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.
A cultured line of C3H mouse FIBROBLASTS that do not adhere to one another and do not express CADHERINS.
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 process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
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.
Orientation of intracellular structures especially with respect to the apical and basolateral domains of the plasma membrane. Polarized cells must direct proteins from the Golgi apparatus to the appropriate domain since tight junctions prevent proteins from diffusing between the two domains.
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.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
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.
A large family of MONOMERIC GTP-BINDING PROTEINS that are involved in regulation of actin organization, gene expression and cell cycle progression. This enzyme was formerly listed as EC 3.6.1.47.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
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-23 in the Medical Dictionary? protocadherin-23 explanation free. What is protocadherin-23? Meaning of protocadherin-23 medical term. What does protocadherin-23 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 ...
... 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. ...
Rolf Kemler's anti serum was what helped him finally identify cadherin. E-cadherin was the first of the cadherin family to be ... After his discovery of cadherins, he continued to research cadherins and their properties. Along with cadherins, he also ... An assay showed the hemaglutinin interaction is specific to e-cadherin. Outside of cadherin, Takeichi studied other molecules ... They found the hemagglutinin directly interacted with the e-cadherin in the epithelial cells to disturbed cell to cell adhesion ...
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- ...
Cadherin-17 is a protein that in humans is encoded by the CