation as well as disruption of tight junction zona occludens protein ZO-1, downregulation of cell adhesion molecule E-cadherin, and nuclear translocation of β-catenin. We further show that the primary tumors as well as metastasized lesions derived from EBV ...
OBJECTIVE: E-cadherin is a potent adherens junction molecule implicated in tissue morphogenesis, epithelial functioning, and immune regulation. Serum levels of soluble E-cadherin (sE-cadherin), an end product of proteolytic cleavage of E-cadherin, is increased in patients with cancer, infections, and inflammation-related diseases. The aim of our study was to measure serum levels of sE-cadherin in systemic lupus erythematosus (SLE) and to determine associations between serum levels of sE-cadherin and markers of inflammation and organ damage in female patients with SLE.. METHODS: Serum levels of sE-cadherin were analyzed by ELISA in 150 female patients with SLE and 31 healthy women. Simple and multiple regression analyses between sE-cadherin levels and disease-related variables were performed in patients with SLE.. RESULTS: Serum levels of sE-cadherin were elevated in patients with SLE compared with levels in healthy controls. sE-cadherin levels correlated positively with age, disease duration, ...
A previous study showed E-cadherin expression was lost in some cervical cancer cell lines and tumours. This study was designed to clarify the significance of DNA methylation in silencing E-cadherin expression. We examined promoter methylation of E-cadherin in five cervical cancer cell lines and 20 cervical cancer tissues using methylation-specific PCR (MSP) and bisulphite DNA sequencing. The correlation of E-cadherin methylation and expression together with methyltransferase (DNMT1) were further studied. We found that hypermethylation of E-cadherin was involved in five cervical cancer cell lines and 40% (8/20) of cervical cancer tissues. E-cadherin protein was lost in 6/8 (75%) samples and 3/5 (60%) cell lines with promoter methylation. E-cadherin methylation was significantly correlated with increased DNMT1. Using an antisense DNMT1 oligo to transfect into SiHa HeLa C33A cell line, E-cadherin protein was re-expressed. We concluded that loss of E-cadherin expression was in part correlated with ...
The intercellular Adherens Junctions (AJs) are specialized sub-apical structures that function as principle mediators of cell-cell adhesion. Their disassembly correlates with a loss of cell-cell contact and an acquisition of migratory potential. The Adherens Junctions have a crucial role both as sensors of extracellular stimuli and in regulating the dynamics of epithelial cell sheets or with neighboring cells. Cadherins, the Type-I transmembrane proteins of the Adherens Junctions, are principally responsible for homotypic cell-cell adhesion. E-Cadherin, which is present primarily in epithelia, is the best-characterized Cadherin and represents the prototype of classical Cadherins. The extracellular domain of E-Cadherin binds to Ca2+ (Calcium) and forms complexes with the extracellular domains of E-Cadherin molecules on neighboring cells. The cytoplasmic domain of E-Cadherin associates with cytosolic proteins called Catenins (Alpha, Beta and p120), which in turn provide anchorage to the Actin ...
The role of E-cadherin in Hereditary Diffuse Gastric Cancer (HDGC) is unequivocal. Germline alterations in its encoding gene (CDH1) are causative of HDGC and occur in about 40% of patients. Importantly, while in most cases CDH1 alterations result in the complete loss of E-cadherin associated with a well-established clinical impact, in about 20% of cases the mutations are of the missense type. The latter are of particular concern in terms of genetic counselling and clinical management, as the effect of the sequence variants in E-cadherin function is not predictable. If a deleterious variant is identified, prophylactic surgery could be recommended. Therefore, over the last few years, intensive research has focused on evaluating the functional consequences of CDH1 missense variants and in assessing E-cadherin pathogenicity. In that context, our group has contributed to better characterize CDH1 germline missense variants and is now considered a worldwide reference centre. In this review, we highlight the
E-cadherin-mediated cell-cell adhesion is critical for naive pluripotency of cultured mouse embryonic stem cells (mESCs). E-cadherin-depleted mESC fail to downregulate their pluripotency program and are unable to initiate lineage commitment. To further explore the roles of cell adhesion molecules during mESC differentiation, we focused on p120 catenin (p120ctn). Although one key function of p120ctn is to stabilize and regulate cadherin-mediated cell-cell adhesion, it has many additional functions, including regulation of transcription and Rho GTPase activity. Here, we investigated the role of mouse p120ctn in early embryogenesis, mESC pluripotency and early fate determination. In contrast to the E-cadherin-null phenotype, p120ctn-null mESCs remained pluripotent, but their in vitro differentiation was incomplete. In particular, they failed to form cystic embryoid bodies and showed defects in primitive endoderm formation. To pinpoint the underlying mechanism, we undertook a structure-function approach.
A primary function of cadherins is to regulate cell adhesion. Here, we demonstrate a broader function of cadherins in the differentiation of specialized epithelial cell phenotypes. In situ, the rat retinal pigment epithelium (RPE) forms cell-cell contacts within its monolayer, and at the apical membrane with the neural retina; Na+, K(+)-ATPase and the membrane cytoskeleton are restricted to the apical membrane. In vitro, RPE cells (RPE-J cell line) express an endogenous cadherin, form adherens junctions and a tight monolayer, but Na+,K(+)-ATPase is localized to both apical and basal-lateral membranes. Expression of E-cadherin in RPE-J cells results in restriction and accumulation of both Na+,K(+)-ATPase and the membrane cytoskeleton at the lateral membrane; these changes correlate with the synthesis of a different ankyrin isoform. In contrast to both RPE in situ and RPE-J cells that do not form desmosomes, E-cadherin expression in RPE-J cells induces accumulation of desmoglein mRNA, and assembly ...
Looking for online definition of protocadherin-16 in the Medical Dictionary? protocadherin-16 explanation free. What is protocadherin-16? Meaning of protocadherin-16 medical term. What does protocadherin-16 mean?
Mol Pharmacol 82(5):777-783. 080309, PubMed PMID: 22821233, PubMed Central PMCID: PMC3477231 36 A. Krishnan et al. 49. Underwood CR, Garibay P, Knudsen LB, Hastrup S, Peters GH, Rudolph R et al (2010) Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor. J Biol Chem 285(1):723-730. M109. 033829, PubMed PMID: 19861722, PubMed Central PMCID: PMC2804221 50. Wouters MA, Rigoutsos I, Chu CK, Feng LL, Sparrow DB, Dunwoodie SL (2005) Evolution of distinct EGF domains with specific functions. ADGRCs are among the oldest aGPCRs. ADGRC consists of nine cadherin repeats (110 aa), followed by six EGF-like domains (see Sect. 1), two LAG domains, and an HBD (see Sect. 1). The cadherin repeats play a role in extracellular calcium binding [90]. The 3D structure of several cadherin domains in other proteins has been solved lately. These cadherin domains are formed by seven beta-strands and show similarity to immunoglobulin constant domains ...
Genetic studies in Drosophila have demonstrated that generation of microbicidal reactive oxygen species (ROS) through the NADPH dual oxidase (DUOX) is a first line of defense in the gut epithelia. Bacterial uracil acts as DUOX-activating ligand through poorly understood mechanisms. Here, we show that the Hedgehog (Hh) signaling pathway modulates uracil-induced DUOX activation. Uracil-induced Hh signaling is required for intestinal expression of the calcium-dependent cell adhesion molecule Cadherin 99C (Cad99C) and subsequent Cad99C-dependent formation of endosomes. These endosomes play essential roles in uracil-induced ROS production by acting as signaling platforms for PLC beta/PKC/Ca2+-dependent DUOX activation. Animals with impaired Hh signaling exhibit abolished Cad99C-dependent endosome formation and reduced DUOX activity, resulting in high mortality during enteric infection. Importantly, endosome formation, DUOX activation, and normal host survival are restored by genetic reintroduction of ...
β2-chimaerin is a Rac1-specific negative regulator and a candidate tumor suppressor in breast cancer but its precise function in mammary tumorigenesis in vivo is unknown. Here, we study for the first time the role of β2-chimaerin in breast cancer using a mouse model and describe an unforeseen role for this protein in epithelial cell-cell adhesion. We demonstrate that expression of β2-chimaerin in breast cancer epithelial cells reduces E-cadherin protein levels, thus loosening cell-cell contacts. In vivo, genetic ablation of β2-chimaerin in the MMTV-Neu/ErbB2 mice accelerates tumor onset, but delays tumor progression. Finally, analysis of clinical databases revealed an inverse correlation between β2-chimaerin and E-cadherin gene expressions in Her2+ breast tumors. Furthermore, breast cancer patients with low β2-chimaerin expression have reduced relapse free survival but develop metastasis at similar times. Overall, our data redefine the role of β2-chimaerin as tumor suppressor and provide ...
The cadherin-catenin complex is important for mediating homotypic, calcium-dependent cell-cell interactions in diverse tissue types. Although proteins of this complex have been identified, little is known about their interactions. Using a genetic assay in yeast and an in vitro protein-binding assay, we demonstrate that beta-catenin is the linker protein between E-cadherin and alpha-catenin and that E-cadherin does not bind directly to alpha-catenin. We show that a 25-amino acid sequence in the cytoplasmic domain of E-cadherin and the amino-terminal domain of alpha-catenin are independent binding sites for beta-catenin. In addition to beta-catenin and plakoglobin, another member of the armadillo family, p120 binds to E-cadherin. However, unlike beta-catenin, p120 does not bind alpha-catenin in vitro, although a complex of p120 and endogenous alpha-catenin could be immunoprecipitated from cell extracts. In vitro protein-binding assays using recombinant E-cadherin cytoplasmic domain and ...
Background:. Recent studies demonstrated that elevated levels of soluble E-cadherin (sE-cadherin), a product of proteolytic cleavage of cell-surface E-cadherin, are associated with higher risk for metastatic disease and poor prognosis in various tumor types. In a retrospective analysis, we have recently shown a significant association between sE-cadherin levels and histopathological regression scores. ABCSG-24, a randomised phase III trial comparing pathological complete response (pCR) rates of early breast cancer following preoperative systemic chemotherapy (PST) with epirubicin-docetaxel (ED) +/- capecitabine (EDC) with the addition of trastuzumab in Her2-positive tumors, was the perfect opportunity to prospectively evaluate, if sE-cadherin is a predictive marker for response to PST in breast cancer patients.. Materials and methods:. In this prospective analysis, sera of 196 patients undergoing PST for six cycles every three weeks were collected before initiation of each cycle. Soluble ...
The calcium-dependent homophilic cell adhesion molecule and candidate suppressor gene, E (epithelial)-cadherin, plays a major role in the organization and integrity of most epithelial tissues. Diffusely growing gastric carcinomas show markedly reduced homophilic cell-to-cell interactions. We speculated that mutations in the E-cadherin gene may be responsible for the scattered phenotype of this type of carcinoma. For that reason we have examined E-cadherin in 26 diffuse type, 20 intestinal type and 7 mixed gastric carcinomas (Lauréns classification) at the DNA, RNA, and protein levels.. Reverse transcription polymerase chain reaction and direct sequencing of amplified E-cadherin complementary DNA fragments revealed inframe skipping of either exon 8 or exon 9 in 10 patients with diffuse tumors and an exon 9 deletion in one patient with a mixed carcinoma; both exons encode putative calcium binding domains. These alterations were not seen in nontumorous gastric tissues. Splice site mutations ...
Cell-cell adhesion plays a key role in development, tissue maintenance and cancer (Birchmeier, 1995; Gumbiner, 2005; Takeichi, 1995; Yap, 1998). In vertebrates, the classical cadherins (i.e. type I and type II cadherins) comprise a large family (26 members) of transmembrane glycoproteins found in essentially all adhesive tissues (Gallin, 1998; Hulpiau and van Roy, 2009). Epithelial cadherin (E-cadherin, or cadherin 1) is the main cadherin in epithelial tissues and plays an important role in morphogenesis and homeostasis in most glandular tissues, including the mammary gland. Although the importance of cadherins in mammary morphogenesis is widely accepted, the role of p120-catenin (also known as catenin delta 1) in this process remains to be investigated.. The extracellular domains of cadherins connect adjacent cells via homophilic interaction, while the cytoplasmic domains form a complex with a group of proteins known as catenins (Gumbiner, 2005; Takeichi, 1991). p120-catenin (hereafter p120) ...
While recent research has shown that expression of ZEB-1 in a variety of tumors has a crucial impact on patient survival, there is little information regarding ZEB-1 expression in hepatocellular carcinoma (HCC). This study investigated the co-expression of ZEB-1 and E-cadherin in HCC by immunohistochemistry and evaluated its association with clinical factors, including patient prognosis. A total of 108 patients with primary HCC treated by curative hepatectomy were enrolled. ZEB-1 expression was immunohistochemically categorized as positive if at least 1% cancer cells exhibited nuclear staining. E-cadherin expression was divided into preserved and reduced expression groups and correlations between ZEB-1 and E-cadherin expression and clinical factors were then evaluated. With respect to ZEB-1 expression, 23 patients were classified into the positive group and 85 into the negative group. Reduced E-cadherin expression was seen in 44 patients and preserved expression in the remaining 64 patients. ZEB-1
Purpose: : Retinal pigment epithelial (RPE) cell proliferation and epithelial-to-mesenchymal transition (EMT) have been implicated to play a role in the development of proliferative vitreoretinopathy (PVR). Our in vitro model of PVR using sheets of RPE in primary culture shows that proliferation and EMT are linked, and that these processes are restricted to cells at the edge of the RPE sheets where cell-cell contacts are lost. The purpose of this study was to examine the change in expression of cell adhesion molecules during RPE cell proliferation and EMT. Methods: : RPE cell sheets, isolated from porcine eyes using Dispase, were cultured on porcine lens posterior capsule for up to 8 days in DMEM supplemented with fetal bovine serum. RPE cells with their underlying lens capsule were micro-dissected, lysed and used for western blot analyses. In addition, RPE sheets were fixed at various time points in culture for immunohistochemical staining of cell-cell adhesion molecules (E-, N-, and P-cadherin ...
Ovarian cancer is the most lethal gynecological cancer. This is mainly due to widespread peritoneal dissemination and malignant ascites, in which angiogenesis, the formation of new blood vessels, is critical to both ascites development and its metastasis. Loss of E-cadherin is a well-established marker that characterizes the progression of metastatic tumors, including ovarian cancer. The release of a soluble form of E-cadherin (sE-cad) has been frequently associated with a rapid reduction of functional E-cadherin at the cell surface. Importantly, sE-cad is significantly present in ascites from women with stage III/IV ovarian cancer when compared to women with benign ovarian cysts. However, despite the clinical significance, most studies have focused on its role in weakening cell-cell adhesion, whether sE-cad itself has any biological function is not fully understood. Here it is shown for the first time a potent angiogenic role for sE-cad released from ovarian carcinoma. Soluble form of ...
TY - JOUR. T1 - Screening the human protocadherin 8 (PCDH8) gene in schizophrenia. AU - Bray, N. J.. AU - Kirov, G.. AU - Owen, R. J.. AU - Jacobsen, N. J.. AU - Georgieva, L.. AU - Williams, H. J.. AU - Norton, N.. AU - Spurlock, G.. AU - Jones, S.. AU - Zammit, S.. AU - ODonovan, M. C.. AU - Owen, M. J.. PY - 2002/8. Y1 - 2002/8. N2 - Abnormalities in synaptic connectivity and plasticity have been implicated in the pathophysiology of schizophrenia. Molecules involved in the development and maintenance of neural circuitry include the recently cloned protocadherins. Human protocadherin 8 (PCDH8) is homologous to arcadlin, a molecule shown to play a role in hippocampal synaptic function in the rat. The gene encoding PCDH8 maps to a region on chromosome 13 where linkage to schizophrenia has been reported. In this study, the entire expressed sequence of the PCDH8 gene and over 800bp of the 5′ flanking region were screened for polymorphisms in 30 DSM-IV schizophrenia individuals using ...
Cadherins mediate homophilic, Ca2+-dependent cellular adhesion at adherens junctions. Experiments in MDCK cells, which provide a model for cadherins at adherens junctions, demonstrated the formation of cadherin-NPRAP-ABP complexes dependent on the expression of NPRAP and the integrity of the NPRAP-ABP interaction, and the formation of NPRAP-ABP-GluR2 complexes dependent on expression of ABP. This suggests that the proposed cadherin-NPRAP-ABP-GluR2 complexes can indeed form in cells. Two dominant-negative mutants of NPRAP were assayed for their effects on GluR2. One mutant does not interact with ABP, GRIP, or PSD-95, and the second binds these scaffolding proteins but does not bind to cadherins. Both mutants reduced GluR2 surface levels. This suggests that cadherin-NPRAP-ABP-GluR2 complexes contribute to the surface stabilization of GluR2. In neurons, adherens junction structures containing cadherins are found at synapses (Takeichi and Abe, 2005). This suggests that the AMPARs that are anchored ...
Mouse submandibular gland (SMG) begins its development at embryonic day 11 when oral epithelium grows into the underlying mesenchyme. The metabolic pathway of protein N-glycosylation is critical for SMG development and partial inhibition of DPAGT1, the gene that initiates N-glycosylation, drives cytodifferentiation of ductal structures. We have shown that DPAGT1 is a target of the canonical Wnt signaling pathway and that DPAGT1 regulates E-cadherin-mediated cell-cell adhesion, required for the survival of differentiating duct cells. Recently, the Hippo pathway has been shown to be critical for tissue development by regulating Wnt signaling and establishing apical-basal polarity. TAZ is a Hippo pathway transcription factor and polarity enhancer that also serves as a mechanosensor of the extracellular matrix. Objective: We investigated whether the Hippo pathway participated in SMG development and if it interacted with the metabolic pathway of N-glycosylation. Method: SMGs were dissected from mice ...
In multi-cellular organisms, cell-cell contacts that are mediated by classical cadherins have essential roles in many fundamental processes, such as morphogenesis, maintenance of tissue integrity, wound healing and cell polarity. Furthermore, there is overwhelming evidence that the adherens junctions (AJs) are also an important tumor and/or invasion suppressor. Alpha-catenin is the protein that connects E-cadherin-beta-catenin complexes with the actin cytoskeleton. Although it was previously considered to be a solely structural protein, it has become increasingly clear that alpha-catenin has a central role in both assembling the actin cytoskeleton and regulating its dynamics at cell-cell junctions thus regulating cell polarity. Cell-polarity mechanisms are responsible not only for the diversification of cell shapes but also for regulation of the asymmetric cell divisions of stem cells that are crucial for their correct self-renewal and differentiation. Disruption of cell polarity is a hallmark ...
In multi-cellular organisms, cell-cell contacts that are mediated by classical cadherins have essential roles in many fundamental processes, such as morphogenesis, maintenance of tissue integrity, wound healing and cell polarity. Furthermore, there is overwhelming evidence that the adherens junctions (AJs) are also an important tumor and/or invasion suppressor. Alpha-catenin is the protein that connects E-cadherin-beta-catenin complexes with the actin cytoskeleton. Although it was previously considered to be a solely structural protein, it has become increasingly clear that alpha-catenin has a central role in both assembling the actin cytoskeleton and regulating its dynamics at cell-cell junctions thus regulating cell polarity. Cell-polarity mechanisms are responsible not only for the diversification of cell shapes but also for regulation of the asymmetric cell divisions of stem cells that are crucial for their correct self-renewal and differentiation. Disruption of cell polarity is a hallmark ...
Cell migration is central to embryonic development, homeostasis and disease, processes in which cells move as part of a group or individually. Whereas the mechanisms controlling single-cell migration in vitro are relatively well understood, less is known about the mechanisms promoting the motility of individual cells in vivo. In particular, it is not clear how cells that form blebs in their migration use those protrusions to bring about movement in the context of the three-dimensional cellular environment. Here we show that the motility of chemokine-guided germ cells within the zebrafish embryo requires the function of the small Rho GTPases Rac1 and RhoA, as well as E-cadherin-mediated cell-cell adhesion. Using fluorescence resonance energy transfer we demonstrate that Rac1 and RhoA are activated in the cell front. At this location, Rac1 is responsible for the formation of actin-rich structures, and RhoA promotes retrograde actin flow. We propose that these actin-rich structures undergoing ...
Wnt pathway deregulation is a common characteristic of many cancers. But only Colorectal Cancer predominantly harbours mutations in APC, whereas other cancer types (hepatocellular carcinoma, solid pseudopapillary tumours of pancreas) have activating mutations in β-catenin (CTNNB1). We have compared the dynamics and the potency of β-catenin mutations in vivo. Within the murine small intestine (SI), an activating mutation of β-catenin took much longer to achieve a Wnt deregulation and acquire a crypt-progenitor-cell (CPC) phenotype than Apc or Gsk3 loss. Within the colon, a single activating mutation of β-catenin was unable to drive Wnt deregulation or induce the CPC phenotype. This ability of β-catenin mutation to differentially transform the SI versus the colon correlated with significantly higher expression of the β-catenin binding partner E-cadherin. This increased expression is associated with a higher number of E-cadherin:β-catenin complexes at the membrane. Reduction of E-cadherin ...
Malignant glioma is a formidable disease that commonly leads to death, mainly due to the invasion of tumor cells into neighboring tissues. Therefore, inhibition of tumor cell invasion may provide an effective therapy for malignant glioma. Here we report that nicotinic acid (NA), an essential vitamin, inhibits glioma cell invasion in vitro and in vivo. Treatment of the U251 glioma cells with NA in vitro results in reduced invasion, which is accompanied by a loss of mesenchymal phenotype and an increase in cell-cell adhesion. At the molecular level, transcription of the adherens junction protein E-cadherin is upregulated, leading to accumulation of E-cadherin protein at the cell-cell boundary. This can be attributed to NAs ability to facilitate the ubiquitination and degradation of Snail1, a transcription factor that represses E-cadherin expression. Similarly, NA transiently inhibits neural crest migration in Xenopus embryos in a Snail1-dependent manner, indicating that the mechanism of action ...
BACKGROUND:Colorectal Cancer (CRC) is one of the most frequently diagnosed neoplasms and also one of the main death causes. Cell adhesion molecules are taking part in specific junctions, contributing to tissue integrality. Lower expression of the cadherins may be correlated with poorer differentiation of the CRC, and its more aggressive phenotype. The aim of the study is to designate the cadherin genes potentially useful for the diagnostics, prognostics, and the treatment of CRC. MATERIAL AND METHODS:Specimens were collected from 28 persons (14 female and 14 male), who were operated for CRC. The molecular analysis was performed using oligonucleotide microarrays, mRNA used was collected from adenocarcinoma, and macroscopically healthy tissue. The results were validated using qRT-PCR technique. RESULTS:Agglomerative hierarchical clustering of normalized mRNA levels has shown 4 groups with statistically different gene expression. The control group was divided into 2 groups, the one was appropriate control
Mouse monoclonal antibody raised against recombinant human E-Cadherin. Recombinant protein corresponding to human E-Cadherin. (MAB21777) - Products - Abnova
Understanding the factors that regulate endothelial cell-cell junctions is important for many pathophysiological processes in which functional vascular integrity is compromised, such as development of neovasculature during angiogenesis and chronic inflammatory disorders. The present study shows that IQGAP1 colocalizes and forms a complex with VE-cadherin at the site of cell-cell contacts in unstimulated confluent HUVECs, and VEGF stimulation reduces their localization at the cell margin without affecting their complex formation. Knockdown of IQGAP1 using siRNA inhibits localization of VE-cadherin at cell-cell contacts as well as the following VEGF-stimulated events: (1) recruitment of VEGF2 to and the dissociation of α-catenin from the VE-cadherin/β-catenin complex; (2) ROS-dependent tyrosine phosphorylation of VE-cadherin, which is required for loss of cell-cell contacts8,9; and (3) capillary tube formation in 3-dimensional collagen gels. We also found that IQGAP1 expression is markedly ...
beta-catenin is a cytoplasmic protein associated with cadherin adhesion molecules and has been implicated in axis formation in Xenopus (McCrea, P. D., Brieher, W. M. and Gumbiner, B. M. (1993) J. Cell Biol. 127, 477-484). We have studied its distribution in Xenopus embryos by immunofluorescence on frozen sections. Consistent with its function in cell-cell adhesion, beta-catenin is present in every cell. However, high levels are expressed in certain regions and different tissues of the embryo. No simple correlation appears to exist between the levels of beta-catenin with the expected strength of adhesion. High levels of beta-catenin were found in regions undergoing active morphogenetic movements, such as the marginal zone of blastulae and gastrulae. This suggests that high expression of beta-catenin could be involved in dynamic adhesion events. Surprisingly, beta-catenin also accumulates on plasma membranes that probably do not establish direct or strong contacts with other cells. In particular, ...
The disappearance of epithelial phenotype and acquisition of mesenchymal phenotype constitute the basic molecular and morphological manifestations of EMT. This process increases cell mobility and constitutes a critical step in cell migration, which is associated with various biological processes, including cancer invasion and metastasis. Thus, the maintenance of epithelial phenotype and suppression of EMT have been increasingly recognized to be important for preventing cancer progression. During the execution of the EMT program many genes involved in cell adhesion, migration and invasion are transcriptionally altered, E-cadherin being one of the most important [51]55. Since E-cadherin functions as a key gatekeeper of the epithelial state, the partial loss of E-cadherin has been associated with carcinoma progression and poor prognosis in various human and mouse tumors [52]56. Evaluation of the molecular mechanisms involved in regulation of E-cadherin expression, therefore, might be a critical ...
2000). "Clustered cadherin genes: a sequence-ready contig for the desmosomal cadherin locus on human chromosome 18". Genomics. ... Garrod DR, Merritt AJ, Nie Z (2003). "Desmosomal cadherins". Curr. Opin. Cell Biol. 14 (5): 537-45. doi:10.1016/S0955-0674(02) ... Jun 1993). "Nomenclature of the desmosomal cadherins". J Cell Biol. 121 (3): 481-3. doi:10.1083/jcb.121.3.481. PMC 2119574. ... 2000). "Genomic organization and amplification of the human desmosomal cadherin genes DSC1 and DSC3, encoding desmocollin types ...
Cadherin-1 also known as CAM 120/80 or epithelial cadherin (E-cadherin) or uvomorulin is a protein that in humans is encoded by ... E-cadherin (epithelial) is the most well-studied member of the cadherin family. It consists of 5 cadherin repeats (EC1 ~ EC5) ... E-cadherin can sequester β-catenin on the cell membrane by the cytoplasmic tail of E-cadherin. Loss of E-cadherin expression ... "Entrez Gene: CDH1 cadherin 1, type 1, E-cadherin (epithelial)".. *^ Fleming TP, Papenbrock T, Fesenko I, Hausen P, Sheth B ( ...
... is required for its high affinity binding to the cytoplasmic domains of E-cadherin and desmosomal cadherin Dsg2, and the tumor ... is required for its high affinity binding to the cytoplasmic domains of E-cadherin and desmosomal cadherin Dsg2, and the tumor ... Bannon LJ, Cabrera BL, Stack MS, Green KJ (Nov 2001). "Isoform-specific differences in the size of desmosomal cadherin/catenin ... Bannon LJ, Cabrera BL, Stack MS, Green KJ (Nov 2001). "Isoform-specific differences in the size of desmosomal cadherin/catenin ...
They are involved in regulating the adhesive activity of cadherin. The three types of plakophilin proteins found in humans are ... The Molecular Biology of Cadherins. Academic Press. 116: 387-407. doi:10.1016/b978-0-12-394311-8.00017-0. PMC 3752792. PMID ...
Desmosomal cadherins, including the desmocollin family members and desmogleins, are found at desmosome cell-cell junctions and ... Cadherin-like junctional molecules generated by alternative splicing". The Journal of Biological Chemistry. 266 (16): 10438-45 ... Desmocollin-2 is a cadherin-type protein that functions to link adjacent cells together in specialized regions known as ... Desmocollin-2 is a calcium-dependent glycoprotein that is a member of the desmocollin subfamily of the cadherin superfamily. ...
Desmocollin-3 is a calcium-dependent glycoprotein that is a member of the desmocollin subfamily of the cadherin superfamily. ... Jun 1993). "Nomenclature of the desmosomal cadherins" (PDF). J Cell Biol. 121 (3): 481-3. doi:10.1083/jcb.121.3.481. PMC ... 2001). "Down-regulation of the desmosomal cadherin desmocollin 3 in human breast cancer". Int. J. Oncol. 19 (1): 169-74. doi: ... 2000). "Genomic organization and amplification of the human desmosomal cadherin genes DSC1 and DSC3, encoding desmocollin types ...
Müller, U (October 2008). "Cadherins and mechanotransduction by hair cells". Current Opinion in Cell Biology. 20 (5): 557-566. ...
Cadherins are calcium-dependent adhesion molecules. Cadherins are extremely important in the process of morphogenesis - fetal ... Cadherin molecules form the actual anchor by attaching to the cytoplasmic plaque, extending through the membrane and binding ... Together with an alpha-beta catenin complex, the cadherin can bind to the microfilaments of the cytoskeleton of the cell. This ... Similarly to desmosomes and hemidesmosomes, their transmembrane anchors are composed of cadherins in those that anchor to other ...
Amagai M (1999). "Autoimmunity against desmosomal cadherins in pemphigus". J. Dermatol. Sci. 20 (2): 92-102. doi:10.1016/S0923- ...
The encoded protein has a signal peptide, 27 cadherin repeat domains and a unique cytoplasmic region. This particular cadherin ... Protein dachsous homolog 1, also known as protocadherin-16 (PCDH16) or cadherin-19 (CDH19) or cadherin-25 (CDH25) or fibroblast ... cadherin-1 (FIB1), is a protein that in humans is encoded by the DCHS1 gene. This gene is a member of the cadherin superfamily ... 2001). "Identification of three novel non-classical cadherin genes through comprehensive analysis of large cDNAs". Brain Res. ...
... forms distinct complexes with cadherins and desmosomal cadherins. Plakoglobin is a major cytoplasmic component of ... is required for its high affinity binding to the cytoplasmic domains of E-cadherin and desmosomal cadherin Dsg2, and the tumor ... interacts with E-cadherin and N-cadherin". The Journal of Cell Biology. 118 (3): 671-9. doi:10.1083/jcb.118.3.671. PMC 2289540 ... interacts with E-cadherin and N-cadherin". The Journal of Cell Biology. 118 (3): 671-9. doi:10.1083/jcb.118.3.671. PMC 2289540 ...
P-cadherins), neural (N-cadherins), retinal (R-cadherins), brain (B-cadherins and T-cadherins), and muscle (M-cadherins). Many ... The cadherins are homophilic Ca2+ -dependent glycoproteins. The classic cadherins (E-, N- and P-) are concentrated at the ... Cadherins are notable in embryonic development. For example, cadherins are crucial in gastrulation for the formation of the ... The diverse family of cadherins include epithelial (E-cadherins), placental ( ...
These neural cadherin-like cell adhesion proteins most likely play a critical role in the establishment and function of ... Wu Q, Maniatis T (Jul 1999). "A striking organization of a large family of human neural cadherin-like cell adhesion genes". ... Each variable region exon encodes the extracellular region, which includes 6 cadherin ectodomains and a transmembrane region. ... Matsuyoshi N, Imamura S (1997). "Multiple cadherins are expressed in human fibroblasts". Biochem. Biophys. Res. Commun. 235 (2 ...
N-cadherin, a classical cadherin from the cadherin superfamily, is composed of five extracellular cadherin repeats, a ... N-cadherin, also known as Cadherin-2 (CDH2) or neural cadherin (NCAD) is a protein that in humans is encoded by the CDH2 gene. ... N-cadherin, as well as other cadherins, interact with N-cadherin on an adjacent cell in an anti-parallel conformation, thus ... N-cadherin complexed to catenins has been described as a master regulator of intercalated disc function. N-cadherin appears at ...
Larue, L.; Antos, C.; Butz, S.; Huber, O.; Delmas, V.; Dominis, M.; Kemler, R. (1996). "A role for cadherins in tissue ... Burdsal, C. A.; Damsky, C. H.; Pedersen, R. A. (1993). "The role of E-cadherin and integrins in mesoderm differentiation and ... EBs are formed by the homophilic binding of the Ca2+ dependent adhesion molecule E-cadherin, which is highly expressed on ...
The human FAT1 cadherin gene was cloned in 1995 from a human T-leukemia (T-ALL) cell line and consists of 27 exons located on ... FAT1 cadherin is multiply phosphorylated on its ectodomain but phosphorylation is not catalysed by FJX1. The ectodomain of FAT1 ... The FAT1 cadherin has been ascribed both as putative tumour suppressor or oncogene in different contexts. Loss of ... December 2015). "FAT1 cadherin acts upstream of Hippo signalling through TAZ to regulate neuronal differentiation". Cellular ...
... has a functional role in metastasis of tumor similar to E-selectin.[20] P-selectin is expressed on the surface of both stimulated endothelial cell and activated platelet and helps cancer cells invade into bloodstream for metastasis and provided locally with multiple growth factors respectively.[21] Moreover, it has been known that platelet facilitates tumor metastasis by forming complexes with tumor cells and leukocytes in the vasculature thus preventing recognition by macrophage, this is thought to contribute to the seeding of tumor microemboli to distant organs.[22] In vivo mice experiment showed that reduction in circulating platelets could reduce cancer metastasis.[23] The oligosaccharide sialylated Lewis x (sLe(x)) is expressed on the surface of tumor cells and can be recognized by E-selectin and P-selectin, playing on a key role in metastasis of the tumor. However, in the 4T1 breast cancer cell line, E-selectin reactivity is sLe(x) dependent while P-selectin reactivity is ...
This gene encodes a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium- ... "Entrez Gene: CDH8 cadherin 8, type 2".. *^ Pagnamenta AT, Khan H, Walker S, Gerrelli D, Wing K, Bonaglia MC, et al. (Jan 2011 ... cadherin binding. Cellular component. • axon terminus. • integral component of membrane. • synaptic cleft. • membrane. • plasma ... Cadherin-8 is a protein that in humans is encoded by the CDH8 gene.[5][6][7] ...
... is a calcium-binding protein of the sarcoplasmic reticulum. The protein helps hold calcium in the cisterna of the sarcoplasmic reticulum after a muscle contraction, even though the concentration of calcium in the sarcoplasmic reticulum is much higher than in the cytosol. It also helps the sarcoplasmic reticulum store an extraordinarily high amount of calcium ions. Each molecule of calsequestrin can bind 18 to 50 Ca2+ ions.[1] Sequence analysis has suggested that calcium is not bound in distinct pockets via EF-hand motifs, but rather via presentation of a charged protein surface. Two forms of calsequestrin have been identified. The cardiac form Calsequestrin-2 (CASQ2) is present in cardiac and slow skeletal muscle and the fast skeletal form Calsequestrin-1(CASQ1) is found in fast skeletal muscle. The release of calsequestrin-bound calcium (through a calcium release channel) triggers muscle contraction. The active protein is not highly structured, more than 50% of it adopting a ...
The VCAM-1 protein mediates the adhesion of lymphocytes, monocytes, eosinophils, and basophils to vascular endothelium. It also functions in leukocyte-endothelial cell signal transduction, and it may play a role in the development of atherosclerosis and rheumatoid arthritis. Upregulation of VCAM-1 in endothelial cells by cytokines occurs as a result of increased gene transcription (e.g., in response to Tumor necrosis factor-alpha (TNF-α) and Interleukin-1 (IL-1)) and through stabilization of Messenger RNA (mRNA) (e.g., Interleukin-4 (IL-4)). The promoter region of the VCAM-1 gene contains functional tandem NF-κB (nuclear factor-kappa B) sites. The sustained expression of VCAM-1 lasts over 24 hours. Primarily, the VCAM-1 protein is an endothelial ligand for VLA-4 (Very Late Antigen-4 or integrin α4β1) of the β1 subfamily of integrins. VCAM-1 expression has also been observed in other cell types (e.g., smooth muscle cells). It has also been shown to interact with EZR[7] and Moesin.[7] CD106 ...
... is a multistructural and multifunctional cell surface molecule involved in cell proliferation, cell differentiation, cell migration, angiogenesis, presentation of cytokines, chemokines, and growth factors to the corresponding receptors, and docking of proteases at the cell membrane, as well as in signaling for cell survival. All these biological properties are essential to the physiological activities of normal cells, but they are also associated with the pathologic activities of cancer cells. Experiments in animals have shown that targeting of CD44 by antibodies, antisense oligonucleotides, and CD44-soluble proteins markedly reduces the malignant activities of various neoplasms, stressing the therapeutic potential of anti-CD44 agents. High levels of the adhesion molecule CD44 on leukemic cells are essential to generate leukemia.[24] Furthermore, because alternative splicing and posttranslational modifications generate many different CD44 sequences, including, perhaps, tumor-specific ...
Cadherin 10 is a protein that in humans is encoded by the CDH10 gene. An association with autism has been suggested. Cadherin ... "Entrez Gene: cadherin 10". Suzuki S, Sano K, Tanihara H (April 1991). "Diversity of the cadherin family: evidence for eight new ... Ali J, Liao F, Martens E, Muller WA (1997). "Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial cell- ... Kools P, Vanhalst K, Van den Eynde E, van Roy F (1999). "The human cadherin-10 gene: complete coding sequence, predominant ...
Therefore, PLEKHA7lstabilises both cadherins and nectins at AJ. Genome-wide association studies suggest that PLEKHA7 is ... However, in Eph4 cell line, PLEKHA7 is recruited to E-cadherin based AJ by Afadin, independently of p120. PLEKHA7 knockdown ... "Mayo Clinic researchers find new code that makes reprogramming of cancer cells possible". Distinct E-cadherin-based complexes ... Nectins are the second major class of transmembrane adhesion molecules at adherens junctions, besides cadherins. ...
Dusek, Rachel L; Godsel, Lisa M.; l, Kathleen J. (January 2007). "Discriminating roles of desmosomal cadherins:Beyond ...
Cadherin-1), CDH2 N-cadherin (Cadherin-2), CDH4 R-cadherin (cadherin-4), CDH5 VE-cadherin (cadherin 5, CDH5), CTNND1 ( ... Cadherins regulate cell-cell adhesion during development of the body and in adult tissue. Disruption of cadherin proteins, by ... Cadherins stabilize adherens junctions through the interaction of the cadherin cytoplasmic domains with catenin proteins, such ... PTPmu likely regulates cadherin-dependent adhesion by interacting with both cadherins and catenins via PTPmu's cytoplasmic ...
The flamingo cadherins are located at the plasma membrane and have nine cadherin domains, seven epidermal growth factor-like ... Cadherin EGF LAG seven-pass G-type receptor 2 is a protein that in humans is encoded by the CELSR2 gene. The protein encoded by ... "Entrez Gene: CELSR2 cadherin, EGF LAG seven-pass G-type receptor 2 (flamingo homolog, Drosophila)". Nagase T, Seki N, Ishikawa ... Wu Q, Maniatis T (1999). "A striking organization of a large family of human neural cadherin-like cell adhesion genes". Cell. ...
Many cadherins in the central nervous system exhibit distinct spatial and temporal expression patterns. For example, N-cadherin ... Cadherins are calcium- dependent, homophilic cell adhesion molecules that form complexes with cytosolic partners known as ... Classical cadherins have five extracellular repeating structures which bind calcium, a single transmembrane domain, and an ... An increase in activity at a particular spine leads to the dimerization of N-cadherin which is then cleaved leading the ...
Cadherin EGF LAG seven-pass G-type receptor 1 also known as flamingo homolog 2 or cadherin family member 9 is a protein that in ... The flamingo cadherins are located at the plasma membrane and have nine cadherin domains, seven epidermal growth factor-like ... "Entrez Gene: CELSR1 cadherin, EGF LAG seven-pass G-type receptor 1 (flamingo homolog, Drosophila)". Human CELSR1 genome ... Wu Q, Maniatis T (1999). "A striking organization of a large family of human neural cadherin-like cell adhesion genes". Cell. ...
N-cadherin mediates cell-cell interactions, stimulates axonal guidance guides neural progenitor cell migration ... "A self-renewing division of zebrafish Müller glial cells generates neuronal progenitors that require N-cadherin to regenerate ...
Cell-cell adhesion is primarily mediated by cadherin receptors and therefore the adhesome of cell-cell adhesion is referred to ... 2. they directly interact with one of the core adhesome components, such as integrin, cadherin or catenins AND/OR their ... Later, with the emergence of the cadherin-catenin-actin structure they were co-opted into the cadhesome. Whittaker, Charles A ... Zaidel-Bar, Ronen (2013-01-15). "Cadherin adhesome at a glance". J Cell Sci. 126 (2): 373-378. doi:10.1242/jcs.111559. ISSN ...
Cadherins are a group of proteins that help cells stick together. They are the main components of certain types of junctions ... Classical cadherins include E-cadherin, N-cadherin, P-cadherin and N-cadherin 2. They all have a similar structure, with five ... Cadherin structure. Cadherins are named for calcium dependent adhesion. The external domain of a cadherin molecule - the part ... Cadherins role in cancer. E-cadherin, a member of the cadherin family, has a very important role in organizing the epithelium ...
Researchers at the Johns Hopkins Kimmel Cancer Center discovered that a cell adhesion protein, E-cadherin, allows breast cancer ...
Epithelial cadherin; Uvomorulin E-cadherin, a 120 kDa molecule, is a prototypical member of the classical cadherin family of ... Thus, E-cadherin and other members of the cadherin family play a crucial role in establishing and maintaining the integrity of ... E-cadherin, a 120 kDa molecule, is a prototypical member of the classical cadherin family of single-pass transmembrane proteins ... E-cadherin is the main adhesion molecule of the adherens junctions of epithelial cells, and via catenins it is linked to the ...
Knockdown of desmosomal cadherins affects gastrulation movements. In situ hybridisation images for gata1 at 30% epiboly (A) and ... Knockdown of desmosomal cadherins causes epiboly defects. A and C show morphants at 6 hpf whose blastomeres became detached and ... Desmosomal cadherins are expressed from early development onwards. Semi-quantitative RT-PCR analysis of zfDsc, zfDsga, zfDsgb ... Knockdown of desmosomal cadherins affects desmosome structure. A. Apical junctional complex between cells of the EL of wild ...
... cadherin 7, type 2 CDH8 - cadherin 8, type 2 CDH9 - cadherin 9, type 2 (T1-cadherin) CDH10 - cadherin 10, type 2 (T2-cadherin) ... CDH2 - N-cadherin (neural): N-cadherins are found in neurons CDH12 - cadherin 12, type 2 (N-cadherin 2) CDH3 - P-cadherin ( ... Proteopedia Cadherin - view cadherin structure in interactive 3D Cadherin domain in PROSITE The cadherin family The Cadherin ... T-cadherin - H-cadherin (heart) CDH15 - M-cadherin (myotubule) CDH16 - KSP-cadherin CDH17 - LI cadherin (liver-intestine) CDH18 ...
Cadherins are transmembrane proteins that mediate cell-cell adhesion in animals [PMID: 22833291]. Cadherin-16 (CDH16) or kidney ... CDH16/Ksp-cadherin is expressed in the developing thyroid gland and is strongly down-regulated in thyroid carcinomas.. ... Expression of Ksp-cadherin during kidney development and in renal cell carcinoma.. Br. J. Cancer 92 2010-7 2005 ... CDH16 colocalises with CDH1/E-cadherin on the basolateral plasma membrane of thyrocytes, and might play a role during thyroid ...
Crystal structures of cadherin-23 and Drosophila N-cadherin reveal unique features of atypical cadherins. (a) Structures of ... VE-cadherin exchanges Trp2 and Trp4 like type II cadherins, but the interface is limited to the apex of the domain, as in type ... Classical cadherins from adhesive dimers by exchange of the N-terminal β-strand. (a) A classical cadherin trans dimer is shown ... In type I cadherins, residue Trp2 in domain EC1 is swapped between binding partners. In type II cadherins, two Trp residues, ...
T-cadherin also known as cadherin 13, H-cadherin (heart) (CDH13) is a unique member of cadherin superfamily because it lacks ... T-cadherin expression results in LDL-induced migration of T-cadherin expressing cells compared to control. It is likely that T- ... T-cadherin expression was found to be altered in tumor vessels: in Lewis carcinoma lung metastasis the expression of T-cadherin ... T-cadherin is a GPI-anchored member of cadherin superfamily, which lacks a direct contact with cytoskeleton and therefore is ...
Medical definition of cadherin: any of various glycoproteins that mediate the calcium-dependent adhesion of cells to other ... Learn More about cadherin. Share cadherin Post the Definition of cadherin to Facebook Share the Definition of cadherin on ... Comments on cadherin What made you want to look up cadherin? Please tell us where you read or heard it (including the quote, if ... Dictionary Entries near cadherin. cade cade oil caderas cadherin cadmium cadmium sulfide caduceus ...
to an intracellular domain of chicken N-cadherin. Specificity. reacts with N-cadherin and does not crossreact with E-cadherin ...
If you know of any papers that use this antibody, please contact us at antibodies [at] alzforum [dot] org for consideration in the References section.. ...
VE-cadherin,. vascular endothelial cadherin;. CHO,. Chinese hamster ovary;. AFM,. atomic force microsopy;. PEG,. polyethylene ... whereas endothelial cells adhere to each other by vascular endothelial-cadherin (VE-cadherin) (3). Cadherins are type I single ... Structure of VE-Cadherin-Fc.. AFM imaging of hydrated VE-cadherin-Fc adsorbed to mica surface in buffer A containing 5 mM CaCl2 ... Recombinant VE-Cadherin-Fc.. A VE-cadherin-Fc fusion protein was generated by placing a cDNA fragment coding for the complete ...
Dystroglycan-type cadherin-like (IPR006644). Short name: Cadg Overlapping homologous superfamilies *Cadherin-like superfamily ( ... Cadherin-like domains in alpha-dystroglycan, alpha/epsilon-sarcoglycan and yeast and bacterial proteins.. Curr. Biol. 12 R197-9 ... In animals, cadherin domain-containing proteins are adhesion molecules that modulate a wide variety of processes including cell ... Crystal structures have revealed that multiple cadherin domains form Ca2+-dependent rod-like structures with a conserved Ca2+- ...
... Curr Opin Cell Biol. 2011 Oct;23(5):523-30. doi: 10.1016/j.ceb.2011.08.003. ... We further discuss the current understanding of the rudiments of a cadherin-based mechanosensing and transduction pathway, ... This review highlights recent findings, which demonstrate that protein complexes associated with classical cadherins, the ...
... Galina Reshetnikova Institute of Cytology, Russian ...
E-cadherin (epithelial-cadherin), encoded by the CDH1 gene, is a transmembrane glycoprotein playing a crucial role in ... E-cadherin has been reported to be a tumor suppressor and to be down regulated in gastric cancer. Besides genetic mutations in ... In addition, expression of E-cadherin could be mediated by infectious agents such as H. pylori (Helicobacter pylori). As E- ... E-Cadherin and Gastric Cancer: Cause, Consequence, and Applications. Xin Liu and Kent-Man Chu ...
Using human AECs and cell lines, we demonstrate that cadherin-26 (CDH26) is abundantly expressed in differentiated AECs, ... localizes to the cell apices near ciliary membranes, and has functional cadherin domains with homotypic binding. We find a ... 2: Cadherin-26 (CDH26) localizes to the apical membrane.. a Immunofluorescence for E-cadherin (green), CDH26 (red), acetylated ... including classical cadherins, protocadherins, and atypical cadherins. Atypical cadherins such as FAT111 and flamingo12 have ...
Cadherins are regulated at the cell surface by an inside-out signalling mechani … ... The dynamic regulation of cadherins in response to various extracellular signals controls cell sorting, cell rearrangements and ... Cadherin cell-adhesion proteins mediate many facets of tissue morphogenesis. ... Cadherin cell-adhesion proteins mediate many facets of tissue morphogenesis. The dynamic regulation of cadherins in response to ...
CDH5 or VE-Cadherin is a 140 kDa protein belonging to the cadherin family of cell adhesion molecules which interact ... VE-cadherin is the major component of endothelial adherens junctions and is specific to endothelial cells ... CD144 (VE-Cadherin) Antigen. CD144, also called Cadherin 5, CDH5 or VE-Cadherin is a 140 kDa protein belonging to the cadherin ... VE-cadherin is the major component of endothelial adherens junctions and is specific to endothelial cells. It is present in all ...
Type II cadherin ectodomain structures: implications for classical cadherin specificity.. Patel, S.D., Ciatto, C., Chen, C.P., ... Cadherin-11. A, B. 99. Mus musculus. Mutation(s): 0 Gene Names: Cdh11, Cad-11. ... The EC1 domains of type I and type II cadherins appear to encode cell adhesive specificity in vitro. Moreover, perturbation of ... Type I and II classical cadherins help to determine the adhesive specificities of animal cells. Crystal-structure determination ...
... for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a ... Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for ... "Cadherins" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Cadherins" by people in Harvard Catalyst Profiles by year, and ...
that glucose-induced insulin secretion in individual β-cells can be directly linked to specific cadherin-cadherin ligation ... From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion. Trends Genet 1993;9:317-321pmid: ... Molecular basis for the regulation of islet beta cell mass in mice: the role of E-cadherin. Diabetologia 2013;56:856-866pmid: ... Integrins and cadherins join forces to form adhesive networks. J Cell Sci 2011;124:1183-1193pmid:21444749. ...
... of metalloproteinases by EphB-ephrin-B interactions alters cell affinity by inducing localized cleavage of E-cadherin. ... of metalloproteinases by EphB-ephrin-B interactions alters cell affinity by inducing localized cleavage of E-cadherin. ...
Abcams E Cadherin ELISA Kit (ab100678) suitable for Cell culture supernatant, Serum, Plasma in mouse. Reliably quantify 6 pg/ ... Abcams E-Cadherin Mouse ELISA (Enzyme-Linked Immunosorbent Assay) kit is an in vitro enzyme-linked immunosorbent assay for the ... Furthermore, E Cadherin plays a crucial role in the maintenance of the epithelial junctional complex and is as such an ... Standards and samples are pipetted into the wells and E-Cadherin present in a sample is bound to the wells by the immobilized ...
Rabbit polyclonal pan Cadherin antibody validated for IHC and tested in Human, Mouse, Rat, Chk, Cow, Dog, Xl and Mk. Immunogen ... This antibody recognizes members of the Cadherin family of proteins including E-cadherin, N-cadherin, P-cadherin and R-cadherin ... In adhesion junctions cadherins are bound to beta and gamma catenins which in turn bind to alpha catenin, an actin binding ... Cadherins are expressed in a tissue specific manner and and are required for assembly of cells into solid tissue. Individual ...
Down-regulation of E-cadherin expression has been observed in a number of carcinomas and is usually associated with advanced ... cadherin is a 120 kDa transmembrane cell adhesion molecule. It has a significant function in intercellular adhesion of ... Anti-E-cadherin, NCH-38 recognizes the 120 kDa mature form and 82 kDa fragment of E-cadherin in Western blots of A431 cells ... FLEX Monoclonal Mouse Anti-Human E-Cadherin Clone NCH-38 Ready-to-Use (Dako Omnis) - EN / FR / DE Instructions for Use, Code ...
The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin. ... EPITHELIAL-CADHERIN B, D 151 Mus musculus Fragment: CYTOPLASMIC DOMAIN Gene Name(s): Cdh1 ...
On the other hand, inhibitory synapses appear to contain a different cadherin (or cadherins) in that N-cadherin is lost but β- ... E-cadherin from epithelial cells, N-cadherin from neural epithelium, and P-cadherin from placenta (Hatta and Takeichi, 1986; ... 1991) T-cadherin, a novel cadherin cell adhesion molecule in the nervous system lacks the conserved cytoplasmic region. Neuron ... N-cadherin is present in axons and dendrites before synaptogenesis. Fluorescence photomicrographs showing N-cadherin (A, D, G) ...
Here, we show that mesenchymal cadherin-11 modulates stromal fibroblast function. Cadherin-11-deficient mice displayed ... Cadherin-11 expression in eWAT, muscle, and liver from WT mice fed a ND or HFD for 5 weeks (. n. = 5 ND-eWAT, n. = 12 HFD-eWAT ... Cell-surface cadherin-11 expression on CD45-CD235α-CD31- cells in stromal vascular cells isolated from obese human omentum fat ... Importantly, anti-cadherin-11 mAb blockade similarly improved inflammation and glycemic control in obese WT mice. These results ...
E-Cadherin in Cell-Cell Adhesion and Cancer Diagnostics. E-Cadherin is a member of the cadherin superfamily and is fundamental ... E-Cadherin as a Cancer Biomarker. E-cadherin is a calcium-regulated adhesion molecule expressed in most normal epithelial ... E-cadherin is also associated with gland formation, stratification, and epithelial polarization, while loss of E-cadherin can ... Specifically, E-cadherin is an approximately 100 kDa epithelial cell glycoprotein whose extracellular domain interacts with ...
  • Although classical cadherins take a role in cell layer formation and structure formation, desmosomal cadherins focus on resisting the catastrophe towards the cells. (wikipedia.org)
  • Desmosomal cadherins are responsible to maintain the function of desmosomes that is to overturn the mechanical stress of the tissues. (wikipedia.org)
  • Similar to classical cadherins, desmosomal cadherins has a single transmembrane domain, five EC repeats, and an intracellular domain. (wikipedia.org)
  • Two types of desmosomal cadherins exist, and they are called desmogleins and desmocollins that contains an intracellular anchor and cadherin like sequence (ICS). (wikipedia.org)
  • The adaptor proteins that associate with desmosomal cadherins are plakoglobin (related to β {\displaystyle \beta } -catenin), plakophilins (p120 catenin subfamily), and desmoplakins. (wikipedia.org)
  • Desmoglein and desmocollin are desmosomal cadherins . (news-medical.net)
  • Desmosomal cadherins in zebrafish epiboly and gastrulation. (nih.gov)
  • The desmosomal cadherins (DCs), desmocollin (Dsc) and desmoglein (Dsg), are the adhesion molecules of desmosomes, intercellular adhesive junctions of epithelia and cardiac muscle. (nih.gov)
  • Classical and desmosomal cadherins at a glance. (ebi.ac.uk)
  • Desmosomal cadherins mediate cell-cell adhesion in epithelial tissues and have been known to be altered in cancer. (nature.com)
  • We have previously shown that one of the two intestinal epithelial desmosomal cadherins, desmocollin-2 (Dsc2) loss promotes colonic epithelial carcinoma cell proliferation and tumor formation. (nature.com)
  • Taken together, these data demonstrate that partner desmosomal cadherins Dsg2 and Dsc2 play opposing roles in controlling colonic carcinoma cell proliferation through differential effects on EGFR signaling. (nature.com)
  • 1 Stratified epithelia such as the epidermis express multiple isoforms of each desmosomal cadherin, whereas simple human columnar intestinal epithelium expresses only the two desmosomal cadherins, desmoglein-2 (Dsg2) and desmocollin-2 (Dsc2). (nature.com)
  • In addition to their function in mediating cell adhesion, desmosomal cadherins have also been implicated in the regulation of epithelial cell proliferation and tumorigenesis. (nature.com)
  • Thus, protocadherins might play roles distinct from those of the classical and desmosomal cadherins. (biologists.org)
  • It binds independently to E-cadherin in the adherens junctions and also to the desmosomal cadherins desmoglein and desmocollin. (uninet.edu)
  • The desmosomal cadherins, desmogleins (Dsgs) and desmocollins (Dscs), are transmembrane molecules that mediate adhesion through their extracellular domains and serve as a scaffold for assembly of the desmosomal plaque through their cytoplasmic domains. (genenames.org)
  • The desmosomal cadherins are potential cell adhesion molecules of the desmosome type of cell junction by virtue of their homology to the cadherin class of cell adhesion molecules. (humpath.com)
  • Two classes of desmosomal cadherins are known, namely, the desmogleins (DSGs) and the desmocollins (DSCs) (MIM.125645). (humpath.com)
  • CDH16 colocalises with CDH1/E-cadherin on the basolateral plasma membrane of thyrocytes, and might play a role during thyroid development [ PMID: 22028439 ]. (ebi.ac.uk)
  • E-cadherin (epithelial-cadherin), encoded by the CDH1 gene, is a transmembrane glycoprotein playing a crucial role in maintaining cell-cell adhesion. (hindawi.com)
  • Besides genetic mutations in CDH1 gene to induce hereditary diffuse gastric cancer (HDGC), epigenetic factors such as DNA hypermethylation also contribute to the reduction of E-cadherin in gastric carcinogenesis. (hindawi.com)
  • Mutations of the E-cadherin gene (CDH1), which is located on chromosome 16q22.1 and acts as a tumour-suppressor gene, have been described in several epithelial cancers, especially in lobular breast and diffuse gastric carcinomas. (uninet.edu)
  • Pan Cadherin including CDH1, CDH2, CDH3, CDH4 protein belong to a family of transmembrane molecules that mediate calcium-dependent intercellular adhesion. (thermofisher.com)
  • In humans, E-cadherin is encoded by the CDH1 gene present on chromosome 16. (thermofisher.com)
  • Auf www.antikoerper-online.de finden Sie aktuell 919 Cadherin 1, Type 1, E-Cadherin (Epithelial) (CDH1) Antikörper von 39 unterschiedlichen Herstellern. (antikoerper-online.de)
  • E-cadherin (CDH1) loss occurs frequently in carcinogenesis, contributing to invasion and metastasis. (sigmaaldrich.com)
  • E-, N-, P-, VE-, Proto-, desmosomal and FAT cadherins have been found to regulate breast cancer in positive as well as negative fashion, whereby both Ecadherin (CDH1) and N-cadherin (CDH2) contribute significantly towards transitioning from epithelial state to mesenchymal state (EMT) and enacting the abnormal cells to invade and metastasize nearby and distant tissues. (eurekaselect.com)
  • Epithelial (E-cadherin) (CDH1). (expasy.org)
  • The CDH3 gene is localized in the larger arm of chromosome 16, just 32Kb upstream of the gene encoding CDH1 (E-cadherin) (Bussemakers et al. (atlasgeneticsoncology.org)
  • Sharing about 67% of homology with the CDH1/E-cadherin gene, P-cadherin differs mainly in the extracellular portion and it is far less characterized. (atlasgeneticsoncology.org)
  • T-cadherin also known as cadherin 13, H-cadherin (heart) (CDH13) is a unique member of cadherin superfamily because it lacks the transmembrane and cytoplasmic domains and is anchored to the cells membrane through the GPI anchor. (wikipedia.org)
  • T-cadherin is a GPI-anchored member of cadherin superfamily, which lacks a direct contact with cytoskeleton and therefore is not involved in cell-cell adhesion. (wikipedia.org)
  • Cadherins are a superfamily of cell surface glycoproteins whose ectodomains contain multiple repeats of β-sandwich extracellular cadherin (EC) domains that adopt a similar fold to immunoglobulin domains. (nih.gov)
  • The cadherin superfamily is comprised of many proteins with different structures and functions, including classical cadherins, protocadherins, and atypical cadherins. (nature.com)
  • This article focuses on adhesion receptors of the cadherin superfamily ( 19 , 20 ), which were referred to as uvomorulin in early work by Kemler et al. (diabetesjournals.org)
  • E-Cadherin is a member of the cadherin superfamily and is fundamental player in a wide range of cellular processes such as development, morphology, polarity, migration and tissue integrity. (novusbio.com)
  • VE-cadherin is a classical cadherin from the cadherin superfamily and the gene is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. (wikidoc.org)
  • E(pithelial)-cadherin is the prototypic member of the type-I cadherin superfamily. (uninet.edu)
  • β-Catenin protein is a member of the 'armadillo' superfamily and was originally described as an element of the E-cadherin/catenin complex. (uninet.edu)
  • Cadherin genes encode a superfamily of conserved transmembrane proteins that share an adhesive ectodomain composed of tandem cadherin repeats. (ovid.com)
  • More than 100 human cadherin superfamily members have been identified, which can be classified into three families: major cadherins, protocadherins and cadherin-related proteins. (ovid.com)
  • The stability of this association is regulated by phosphorylation and dephosphorylation of beta-catenin.This gene is a classical cadherin from the cadherin superfamily. (thermofisher.com)
  • E-Cadherin (epithelial cadherin) is a classical cadherin from the cadherin (alcium dependent adhesion protein) superfamily. (thermofisher.com)
  • Maeirah Afzal Ashaie and Ezharul Hoque Chowdhury, "Cadherins: The Superfamily Critically Involved in Breast Cancer", Current Pharmaceutical Design (2016) 22: 616. (eurekaselect.com)
  • The fat tumor suppressor gene in Drosophila encodes a novel member of the cadherin gene superfamily. (expasy.org)
  • This gene is a type II classical cadherin from the cadherin superfamily. (genetex.com)
  • The fact that kidney development involves several morphogenetic processes (e.g., cell aggregation, cell movement, mesenchymal-epithelial conversion, cell sorting, and cell shape changes) that members of the classic cadherin superfamily of cell adhesion molecules have been implicated in validates studies of cadherin function during kidney organogenesis. (asm.org)
  • Cadherins are a class of type-1 transmembrane proteins, and they are dependent on calcium (Ca2+) ions to function, hence their name. (wikipedia.org)
  • Cell-cell adhesion is mediated by extracellular cadherin domains, whereas the intracellular cytoplasmic tail associates with numerous adaptors and signaling proteins, collectively referred as the cadherin adhesome. (wikipedia.org)
  • The intracellular portion of classical cadherins has regulatory proteins that helps the cadherins joining the actin cytoskeleton. (wikipedia.org)
  • Cadherins are synthesized as polypeptides and undergo many post-translational modifications to become the proteins which mediate cell-cell adhesion and recognition. (wikipedia.org)
  • Exact signaling partners and adapter proteins for T-cadherin remain to be elucidated. (wikipedia.org)
  • It is likely that T-cadherin regulates cell migration and phenotype via activation of small G-proteins with subsequent actin reorganization. (wikipedia.org)
  • Cadherins are a group of proteins that help cells stick together. (news-medical.net)
  • E-cadherin, a 120 kDa molecule, is a prototypical member of the classical cadherin family of single-pass transmembrane proteins that mediate calcium-dependent cell-cell adhesion. (springer.com)
  • Cadherins are transmembrane proteins that mediate cell-cell adhesion in animals [ PMID: 22833291 ]. (ebi.ac.uk)
  • Cadherins are type I single membrane-spanning cell surface proteins that require free extracellular Ca 2+ for homophilic interaction of their N-terminal extracellular domains with cadherins of adjoining cells ( 4 ). (pnas.org)
  • In animals, cadherin domain-containing proteins are adhesion molecules that modulate a wide variety of processes including cell polarization and migration but they have also been identified in yeast and magnetotactic bacteria. (ebi.ac.uk)
  • Cadherin-like domains in alpha-dystroglycan, alpha/epsilon-sarcoglycan and yeast and bacterial proteins. (ebi.ac.uk)
  • This review highlights recent findings, which demonstrate that protein complexes associated with classical cadherins, the principal architectural proteins at cell-cell junctions in all soft tissues, are mechanosensors. (nih.gov)
  • Cadherin cell-adhesion proteins mediate many facets of tissue morphogenesis. (nih.gov)
  • Signal-transduction pathways impinge on the catenins (cytoplasmic cadherin-associated proteins), which transduce changes across the membrane to alter the state of the cadherin adhesive bond. (nih.gov)
  • It appears that the transmission of forces from cellular domains occupied by E-cadherin to F-actin filaments is regulated by the intracellular recruitment and accumulation of a number of effector proteins at sites of cell-cell adhesion ( 27 , 28 ). (diabetesjournals.org)
  • This antibody recognizes members of the Cadherin family of proteins including E-cadherin, N-cadherin, P-cadherin and R-cadherin. (abcam.com)
  • N-cadherin possesses a single transmembrane domain with an intracellular tail region through which it is associated with a family of proteins, the catenins, that enable it to function in multiple signaling pathways ( Arikkath and Reichardt, 2008 ). (rupress.org)
  • Cadherins are calcium-dependent cell adhesion proteins. (uniprot.org)
  • Cadherins are a family of Ca2+-dependent cell-cell adhesion proteins with a precise spatio-temporal pattern during embryonic development. (csic.es)
  • Catenins have been identified as cytoplasmic anchorage proteins for cadherins. (uninet.edu)
  • N-cadherin's function is dependent on its association with the actin-cytoskeleton and is mediated through interactions between the C-terminal region of N-cadherin and the cytoplasmic catenin proteins. (thermofisher.com)
  • However, strand-swapping sequence signatures are absent from nonclassical cadherins, raising the question of how these proteins function in adhesion. (mdc-berlin.de)
  • Additionally we are shipping N-Cadherin Antibodies (429) and N-Cadherin Proteins (25) and many more products for this protein. (antibodies-online.com)
  • Additionally we are shipping Cadherin 13 Kits (16) and Cadherin 13 Proteins (8) and many more products for this protein. (antibodies-online.com)
  • Cadherins are cell-cell adhesion proteins which form part of multiprotein complexes at the cell membrane to bind neighboring cells and determine the tissue architecture. (redorbit.com)
  • The cytoplasmatic tail of the E-cadherin molecule binds to the proteins of the catenin family: p120-catenin, beta-catenin, and beta-catenin. (redorbit.com)
  • The cytoplasmic domain of E-cadherin is reported to interact with a range of intracellular proteins including erbin, ezrin, caspase-3, caspase-8, β-catenin, presenilin 1, and casein kinase II. (stemcell.com)
  • The results showed that epithelial E-cadherin expression is reduced and c-Met expression is increased as lip carcinogenesis progresses, suggesting that these proteins may be useful markers of malignant transformation. (scielo.cl)
  • Cadherins, NPRAP, GRIP, and GluR2 copurified in the fractionation of synaptosomes and the postsynaptic density, two fractions enriched in synaptic proteins. (jneurosci.org)
  • Thus, the interaction of scaffolding proteins with cadherin-NPRAP complexes may anchor diverse signaling and adhesion molecules at cadherins. (jneurosci.org)
  • Cadherins are a family of proteins that mediate calcium dependent cell-cell adhesion. (embl.de)
  • Cadherins are a group of proteins that mediate calcium dependent cell-cell adhesion. (embl.de)
  • There are 1917 Cadherin_pro domains in 1912 proteins in SMART's nrdb database. (embl.de)
  • Taxonomic distribution of proteins containing Cadherin_pro domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with Cadherin_pro domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing Cadherin_pro domain in the selected taxonomic class. (embl.de)
  • The classic cadherins contain a highly conserved cytoplasmic domain that interacts with a family of cytoplasmic proteins called catenins: α-catenin, β-catenin, plakoglobin, and p120 ( 30 , 31 , 36 , 41 ). (asm.org)
  • Searching for proteins that could be involved in VE-cadherin signaling, we found the cytosolic C-terminal Src kinase (Csk), a negative regulator of Src family kinases. (diva-portal.org)
  • VE-cadherin recruits Csk to cell contacts and both proteins can be co-precipitated from cell lysates of transfected cells and endothelial cells. (diva-portal.org)
  • Reduced expression or absence of E-cadherin in addition to alpha, beta and gamma-catenin in primary breast carcinomas has also been reported and these four proteins are associated with the development of metastases. (leicabiosystems.com)
  • Each cadherin has a small C-terminal cytoplasmic component, a transmembrane component, and the remaining bulk of the protein is extra-cellular (outside the cell). (wikipedia.org)
  • Once the cell-cell adhesion between cadherins present in the cell membranes of two different cells has formed, adherens junctions can then be made when protein complexes, usually composed of α-, β-, and γ-catenins, bind to the cytoplasmic portion of the cadherin. (wikipedia.org)
  • The external domain of a cadherin molecule - the part that is on the outside of a cell - is made up of many repeats of the same protein chain. (news-medical.net)
  • Researchers at the Johns Hopkins Kimmel Cancer Center discovered that a cell adhesion protein, E-cadherin, allows breast cancer cells to survive as they travel through the body and form new tumors, a process termed metastasis. (news-medical.net)
  • A VE-cadherin-Fc fusion protein was generated by placing a cDNA fragment coding for the complete extracellular part of mouse VE-cadherin, including the membrane proximal glutamine, in front of a cDNA fragment coding for the Fc part of human IgG1, including the hinge region and Ig domains CH2 and CH3. (pnas.org)
  • The secreted VE-cadherin-Fc chimera were purified from the culture supernatants of stably transfected Chinese hamster ovary (CHO) cells by affinity chromatography using protein A agarose. (pnas.org)
  • CD144, also called Cadherin 5, CDH5 or VE-Cadherin is a 140 kDa protein belonging to the cadherin family of cell adhesion molecules which interact homophilically in trans and form lateral interactions in cis. (beckman.com)
  • The authors used an elegant approach in which recombinant E-, N-, or P-cadherin ectodomains fused to the Fc of immunoglobulin (E-cad/Fc, N-cad/Fc, or P-cad/Fc) were used for protein mimicry to support islet cell attachment ( Fig. 1 ). (diabetesjournals.org)
  • In adhesion junctions cadherins are bound to beta and gamma catenins which in turn bind to alpha catenin, an actin binding protein. (abcam.com)
  • E-cadherin (uvomorulin) recombinant protein (4). (agilent.com)
  • Beta-catenin is a cytosolic, 88 kDa intracellular protein associated with cell surface cadherin glycoproteins. (novusbio.com)
  • These data support the notion that Dsg2 is a pro-proliferative cadherin family member, and that interfering with the expression and/or function of this protein may be a viable strategy to impair cancer cell growth. (nature.com)
  • Reduction of IQGAP1 induced an increase and a decrease, respectively, in the protein levels of VE-cadherin and N-cadherin. (cdc.gov)
  • These findings suggest that a reduction of IQGAP1 positively influences the endothelial barrier by increasing the protein level of VE-cadherin and the interaction of VE-cadherin with the actin cytoskeleton. (cdc.gov)
  • The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail . (wikidoc.org)
  • Functioning as a classic cadherin by imparting to cells the ability to adhere in a homophilic manner, the protein may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. (wikidoc.org)
  • The E-cadherin/catenin complex is a substrate of receptor tyrosine kinases e.g. c-erbB-2, c-met, EGFR, of non-receptor tyrosine kinases e.g. src, of receptor protein tyrosine phosphatases and of MUC-1 (episialin). (uninet.edu)
  • In normal cells, β-catenin is associated not only with cadherins but also with the APC (adenomatous polyposis coli) multi-protein complex. (uninet.edu)
  • The central player is β-catenin, which is a transcription cofactor with T cell factor/lymphoid enhancer factor TCF/LEF in the Wnt pathway ( 2 ) and a structural adaptor protein linking cadherins to the actin cytoskeleton in cell-cell adhesion ( 5 ). (sciencemag.org)
  • Here, we revisit and review the functions, phylogenetic classifications and co-evolution of the cadherin and catenin protein families. (ovid.com)
  • A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human M-Cadherin/Cadherin-15. (fishersci.com)
  • The M-Cadherin/Cadherin-15 Recombinant Protein Antigen has been validated for the following applications: Antibody Competition. (fishersci.com)
  • Zusätzlich bieten wir Ihnen E-cadherin Kits (84) und E-cadherin Proteine (37) und viele weitere Produktgruppen zu diesem Protein an. (antikoerper-online.de)
  • IFN-γ acts pathogenic by causing a breakdown of the vascular barrier through disruption of the adherens junction protein VE-cadherin. (jci.org)
  • Whereas the disruption of cell-cell contacts alone does not enable metastasis, the loss of E-cadherin protein does, through induction of an epithelial-to-mesenchymal transition, invasiveness, and anoikis resistance. (broadinstitute.org)
  • cadherin 2 (CDH2 ) and CDH4 (show CDH4 ELISA Kits ) cooperate to regulate radial migration in mouse brain via the protein tyrosine phosphatase 1B (PTP1B (show PTPN1 ELISA Kits )) and alpha- and beta-catenins. (antibodies-online.com)
  • In this process there are multiple protein-complexes involved which interact with beta-catenin and E-cadherin. (redorbit.com)
  • Of particular interest is E-cadherin, sometimes considered as a tumor suppressor protein due to its functionality in maintaining the compactness of the epithelium. (redorbit.com)
  • Greater than 80% of colorectal tumors show malfunctions in APC, a key protein in the wnt-pathway related also to intracellular interactions where E-cadherin plays a main role. (redorbit.com)
  • Signaling molecules such as Notch, TGF-β, estrogen receptors, EGF and Wnt initiate numerous signaling cascades via these vital factors of cell programming, controlling expression of E-cadherin at transcriptional (mRNA) and protein level. (eurekaselect.com)
  • NPRAP is an ARM repeat protein that binds to the juxtamembrane region of the cadherin intracellular domain. (jneurosci.org)
  • Cadherin-E protein (100µg/1ml) in 50mM Tris-HCl, pH7.5 and 10mM L-glutathione (reduced). (prospecbio.com)
  • Drosophila fat protein [ 3 ], a huge protein of over 5000 amino acids that contains 34 cadherin-like repeats in its extracellular domain. (expasy.org)
  • The top arrow indicates the full length E-Cadherin protein. (biolegend.com)
  • Human CD324 (E-cadherin) is a 882 amino acid protein with a predicted molecular mass of 97 kD and observed molecular mass of ~120 kD. (biolegend.com)
  • P-cadherin is a transmembrane protein included in the classical cadherin family, with an ectodomain containing 5 cadherin repeats (which interacts with another cadherin's ectodomain in a cis or trans manner) and a highly conserved cytoplasmic domain that binds to catenins. (atlasgeneticsoncology.org)
  • Sixty-four genes, including Nkx3.1 and probasin, and 65 other genes, including insulin-like growth factor binding protein 3 and H-cadherin (H-Cad), were further identified respectively as androgen-responsive genes and genes inversely correlated with androgen, based on their down- or up-regulation following castration and up- or down-regulation following androgen replacement. (wiley.com)
  • Cadherin-7 Polyclonal Antibody detects endogenous levels of Cadherin-7 protein. (genetex.com)
  • It is a single pass type I membrane protein that contains 27 cadherin domains. (acris-antibodies.com)
  • Recombinant protein encompassing a sequence within the center region of human E-Cadherin. (genetex.com)
  • E-Cadherin antibody [GT358] detects E-Cadherin protein at cell membrane by immunofluorescent analysis. (genetex.com)
  • Green: E-Cadherin protein stained by E-Cadherin antibody [GT358] (GTX629694) diluted at 1:500. (genetex.com)
  • E-cadherin antibody [GT358] detects E-cadherin protein by Western blot analysis. (genetex.com)
  • This assay employs an antibody specific for mouse E-Cadherin coated on a 96- well plate. (abcam.com)
  • Standards and samples are pipetted into the wells and E-Cadherin present in a sample is bound to the wells by the immobilized antibody. (abcam.com)
  • The wells are washed and biotinylated anti-mouse E-Cadherin antibody is added. (abcam.com)
  • Each Cadherin-6/KCAD Antibody is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • Choose from our Cadherin-6/KCAD polyclonal antibodies and browse our Cadherin-6/KCAD monoclonal antibody catalog. (novusbio.com)
  • Cadherin-16 Polyclonal antibody specifically detects Cadherin-16 in Human samples. (fishersci.com)
  • The following antibody was used in this experiment: Pan-cadherin Polyclonal Antibody from Thermo Fisher Scientific, catalog # PA5-16481, RRID AB_10981183. (thermofisher.com)
  • The DECMA-1 antibody recognizes E-cadherin, a calcium-dependent transmembrane glycoprotein involved in cell-cell adhesion, bacterial pathogenesis, and tumor invasion. (stemcell.com)
  • The E-cadherin antibody is often used as a neutralizing antibody to inhibit E-cadherin-mediated cell-cell interactions. (stemcell.com)
  • The cells were labeled with Anti-Mouse E-Cadherin (CD324) Antibody, Clone DECMA-1, followed by a donkey anti-mouse IgG antibody, Alexa Fluor® 488, and counterstained with DAPI. (stemcell.com)
  • B) Flow cytometry analysis of MDCK epithelial cells labeled with Anti-Mouse E-Cadherin (CD324) Antibody, Clone DECMA-1, followed by an anti-rat IgG1 antibody, PE (filled histogram) or Rat IgG1, kappa Isotype Control Antibody, Clone RTK2071 (Catalog #60075), followed by an anti-rat IgG1 antibody, PE (dotted line histogram). (stemcell.com)
  • The present study examined E-cadherin expression in normal salivary glands, pleomorphic adenoma, Warthin's tumor, mucoepidermoid carcinoma, acinic cell carcinoma, adenoid cystic carcinoma and adenocarcinoma of salivary glands in paraffin sections using a monoclonal antibody (5H9). (nii.ac.jp)
  • This antibody is expected to exhibit the same species cross-reactivity as the unconjugated E-Cadherin (4A2) Mouse mAb #14472. (cellsignal.com)
  • The goal of this Development Candidate project is to identify a human or humanized antibody targeting N-cadherin as a potential therapy to target castration-resistant prostate cancer and prostate cancer stem cells. (ca.gov)
  • Western blot of purified anti-CD324 (E-Cadherin) antibody (clone 4A2). (biolegend.com)
  • Western Blot (WB) analysis of specific cells using Cadherin-7 Polyclonal Antibody. (genetex.com)
  • Non-transfected (-) and transfected (+) MCF-7 whole cell extracts (30 µg) were separated by 5% SDS-PAGE, and the membrane was blotted with E-Cadherin antibody [GT358] (GTX629694) diluted at 1:500. (genetex.com)
  • Monoclonal antibodies have been used to remove cadherins in cultured epithelial cells, and those cells fall apart. (news-medical.net)
  • In a recent study, human breast cancer tissues were stained immunohistochemistry (IHC) by anti- E-Cadherin antibodies. (novusbio.com)
  • VE-cadherin is known to be required for maintaining a restrictive endothelial barrier - early studies using blocking antibodies to VE-cadherin increased monolayer permeability in cultured cells [3] and resulted in interstitial edema and hemorrhage in vivo. (wikidoc.org)
  • Our Cadherin-6/KCAD Antibodies can be used in a variety of model species: Human, Rat. (novusbio.com)
  • The cases were studied immunohistochemically, using specific monoclonal antibodies against E-cadherin, α-catenin, β-catenin, γ-catenin and p120 CTN . (uninet.edu)
  • Inhibition of the cadherin activity with antibodies induces dissociation of cell layers, indicating a fundamental importance of these molecules in maintaining the multicellular structure. (biologists.org)
  • Antibodies to cadherins were shown to perturb the morphogenesis of some embryonic organs in vitro. (biologists.org)
  • Using conformation specific antibodies I show that Trp2 integrates into the domain fold of its own cadherin molecule in physiological conditions, but that this integration is not stable owing to structural constraints imposed by calcium binding to the cadherin. (bl.uk)
  • On www.antibodies-online.com are 56 Cadherin 2 (CDH2) ELISA Kits from 13 different suppliers available. (antibodies-online.com)
  • On www.antibodies-online.com are 191 Cadherin 13 (CDH13) Antibodies from 25 different suppliers available. (antibodies-online.com)
  • Availability of these monoclonal antibodies to human P- and E-cadherin allowed us to examine their distributions in human tissues immunohistochemically. (aacrjournals.org)
  • We therefore developed antibodies against N-cadherin, which are able to inhibit growth, metastasis and progression of prostate cancers in vivo. (ca.gov)
  • ABSTRACT In this article, we show, using a mathematical multiscale model, how cell adhesion may be regulated by interactions between E-cadherin and beta-catenin and how the control of cell adhesion may be related to cell migration, to the epithelial- mesenchymal transition and to invasion in populations of eukaryotic cells. (redorbit.com)
  • E-cadherin is the main adhesion molecule of the adherens junctions of epithelial cells, and via catenins it is linked to the underlying actin cytoskeleton. (springer.com)
  • We specifically explored whether CDH26 has functional cadherin domains that regulate the actin cytoskeleton and the apicobasal polarity of AECs. (nature.com)
  • α-Catenin is believed to link the classical cadherins to the actin cytoskeleton by binding to β-catenin. (biologists.org)
  • It has long been recognized that the biology of E-cadherin arises from cooperation between adhesion and the actin cytoskeleton. (dovepress.com)
  • Indeed, it has long been appreciated that biochemical and functional links with the actin cytoskeleton play a vital role in cadherin biology. (dovepress.com)
  • Cadherins function as membrane receptors mediating outside-in signals, activating small GTPases and beta-catenin/Wnt pathway, and resulting in dynamic cytoskeleton reorganization and changes in the phenotype. (wikipedia.org)
  • β-catenin interacts with α-catenin, which in turn binds to actin filaments linking cadherins to the cytoskeleton. (nih.gov)
  • E- cadherins bind to beta-catenin to form a complex which can interact both with neighboring cells to form bonds, and with the cytoskeleton of the cell. (redorbit.com)
  • The alpha- catenin and beta-catenin then form a complex to link the actin filaments of the cytoskeleton and the E-cadherins. (redorbit.com)
  • Catenins have a dual role, acting as signalling mediators or as adaptor molecules that stabilize the cadherin complex at the membrane and link the cadherin molecule to the actin filaments of the cytoskeleton (Wheelock et al. (atlasgeneticsoncology.org)
  • Binding of p-120 catenin and β {\displaystyle \beta } -catenin to the homodimer increases the stability of the classical cadherin. (wikipedia.org)
  • This study shows that neural (N)-cadherin and β-catenin, an intracellular binding partner for the classic cadherins, are present in axons and dendrites before synapse formation and then cluster at developing synapses between hippocampal neurons. (jneurosci.org)
  • Sites of GABAergic, inhibitory synapses in mature cultures therefore lack N-cadherin but are associated with clusters of β-catenin, implying that they contain a different classic cadherin. (jneurosci.org)
  • Figure: This image depicts the ornamental braiding (Pan Kou) for fastening the front of traditional Chinese clothing in watercolor, as an analogy of how cadherin/catenin complexes regulate the synapse maturation. (eurekalert.org)
  • A recent study conducted by Dr. YU Xiang's lab at the Institute of Neuroscience of the Chinese Academy of Sciences uncovered an asymmetric role for symmetric cadherin/catenin cell adhesion complexes in functional synapse formation in the neocortex. (eurekalert.org)
  • Pre-synaptic β-catenin is predominant during functional synapse formation and mediates dendritic spine stabilization through N-cadherin-dependent anterograde trans-synaptic signaling. (eurekalert.org)
  • The effect of the cadherin/catenin complexes requires p140Cap, a novel β-catenin interacting partner. (eurekalert.org)
  • They showed the presence of cadherin/catenin/p140Cap complexes. (eurekalert.org)
  • These results uncovered an asymmetric role for the cadherin/catenin complex in neocortical circuit wiring -contrary to the earlier assumption of symmetry. (eurekalert.org)
  • In this subfamily, all cadherins have an ectodomain possessing five characteristic EC repeats, responsible for their Ca ++ -dependent cell affinity, a transmembrane domain, and a highly conserved cytoplasmic tail that anchors cadherins to the cell cortex through their association with p120 catenin, β-catenin, and α-catenin. (genetics.org)
  • They have five cadherin repeats and a highly conserved cytoplasmic region to which p120-catenin and β-catenin bind. (biologists.org)
  • for maintenance of normal intercellular adhesion, an intact E-cadherin/catenin complex is required. (uninet.edu)
  • The cytoplasmic domain of E-cadherin binds directly to either β-catenin or γ-catenin (also called plakoglobin). (uninet.edu)
  • The E-cadherin/catenin complex is implicated not only in cell-cell adhesion, but in directed migration during epithelial wound healing, presumably through contact inhibition of membrane ruffling. (uninet.edu)
  • Of the many growth factors involved in these events, Wnts are particularly interesting regulators, because a key component of their signaling pathway, β-catenin, also functions as a component of the cadherin complex, which controls cell-cell adhesion and influences cell migration. (sciencemag.org)
  • Here, we assemble evidence of possible interrelations between Wnt and other growth factor signaling, β-catenin functions, and cadherin-mediated adhesion. (sciencemag.org)
  • This review explores intriguing connections between Wnt and other growth factor signals, β-catenin distribution, and cadherin-mediated cell adhesion ( Fig. 1 , inset). (sciencemag.org)
  • The central role of β-catenin in Wnt signaling and the cadherin complex. (sciencemag.org)
  • The insert displays possible levels of interactions between Wnt signaling and cadherin-mediated adhesion (dotted lines) and the central role of β-catenin in both processes that are the focus of the review. (sciencemag.org)
  • In the absence of Wnt signaling, the level of β-catenin is kept low through degradation of (cytoplasmic) β-catenin that is in excess of binding sites, such as cadherins at the plasma membrane (see below). (sciencemag.org)
  • Further, α-catenin links the cadherin/armadillo catenin complex to the actin filament network. (ovid.com)
  • Moreover, a large expansion of the cadherin and catenin families coincides with the emergence of vertebrates and reflects a major functional diversification in higher metazoans. (ovid.com)
  • We find the E-cadherin binding partner beta-catenin to be necessary, but not sufficient, for induction of these phenotypes. (broadinstitute.org)
  • In laboratory models, downstream post-transcriptional modifiers such as TWIST and SNAIL contribute to the dissociation of the intracellular component of the cadherin-catenin complex (CCC), resulting in tumor progression and invasion. (springer.com)
  • Study demonstrates a critical role of presynaptic cadherin / catenin / p140Cap (show SRCIN1 ELISA Kits ) cell adhesion complexes in stabilizing functional synapses and spines in the developing neocortex. (antibodies-online.com)
  • The role of E- cadherin in the malfunction of cell-cell adhesion observed in colorectal cancer, and in the beta-catenin degradation system after mutations that affect the wnt-pathway, belong to the most studied examples (2-4). (redorbit.com)
  • Zhang B, Li M, McDonald T, Holyoake TL, Moon RT, Campana D, Shultz L, Bhatia R. Microenvironmental protection of CML stem and progenitor cells from tyrosine kinase inhibitors through N-cadherin and Wnt-ß-catenin signaling. (umassmed.edu)
  • Concerning CDH3/P-cadherin gene regulation, the main transcriptional activators described for the CDH3/P-cadherin gene promoter are β-catenin (Faraldo et al. (atlasgeneticsoncology.org)
  • There are multiple classes of cadherin molecules, each designated with a prefix (in general, noting the types of tissue with which it is associated). (wikipedia.org)
  • The distribution of T-cadherin on the cell membrane is restricted to lipid rafts where it co-localizes with signal-transducing molecules. (wikipedia.org)
  • Within the junctions, cadherin molecules on the cell surfaces hook onto each other, like a tiny piece of velcro. (news-medical.net)
  • Protocadherins are a large group of cadherin molecules present in a wide range of species that are thought to be related to an ancestral cadherin. (news-medical.net)
  • Aherens junctions have a strip of cadherin molecules that connect the membranes of epithelial cells. (news-medical.net)
  • In cellular monolayers that form permeability barriers, such as the simple epithelial lining of the intestine or the vascular endothelium covering the inner surface of blood vessels, adhesion between cells is mainly accomplished by Ca 2+ -dependent adhesion molecules named cadherins ( 1 , 2 ). (pnas.org)
  • 21 ). Over the past three decades, the function of cadherins in epithelia has evolved from simple cell-cell adhesion molecules that populate subcellular domains called "adherens junctions" to biochemical transducers of signaling processes that contribute to the development, homeostasis, and function of multiple tissues ( 22 - 24 ). (diabetesjournals.org)
  • One of the epithelial cell adhesion molecules, E Cadherin, plays an important role in the formation of cell-cell contacts in epithelia irrespective their origin form ecto-, meso- or endodermal tissue. (abcam.com)
  • Individual cadherin molecules are known to co-operate with each other to form a linear cell adhesion zipper. (abcam.com)
  • Cadherins are homophilic adhesion molecules that, together with their intracellular binding partners the catenins, mediate adhesion and signaling at a variety of intercellular junctions. (jneurosci.org)
  • Specifically, E-cadherin is an approximately 100 kDa epithelial cell glycoprotein whose extracellular domain interacts with that of other E-cadherin molecules on adjacent cells to establish cell-cell adhesion. (novusbio.com)
  • E-cadherin endocytosis is blocked by IQGAP1 unless actin filaments are disrupted by Lat-A. E-cadherin interacts with other E-cadherin molecules on neighboring cells to form cell-cell adhesions. (rupress.org)
  • E-cadherin that is not involved in these trans interactions is removed from the cell surface and replaced with newly synthesized molecules to maintain dynamic adhesions. (rupress.org)
  • Cadherins are cell adhesion molecules that regulate numerous adhesive interactions during embryonic development and adult life. (genetics.org)
  • Several classes of adhesion molecule are used to achieve this, and cadherins represent a major family of such molecules. (biologists.org)
  • Members of the Fat cadherin subfamily, which is conserved across species, have an extraordinarily large extracellular region, comprising 34 repeated domains, making them the largest cadherin molecules. (biologists.org)
  • The cadherins are a large family of adhesion molecules. (biologists.org)
  • The expression of such cell-cell adhesion molecules as E-cadherin and E-cadherin complex-associated catenins has not been investigated to date. (uninet.edu)
  • Adhesion by classical cadherins depends on binding interactions in their N-terminal EC1 domains, which swap N-terminal beta-strands between partner molecules from apposing cells. (mdc-berlin.de)
  • Newly synthesized N-cadherin molecules move from the lateral to the basal surface of cardiomyocytes during trabeculation. (antibodies-online.com)
  • When a cell adheres to adjacent neighbors, the E-cadherin molecules are situated in an intermembrane position, forming bonds with local neighbors at the intercellular space. (redorbit.com)
  • Moreover, immunohistochemical examination of 44 lung carcinomas showed that both molecules were coexpressed in all of them, and suggested that expression of P-cadherin was closely related to the differentiation of carcinoma cells. (aacrjournals.org)
  • Breast cancer, one of the leading causes of mortality and morbidity among females, is regulated in part by diverse classes of adhesion molecules one of which is known as cadherins. (eurekaselect.com)
  • P-cadherin is a transmembrane glycoprotein that belongs to a large family of molecules that mediate calcium-dependent homophilic cell-cell adhesion. (atlasgeneticsoncology.org)
  • Cells are linked together dynamically by adhesion molecules, such as the classical cadherins. (dovepress.com)
  • Immunoperoxidase staining for E-cadherin (HECD-1 clone, 1: 200 dilution, Zymed Laboratories, South San Francisco, Calif) was performed following heat-induced antigen retrieval, using the avidin-biotin peroxidase technique. (thefreelibrary.com)
  • Purified tryptic fragments of the antigen recognized by NCC-CAD-299 showed cross-reactivity with a rabbit antiserum against mouse P-cadherin, indicating that this molecule was the human homologue of P-cadherin. (aacrjournals.org)
  • On the other hand, the antigen recognized by HECD-1 showed essentially the same tissue distribution pattern as E-cadherin in the mouse, suggesting that this molecule is the human homologue of E-cadherin. (aacrjournals.org)
  • In structure, they share cadherin repeats, which are the extracellular Ca2+-binding domains. (wikipedia.org)
  • Because cadherins are Ca2+ dependent, they have five tandem extracellular domain repeats that act as the binding site for Ca2+ ions. (wikipedia.org)
  • They all have a similar structure, with five extracellular cadherin repeats, a transmembrane domain, and an intracellular domain. (news-medical.net)
  • In general, classical cadherins exert their effect by homophilic interactions via their five characteristic extracellular (EC) repeats. (genetics.org)
  • They can have 5-27 cadherin repeats. (biologists.org)
  • Dachsous is a large cadherin molecule that has 27 cadherin repeats. (biologists.org)
  • They commonly have 34 cadherin repeats, one or two laminin A-G domains and several epidermal growth factor (EGF) motifs in their extracellular regions. (biologists.org)
  • The extracellular region of E-cadherin is composed of multiple cadherin repeats that contain calcium-binding motifs. (stemcell.com)
  • It is suggested that the calcium-binding region of cadherins is located in the extracellular repeats. (expasy.org)
  • A gene on chromosome 16q22.1 that encodes a calcium-dependent cell-cell adhesion glycoprotein (cadherin), which is involved in regulating cell-cell adhesions, mobility and proliferation of epithelial cells. (thefreedictionary.com)
  • A gene on chromosome 16q24.3 that encodes a cadherin expressed in myoblasts and upregulated in myotubule-forming cells. (thefreedictionary.com)
  • Even genomes of ancestral metazoan species such as cnidarians and placozoans encode a limited number of distinct cadherins and catenins, emphasizing the conservation and functional importance of these gene families. (ovid.com)
  • In addition, gene expression analysis shows that E-cadherin loss results in the induction of multiple transcription factors, at least one of which, Twist, is necessary for E-cadherin loss-induced metastasis. (broadinstitute.org)
  • The single nucleotide polymorphisms (SNPs) rs12596316AG genotype of the T-cadherin (CDH13 ) gene is associated with the susceptibility to metabolic syndrome (MS) among ethnic Han Chinese. (antibodies-online.com)
  • Aberration in gene expression of cadherins can be either due to somatic or epigenetic silencing or via transcriptional factors. (eurekaselect.com)
  • Localization of CDH3 gene (P-cadherin). (atlasgeneticsoncology.org)
  • 2009). It was also demonstrated that ER can indirectly repress P-cadherin expression by promoting epigenetic changes in the CDH3 gene promoter (Paredes et al. (atlasgeneticsoncology.org)
  • OB-cadherin gene silencers are available as OB-cadherin CRISPR/Cas9 Knockout plasmids and OB-cadherin Double Nickase Plasmids. (scbt.com)
  • OB-cadherin CRISPR/dCas9 Activation Plasmids and CRISPR Lenti Activation Systems for gene activation are also available. (scbt.com)
  • Defects in the gene encoding Cadherin like 23 are a cause of Usher syndrome, which is characterised by profound congenital sensorineural deafness and eventual blindness. (acris-antibodies.com)
  • In addition to E-cadherin's role in the formation of epithelium, N-cadherin is important in neural tissue and muscle, R-cadherin is used in brain and bone tissue, P-cadherin is present in skin, and VE-cadherin is also significant in the epithelium. (news-medical.net)
  • Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). (harvard.edu)
  • N-cadherin -null enteric neural crest cells do not respond to C3a (show C3 ELISA Kits ) co-attraction. (antibodies-online.com)
  • Knock-down of ZBED6 in insulin (show INS ELISA Kits )-producing cells promotes N-cadherin junctions between beta-cells and neural crest stem cells in vitro. (antibodies-online.com)
  • Neural (N-cadherin) (CDH2). (expasy.org)
  • Conditional loss of E-cadherin in mouse brain causes defects in the self-renewal of neural stem cells both in vivo and in vitro . (biolegend.com)
  • Overexpression of E-cadherin increases the number of neural stem cell colonies indicating that E-cadherin is required for the neural stem cell self-renewal function. (biolegend.com)
  • Structure of the neural (N-) cadherin prodomain reveals a cadherinextracellular domain-like fold without adhesive characteristics. (embl.de)
  • Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that are important in the formation of adherens junctions to bind cells with each other. (wikipedia.org)
  • Cadherins are named for calcium dependent adhesion . (news-medical.net)
  • Cadherins are members of a multigene family of single chain glycoprotein receptors mediating calcium dependent cell-cell adhesion. (abcam.com)
  • Cadherins are a large family of transmembrane glycoproteins, that mediate calcium-dependent cell-cell adhesion in normal epithelial cells and play essential role in development, establishment and maintenance of cell polarity and tissue architecture. (uninet.edu)
  • E-cadherin is a calcium dependent cell adhesion molecule, important in cell to cell interactions in epithelial tissues. (nii.ac.jp)
  • Cadherin-2 isoform 1, also known as CDH2 is a transmembrane, homophilic glycoprotein which belongs to the calcium-dependent cell adhesion molecule family. (prospecbio.com)
  • E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. (prospecbio.com)
  • E-cadherin is a calcium-dependent cell adhesion molecule (CAM) critical for formation and functions of adherent junctions during development and tumorigenesis. (biolegend.com)
  • Cadherin like 23 (or Cadherin 23) is, like other members of the cadherin family, a calcium-dependent cell adhesion glycoprotein that preferentially interacts with itself in connecting cells. (acris-antibodies.com)
  • Cadherin-16 (CDH16) or kidney-specific (Kps) cadherin was first described as a kidney-specific adhesion molecule [ PMID: 15886705 ] and thereafter also found expressed in the thyroid gland. (ebi.ac.uk)
  • Single molecule atomic force microscopy was used to characterize structure, binding strength (unbinding force), and binding kinetics of a classical cadherin, vascular endothelial (VE)-cadherin, secreted by transfected Chinese hamster ovary cells as cis-dimerized full-length external domain fused to Fc-portion of human IgG. (pnas.org)
  • In physiological buffer, the external domain of VE-cadherin dimers is a ≈20-nm-long rod-shaped molecule that collapses and dissociates into monomers (V-shaped structures) in the absence of Ca 2+ . (pnas.org)
  • The cadherin 5 molecule may play a role in the permeability properties of vascular endothelium. (beckman.com)
  • Furthermore, E Cadherin plays a crucial role in the maintenance of the epithelial junctional complex and is as such an important molecule in maintaining epithelial integrity. (abcam.com)
  • E (epithelial)-cadherin is a 120 kDa transmembrane cell adhesion molecule. (agilent.com)
  • E-cadherin is a calcium-regulated adhesion molecule expressed in most normal epithelial tissues. (novusbio.com)
  • doi:10.1083/jcb.201003007) demonstrate a pivotal role for the cell adhesion molecule N-cadherin in activity-mediated spine stabilization, offering a new mechanism for how spine dynamics and stability are regulated by activity in central neurons. (rupress.org)
  • provide support for this idea by showing that N-cadherin, a transsynaptic cell adhesion molecule, regulates activity-mediated stabilization of spines in hippocampal neurons. (rupress.org)
  • E-cadherin is a potent adherens junction molecule implicated in tissue morphogenesis, epithelial functioning, and immune regulation. (diva-portal.org)
  • Structural studies have shown Trp2 to be integrated into its own cadherin domain, integrated into the domain an opposing cadherin molecule, or freed from the domain and exposed to solvent. (bl.uk)
  • Loss of the epithelial adhesion molecule E-cadherin is thought to enable metastasis by disrupting intercellular contacts-an early step in metastatic dissemination. (broadinstitute.org)
  • E-cadherin (E-cad) is an adhesion molecule associated with tumor invasion and metastasis. (aacrjournals.org)
  • The loss of the intercellular adhesion molecule E-cadherin is a hallmark of the epithelial-mesenchymal transition (EMT), which promotes a transition of cancer cells to a migratory and invasive phenotype. (biorxiv.org)
  • SUMMARY E-cadherin, an extensively studied transmembrane molecule ubiquitously expressed in normal epithelial tissues, promotes and maintains intercellular adhesion. (biorxiv.org)
  • In cancer, the loss of adhesion molecule E-cadherin is associated with onset of invasion via epithelial-to-mesenchymal transition (EMT) process. (biorxiv.org)
  • Moreover, the expression of intercellular adhesion molecule E-cadherin (E-cad) is associated with a decrease in cell proliferation in normal cells. (biorxiv.org)
  • Image of a classical type I cadherin, adapted with permission from the RCSB PDB March 2008 Molecule of the Month feature by David Goodsell (doi: 10.2210/rcsb_pdb/mom_2008_3). (atlasgeneticsoncology.org)
  • Described for the first time in 1986, as "a novel class of cadherin that appeared in developing mouse embryos", this adhesion molecule was found in the tissues that gave rise to its name, the placenta (Nose and Takeichi, 1986). (atlasgeneticsoncology.org)
  • E-cadherin is a Ca 2+ -dependent, transmembrane cell adhesion molecule. (leicabiosystems.com)
  • In this review, we summarize the functions of E-cadherin and the signaling pathways it regulates. (hindawi.com)
  • Fbxo45 Binds SPRY Motifs in the Extracellular Domain of N-Cadherin and Regulates Neuron Migration during Brain Development. (harvard.edu)
  • Islet β-cell adhesion to recombinant Fc-cadherins emulates cell-cell interactions and positively regulates glucose-dependent insulin secretion. (diabetesjournals.org)
  • C3a (show C3 ELISA Kits ) regulates cell migration in a N-cadherin -dependent process. (antibodies-online.com)
  • The predominant cadherin of most epithelia is E-cadherin, whereas endothelial cells adhere to each other by vascular endothelial-cadherin (VE-cadherin) ( 3 ). (pnas.org)
  • VE-cadherin is the major component of endothelial adherens junctions and is specific to endothelial cells. (beckman.com)
  • Reduction of IQGAP1 increases insoluble VE-cadherin at endothelial adherens junctions. (cdc.gov)
  • In human umbilical vein endothelial cells (HUVECs), soluble IQGAP1 associated with VE-cadherin and the catenins, b, y, and a, but not N-cadherin. (cdc.gov)
  • Cadherin 5, type 2 or VE-cadherin (vascular endothelial cadherin) also known as CD144 ( C luster of D ifferentiation 144 ), is a type of cadherin . (wikidoc.org)
  • Deubiquitinase function of A20 was shown to remove ubiquitin chains from VE-cadherin, thereby prevented loss of VE-cadherin expression at the endothelial adherens junctions. (wikidoc.org)
  • Vascular endothelial (VE-cadherin) (CDH5). (expasy.org)
  • Vascular endothelial cadherin (VE-cadherin) mediates contact inhibition of cell growth in quiescent endothelial cell layers. (diva-portal.org)
  • Association of VE-cadherin and Csk in endothelial cells increased with increasing cell density. (diva-portal.org)
  • Most cancers arise from epithelial tissue, and in those cancers, cell adhesion mediated by E-cadherin is lost at the same time that a tumor progresses toward malignancy. (news-medical.net)
  • E-cadherin has been reported to be a tumor suppressor and to be down regulated in gastric cancer. (hindawi.com)
  • Cadherins play an important part in tumor invasion and metastasis. (abcam.com)
  • In this study we show that loss of the other intestinal desmosomal cadherin, desmoglein-2 (Dsg2) that pairs with Dsc2, results in decreased epithelial cell proliferation and suppressed xenograft tumor growth in mice. (nature.com)
  • Tumor invasion and metastasis are partly regulated by a switch from epithelial to mesenchymal cadherins in the transformed epithelium. (aacrjournals.org)
  • Thus, interactions of cadherins with their roles in tumor suppression and oncogenic transformation can be beneficial in providing valuable insights for breast cancer diagnosis and therapeutics development. (eurekaselect.com)
  • E-cadherin expression dramatically increases tumor growth and, without affecting the ability of cells to extravasate and colonize the lung, significantly increases macrometastasis formation via cell proliferation at the distant site. (biorxiv.org)
  • Pharmacological inhibition of MEK1/2, blocking phosphorylation of ERK in E-cadherin-expressing cells, significantly depresses both tumor growth and macrometastasis. (biorxiv.org)
  • This work suggests a novel role of E-cadherin in tumor progression and identifies a potential new target to treat hyper-proliferative breast tumors. (biorxiv.org)
  • Cleavage of E-cadherin usually occurs in tumor development and cleaved E-cadherin fragments of ~29-38 kD often possess distinct oncogenic properties. (biolegend.com)
  • Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body. (harvard.edu)
  • It has been suggested that cadherins bind cells by their homophilic interactions at the extracellular domain and are associated with actin bundles at the cytoplasmic domain. (biologists.org)
  • Our findings reveal the likely molecular architecture of the T-cadherin homophilic interface and its requirement for axon outgrowth regulation. (mdc-berlin.de)
  • Cadherins are Ca 2+ -dependent homophilic synaptic CAMs that contribute to spine morphogenesis and synapse assembly and regulation (for review, see Takeichi and Abe, 2005 ). (jneurosci.org)
  • Cadherins cluster to form foci of homophilic binding units. (embl.de)
  • Cadherins mediate cell-cell binding in a homophilic manner, contributing to the sorting of heterogeneous cell types and the maintenance of orderly structures. (genetex.com)
  • In confluent cultures of vascular cells, T-cadherin was distributed equally over the entire cell surface, in contrast to VE-cadherin, which was restricted to the cell junctions. (wikipedia.org)
  • The best characterized cadherins are the vertebrate 'classical' cadherins, which mediate adhesion via trans homodimerization between their membrane-distal EC1 domains that extend from apposed cells, and assemble intercellular adherens junctions through cis clustering. (nih.gov)
  • As a result, cells that are in contact with each other through cadherin-mediated junctions sense tension forces that are directly proportional to the degree of actin-anchored cadherin adhesions. (diabetesjournals.org)
  • C ) Confocal microscopic images of cadherin-11 expression (green) at adherens junctions on day-2 ex vivo SVF cell cultures. (jci.org)
  • Furthermore, more insoluble (actin-associated) VE-cadherin was localized at intercellular junctions and less insoluble N-cadherin was present in the cell. (cdc.gov)
  • Integrity of intercellular junctions is a major determinant of permeability of the endothelium , and the VE-cadherin-based adherens junction is thought to be particularly important. (wikidoc.org)
  • Treatment with imatinib restored VE-cadherin/adherens junctions, inhibited vascular permeability, and significantly reduced colonic inflammation in experimental colitis. (jci.org)
  • Exogenous NPRAP that was bound to cadherins at adherens junctions of Madin-Darby canine kidney cells recruited ABP from the cytosol to form cadherin-NPRAP-ABP complexes, dependent on NPRAP interaction with the ABP PDZ domain 2. (jneurosci.org)
  • Here we discuss recent developments in understanding how cadherin junctions integrate signaling and cytoskeletal dynamics to sense and generate force. (dovepress.com)
  • Here an important advance has been the realization that cadherin junctions and their cytoskeletons provide an apparatus for force to be generated and resisted at cell-cell junctions. (dovepress.com)
  • Here we discuss some advances in our understanding of the functional architecture of E-cadherin-cytoskeletal cooperation, considering their dynamic properties together with their role in the mechanobiology of junctions. (dovepress.com)
  • One current model proposes that cells distinguish cadherin subtypes based on kinetic specificity rather than thermodynamic specificity, as different types of cadherin homotypic bonds have different lifetimes. (wikipedia.org)
  • The EC1 domains of type I and type II cadherins appear to encode cell adhesive specificity in vitro. (rcsb.org)
  • Moreover, perturbation of motor neuron segregation with chimeric cadherins depends on EC1 domain identity, suggesting that this region, which includes the structurally defined adhesive interface, encodes type II cadherin functional specificity in vivo. (rcsb.org)
  • These results suggest that differential cadherin expression may orchestrate the point-to-point specificity displayed by developing synapses. (jneurosci.org)
  • synaptic specificity is generated by the differential expression and distribution of cadherins. (jneurosci.org)
  • It appears that each cadherin subclass has binding specificity and this molecular family is involved in selective cell-cell adhesion. (biologists.org)
  • Elementary trans-interactions observed between strand dimers revealed Ca 2+ -dependent highly specific molecular recognition properties that provide a basis for modeling cadherin-mediated intercellular adhesion. (pnas.org)
  • Activation of metalloproteinases by EphB-ephrin-B interactions alters cell affinity by inducing localized cleavage of E-cadherin. (sciencemag.org)
  • page 237 ) show that E-cadherins that are involved in trans interactions are excused from this endocytosis by small GTPases. (rupress.org)
  • E-cadherins engaged in trans interactions, however, activated Rac and Cdc42, which blocked their internalization. (rupress.org)
  • Once trans -dimerization happens, cis interactions can occur between the EC1 repeat of one cadherin protomer and the EC2 repeat of a parallel cadherin protomer on the same cell. (genetics.org)
  • This raises the possibility that Trp2 could participate in intermolecular interactions during adhesion by inserting into opposing cadherins in what is referred to as the strand exchange model of cadherin adhesion. (bl.uk)
  • Our results thus define the mechanism of cadherin adhesion as a dynamic balance between the conflicting tendencies of Trp2 to engage in intramolecular and intermolecular interactions. (bl.uk)
  • The prodomain shows structural resemblance to the cadherin domain, but lacks all the features known to be important for cadherin-cadherin interactions ( PUBMED:15130472 ). (embl.de)
  • Classical cadherins mediate cell-cell adhesion through calcium-dependenthomophilic interactions and are activated through cleavage of aprosequence in the late Golgi. (embl.de)
  • Our detailed structural and evolutionaryanalysis revealed that prodomains are distant relatives of cadherin"adhesive" domains but lack all the features known to be important forcadherin-cadherin interactions. (embl.de)
  • E-cadherin, which mediates epithelial cell-cell interactions, plays fundamental roles in tissue organization and is often perturbed in diseases such as cancer. (dovepress.com)
  • Two other members of the cadherin family, desmoglein and desmocollin, mediate adhesion in desmosomes. (springer.com)
  • Thus, E-cadherin and other members of the cadherin family play a crucial role in establishing and maintaining the integrity of epithelial tissues. (springer.com)
  • In the present study, we applied atomic force microscopy (AFM) ( 10 ) as a powerful molecular approach to probe specific trans-interaction forces and conformational changes of recombinant VE-cadherin strand dimers in aqueous physiological conditions ( 11 - 15 ). (pnas.org)
  • Recombinant VE-Cadherin-Fc. (pnas.org)
  • This approach allowed them to emulate cadherin-mediated adhesions in single β-cells adherent to a substrate that presented high concentrations of recombinant E-cad/Fc, N-cad/Fc, or P-cad/Fc as if presented by another cell ( Fig. 1 ). (diabetesjournals.org)
  • In this sense, we decided to take advantage of the affinity of chelated metals for histidine residues present in His-tagged biomolecules to develop a protocol for oriented functionalization of MNPs with cadherin recombinant fragments. (csic.es)
  • Cadherin-E Human Recombinant (aa 600-707) expressed in E.coli, shows a 38 kDa band on SDS-PAGE. (prospecbio.com)
  • T-cadherin expression results in LDL-induced migration of T-cadherin expressing cells compared to control. (wikipedia.org)
  • Expression of T-cadherin is upregulated in atherosclerotic lesions and post-angioplasty restenosis -conditions associated with pathological angiogenesis. (wikipedia.org)
  • T-cadherin expression is upregulated in ECs, pericytes and VSMC of atherosclerotic lesions. (wikipedia.org)
  • T-cadherin expression in arterial wall after balloon angioplasty correlates with late stages of neointima formation and coincidentally with the peak in proliferation and differentiation of vascular cells. (wikipedia.org)
  • Loss of E-cadherin expression. (springer.com)
  • Expression of Ksp-cadherin during kidney development and in renal cell carcinoma. (ebi.ac.uk)
  • One of the prerequisites for the release of carcinoma cells from the primary site might be a defect in intercellular adhesion mediated by the absence of E Cadherin expression. (abcam.com)
  • Therefore, the expression of E Cadherin might be an important parameter for the determination of the invasive potential of epithelial neoplasms, and for the transition of a benign to a malignant neoplasm. (abcam.com)
  • Down-regulation of E-cadherin expression has been observed in a number of carcinomas and is usually associated with advanced stage and progression. (agilent.com)
  • Higher expression levels of IL-33 in cadherin-11-deficient mice mediated ILC2 activation, resulting in higher IL-13 expression levels and M2 macrophage expansion in adipose tissue. (jci.org)
  • A ) Representative flow cytometric plots of cell-surface cadherin-11 (Cad11) expression on CD45 - Ter119 - CD31 - PDGFR + fibroblasts among SVF cells in eWAT from WT and cad-11 -/- mice. (jci.org)
  • B ) Cell-surface cadherin-11 expression on CD45 - CD235α - CD31 - cells in stromal vascular cells isolated from obese human omentum fat (data from 1 of 3 experiments with similar results are shown). (jci.org)
  • Furthermore, knockdown of N-cadherin or expression of a dominant-negative construct of N-cadherin that is deficient in mediating adhesion and can compete for endogenous intracellular N-cadherin-mediated signaling decreases spine stability. (rupress.org)
  • The authors further demonstrate that the expression of EGFP-N-cadherin is restricted to some spines and that this expression correlates with the stability of spines. (rupress.org)
  • The expression of the dominant-negative construct of N-cadherin prevents this activity-dependent enlargement of the spine head. (rupress.org)
  • Interestingly, this effect is also prevented by the expression of the full-length N-cadherin, suggesting that a physiological level of N-cadherin is critical for its ability to regulate the spine head width. (rupress.org)
  • [4] A recent study has shown that A20 (which is a dual-ubiquitin editing enzyme) is essential for stability and expression of VE-cadherin. (wikidoc.org)
  • misregulated cadherin expression can alter characteristics of differentiated cells. (uninet.edu)
  • aberrant expression of cadherin 3 occurs in cervical adenocarcinomas. (thefreedictionary.com)
  • Their colony morphology was altered by the ectopic expression of cadherins from the dispersed type to the compact type, providing direct evidence for a key role of cadherins in cell-cell adhesion. (biologists.org)
  • e.g. the termination or initiation of expression of a cadherin subclass in a given cell collective is correlated with its segregation from or connection with other cell collectives. (biologists.org)
  • Studies have demonstrated that reduction and/or loss of E-cadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis. (thermofisher.com)
  • Böhm, Totzeck, Birchmeier, Wieland: Differences of E-cadherin expression levels and patterns in primary and metastatic human lung cancer. (antikoerper-online.de)
  • Loss of Membrane Expression of E-Cadherin in Leukemic Erythroblasts. (thefreelibrary.com)
  • In this study, we characterize for the first time, to our knowledge, the expression pattern of E-cadherin by bone marrow erythroid precursors using immunohistochemistry, and we demonstrate the loss of membrane expression of E-cadherin in erythroleukemia. (thefreelibrary.com)
  • Cdc6 expression represses E-cadherin transcription and activates adjacent replication origins. (sigmaaldrich.com)
  • Analysis in various types of human cancer revealed a strong correlation between increased Cdc6 expression and reduced E-cadherin levels. (sigmaaldrich.com)
  • Gould Rothberg BE, Bracken MB (2006) E-cadherin immunohistochemical expression as a prognostic factor in infiltrating ductal carcinoma of the breast: a systematic review and meta-analysis. (springer.com)
  • This study is firstly reported E-cadherin expression in the salivary gland and tumors. (nii.ac.jp)
  • The aim of this study was to assess epithelial expression of E-cadherin and c-Met in normal lip, in actinic cheilitis and lip squamous cell carcinoma. (scielo.cl)
  • In human glioblastoma tissue, the expression of E-cadherin is increased and usually correlates with unfavorable outcome. (biolegend.com)
  • PURPOSE: To test whether the expression of P-cadherin, a component of slit diaphragms between podocyte foot processes, would be altered by puromycin aminonucleoside (PAN) in a cultured podocyte in vitro. (koreamed.org)
  • Western blotting and reverse transcriptase-polymerase chain reaction (RT-PCR) were used to measure the change in P-cadherin expression. (koreamed.org)
  • The distinct expression of R-cadherin in the induced aggregating metanephric mesenchyme suggests that it may regulate the mesenchymal-epithelial transition during kidney development. (asm.org)
  • Finally, to investigate whether the redundant expression of other classic cadherins expressed in the kidney could explain the rather mild kidney defects in R-cadherin-deficient mice, we intercrossed R-cadherin −/− mice with cadherin-6 −/− , P-cadherin −/− , and N-cadherin +/− mice. (asm.org)
  • In prostate cancers, for example, the expression of E-cadherin is reported to be reduced or absent in comparison with its expression in normal prostate which is uniformly strong. (leicabiosystems.com)
  • In vivo T-cadherin was detected on the apical cell surface of the chick intestinal epithelium. (wikipedia.org)
  • E-cadherin, a member of the cadherin family, has a very important role in organizing the epithelium. (news-medical.net)
  • The mammary epithelium is thought to be stabilized by cell-cell adhesion mediated mainly by E-cadherin (E-cad). (aacrjournals.org)
  • Cadherin like 23 is expressed in the neurosensory epithelium, where it is thought to be involved in stereocilia organisation and hair bundle formation. (acris-antibodies.com)
  • Classical cadherins are necessary for cell-cell contacts, dynamic regulation of morphogenetic processes in embryos and tissue integrity in adult organism. (wikipedia.org)
  • Cell-to-cell adhesion mediated by cadherins plays an important role in tissue differentiation, holding the tissues together as they form during embryonic development. (news-medical.net)
  • Cadherins are also important in other aspects of cell organization, like the formation of boundaries, coordinated cell movements, and maintenance of structural and functional cell and tissue polarity. (news-medical.net)
  • Josie Glausiusz , Discover , September 1995 Cadherins are critical mediators of metazoan cell adhesion and signaling and provide the structural basis for vital developmental processes, including tissue morphogenesis and maintenance, cell sorting, and cell polarization … - Monika Abedin et al. (merriam-webster.com)
  • Cadherins are expressed in a tissue specific manner and and are required for assembly of cells into solid tissue. (abcam.com)
  • Cadherin-11-deficient mice displayed increased stromal production of IL-33, with concomitant enhancements in ILC2s and M2 macrophages that helped control adipose tissue inflammation. (jci.org)
  • Consistent with reduced adipose tissue inflammation, cadherin-11-deficient mice were protected from obesity-induced glucose intolerance and adipose tissue fibrosis. (jci.org)
  • These results suggest that stromal fibroblasts expressing cadherin-11 regulate adipose tissue inflammation and thus highlight cadherin-11 as a potential therapeutic target for the management of obesity. (jci.org)
  • Cadherin-11 is expressed by fibroblasts in adipose tissue. (jci.org)
  • Among them, E-cadherin is the most studied, having a relevant role in maintaining the cohesion of epithelial tissue. (csic.es)
  • E-cadherin plays a central role in the growth and development of cells by controlling tissue architecture, and maintenance of tissue integrity. (thermofisher.com)
  • PDGF-A (show PDGFA ELISA Kits )/PDGFRalpha signalling as a tissue-autonomous regulator of contact inhibition of locomotion by controlling N-cadherin upregulation during epithelial-to-mesenchymal transition. (antibodies-online.com)
  • The dependence of migration of the fiber cell apical domains along the Epithelial Fiber Interface for lens morphogenesis on N-cadherin provides new insight into the process of tissue development. (antibodies-online.com)
  • Knockdown of N-cadherin in 3T3 fibroblasts did not impede gap closure in a soft tissue wound healing model. (antibodies-online.com)
  • The different types of cadherins are named from the type of tissue where they originate from, e.g. (redorbit.com)
  • Cadherin 11 (CDH11) as a typical type II cadherin plays an essential role in ranging from cellular adhesion to maintenance of tissue integrity and homeostasis. (aiche.org)
  • The cadherins are key regulators of tissue patterning and organ formation. (dissertations.se)
  • Of these, the classical cadherin family plays a central role, both during morphogenesis and in post-developmental tissue homeostasis. (dovepress.com)
  • To form mature trans adhesive dimers, cadherin domains from apposed cells dimerize in a 'strand-swapped' conformation. (nih.gov)
  • Cadherins outside the classical subfamily appear to have evolved distinct adhesive mechanisms that are only now beginning to be understood. (nih.gov)
  • Classical cadherins from adhesive dimers by exchange of the N-terminal β-strand. (nih.gov)
  • b) The adhesive mechanism of classical cadherins is an example of 3D domain swapping, EC1 domains are shown for monomer and dimer (ribbon representation). (nih.gov)
  • In this model, adhesive bonds between cadherins of interacting cell membranes are predicted to result from binding between subdomains 1 of oppositely oriented cis-dimers to form trans-interacting antiparallel tetramers that are termed adhesion dimers. (pnas.org)
  • X-ray crystallographic studies of subdomain 1 of N-cadherin suggest that adhesion dimers might associate laterally into zipper-like supramolecular clusters providing cumulative adhesive strength ( 5 ). (pnas.org)
  • Type I and II classical cadherins help to determine the adhesive specificities of animal cells. (rcsb.org)
  • Crystal-structure determination of ectodomain regions from three type II cadherins reveals adhesive dimers formed by exchange of N-terminal beta strands between partner extracellular cadherin-1 (EC1) domains. (rcsb.org)
  • The adhesive properties of classic cadherins are undisputed. (jneurosci.org)
  • Using their most membrane-distal EC1 repeat, cadherin protomers on opposed cells swap strands with each other to form adhesive dimers. (genetics.org)
  • My work examines the role of a conserved tryptophan residue, Trp2, in the adhesive domain of cadherins that has been shown to be essential for their adhesive function. (bl.uk)
  • Mutations within this interface ablate the adhesive capacity of T-cadherin. (mdc-berlin.de)
  • The adhesive binding mode used by T-cadherin may also be used by other nonclassical cadherins. (mdc-berlin.de)
  • The folded part of the prosequence-termedprodomain-has a striking structural resemblance to cadherin "adhesive"domains that could not have been predicted from the amino acid sequencedue to low sequence similarities. (embl.de)
  • In migrating vascular cells, T-cadherin was located at the leading edge as revealed by confocal microscopy. (wikipedia.org)
  • Studying signaling effects of low density lipoproteins (LDL) in vascular smooth muscles (VSMCs), T-cadherin was isolated and identified as new LDL receptor using human aortic media and the ligand-blotting method. (wikipedia.org)
  • Adiponectin binding to T-cadherin on vascular cells is associated with NF-kappa B activation. (wikipedia.org)
  • VE-cadherin is indispensable for proper vascular development - there have been two transgenic mouse models of VE-cadherin deficiency, both embryonic lethal due to vascular defects. (wikidoc.org)
  • Ivanov, Philippova, Allenspach, Erne, Resink: T-cadherin upregulation correlates with cell-cycle progression and promotes proliferation of vascular cells. (antibodies-online.com)
  • Structurally, cadherins are built of the following domains: a signal sequence, followed by a propeptide of about 130 residues, then an extracellular domain of around 600 residues, then a transmembrane region, and finally a C-terminal cytoplasmic domain of about 150 residues. (expasy.org)
  • Cadherins comprise an extensive family of type I glycoproteins having large, extracellular N-terminal domains and smaller, intracellular C-terminal domains ( Geiger and Ayalon, 1992 ). (jneurosci.org)
  • CADHERINS are a large family of transmembrane glycoproteins that regulate cell affinity. (genetics.org)
  • Cadherins are a family of glycoproteins involved in the Ca2+-dependent cell-cell adhesion mechanism which is detected in most kinds of tissues. (biologists.org)
  • Though T-cadherin can mediate weak adhesion in aggregation assays in vitro, the lack of intracellular domain suggests that T-cadherin is not involved in stable cell-cell adhesion. (wikipedia.org)
  • Classical cadherins, the first cadherins identified, are well known to be essential for cell-cell adhesion, serving to organize the adherens junction. (biologists.org)
  • Colon cancer is characterized by the progressive loss of E-cadherin, a Ca2+-dependent adherens junction component and epithelial marker. (queensu.ca)
  • Adhesion by classic cadherins is involved in some significant cellular signaling pathways, including Wnt, Hedgehog, Ras, and RhoGTPase signaling. (news-medical.net)
  • As E-cadherin is vitally involved in signaling pathways modulating cell proliferation, survival, invasion, and migration, dysregulation of E-cadherin leads to dysfunction of gastric epithelial cells and contributes to gastric cancer development. (hindawi.com)
  • Loss of E-cadherin promotes metastasis via multiple downstream transcriptional pathways. (broadinstitute.org)
  • Here, using physiologically relevant 3D in vitro models, we find that E-cadherin induces hyper-proliferation in breast cancer cells through activation of the Raf/MEK/ERK signaling pathway. (biorxiv.org)
  • Auf www.antikoerper-online.de finden Sie aktuell 376 Cadherin 5 (CDH5) Antikörper von 32 unterschiedlichen Herstellern. (antikoerper-online.de)
  • The cadherin family is essential in maintaining the cell to cell contact between each other and regulating for cytoskeletal complexes. (wikipedia.org)
  • High-molecular weight (HMW) complexes of adiponectin were suggested to be a specific ligand for T-cadherin. (wikipedia.org)
  • Higher order unbinding forces, that increase with interaction time, indicate association of cadherins into complexes with cumulative binding strength. (pnas.org)
  • In turn, these forces elicit mechanosensory signals from cadherin complexes that ultimately impact on cell phenotype and function in multiple cell types ( 29 , 30 ), including pancreatic islets ( 31 ). (diabetesjournals.org)
  • The resulting cadherin-NPRAP-ABP/GRIP complexes serve as anchorages for AMPARs. (jneurosci.org)
  • The cadherin-NPRAP-ABP complexes also bound GluR2. (jneurosci.org)
  • In cultured hippocampal neurons, dominant-negative mutants of NPRAP designed to disrupt tethering of ABP to NPRAP-cadherin complexes reduced surface levels of endogenous GluR2, indicating that interaction with cadherin-NPRAP-ABP complexes stabilized GluR2 at the neuronal plasma membrane. (jneurosci.org)
  • Because we find that NPRAP also binds to PSD-95, cadherin-NPRAP complexes may be linked to the PSD-95 scaffold, which is involved in tethering NMDAR and TARP-AMPAR complexes and which also interacts with neuroligins. (jneurosci.org)
  • E-cadherin (E-cad) is a transmembrane glycoprotein that functions to maintain stable cell-cell contacts in epithelial cell types ( 1 ). (aacrjournals.org)
  • Introducing an E-cadherin EC5 missense allele into the homozygous N-cadherin EC1 missense mutant more radically affects morphogenesis, causing synergistic phenotypes consistent with interdependent functions being disrupted. (genetics.org)
  • E-cadherin is important for cell-cell adhesion and promotes epithelial morphogenesis and maintenance of the epithelial phenotype. (dissertations.se)
  • It uses the cadherins, desmoglein and desmocollin to penetrate through the membrane and form an interlocking network that binds cells together. (news-medical.net)
  • Desmoglein and desmocollin are cadherin family members that mediate cell-cell adhesion in desmosomes of epithelial tissues and cardiac muscle. (nature.com)
  • Using human AECs and cell lines, we demonstrate that cadherin-26 (CDH26) is abundantly expressed in differentiated AECs, localizes to the cell apices near ciliary membranes, and has functional cadherin domains with homotypic binding. (nature.com)
  • Cadherins are involved in controlling morphogenetic movements during development and regulate cell surface adhesion through homotypic adhesion with the same cadherin species. (thermofisher.com)
  • Recent studies in our lab also revealed that engagement of cadherin 11 through homotypic binding is necessary for the differentiation process of mesenchymal stem cell (MSC) to smooth muscle cell (SMC) 1 . (aiche.org)
  • Atypical cadherins are different from other types of cadherins and consist of one or more extracellular repeat domains. (wikipedia.org)
  • To date, over 100 types of cadherins in humans have been identified and sequenced. (wikipedia.org)
  • There are about one hundred types of cadherins in vertebrates, and they fall into four groups. (news-medical.net)
  • The homodimeric cadherins create cell-cell adhesion with cadherins present in the membranes of other cells through changing conformation from cis-dimers to trans-dimers. (wikipedia.org)
  • Trans dimers are less flexible than cadherin monomers, a factor that drives junction assembly following cell-cell contact by reducing the entropic cost associated with the formation of lateral cis oligomers. (nih.gov)
  • It has been stated that "as long as cadherins are functioning, other adhesion systems have little effect on cell-cell adhesion" ( Takeichi, 1991 ). (jneurosci.org)
  • It is hypothesized, that p120 CTN existing in an 'active' form, induces cadherin clustering and cell-cell adhesion by binding to the juxtamembrane part of E-cadherin, and that intracellular signalling can induce an 'inactive' form of p120 CTN . (uninet.edu)
  • Pece, Gutkind: Signaling from E-cadherins to the MAPK pathway by the recruitment and activation of epidermal growth factor receptors upon cell-cell contact formation. (antikoerper-online.de)
  • To further investigate the molecular basis of this notion, we use two methods to inhibit E-cadherin function that distinguish between E-cadherin's cell-cell adhesion and intracellular signaling functions. (broadinstitute.org)
  • E-cadherin mediates cell-cell adhesion and plays a critical role in the formation and maintenance of junctional contacts between cells. (redorbit.com)
  • Cadherins: a molecular family important in selective cell-cell adhesion. (expasy.org)
  • A key determinant to the strength of the binding that it is mediated by cadherins is the juxtamembrane region of the cadherin. (embl.de)
  • We aim to provide comprehensive perspectives in the molecular mechanism of E-cadherin and its involvement in gastric cancer initiation and progression. (hindawi.com)
  • These data demonstrate that Cdc6 acts as a molecular switch at the E-cadherin locus, linking transcriptional repression to activation of replication, and provide a telling example of how replication licensing factors could usurp alternative programs to fulfill distinct cellular functions. (sigmaaldrich.com)
  • Moreover, during the epithelialmesenchymal transition, E-cadherin disappearance is associated with metastasis. (csic.es)
  • The extracellular part of E-cadherin interacts mainly homotypically (epithelial cell to epithelial cell), but also heterotypically (melanocytes or dendritic cells to keratinocytes). (uninet.edu)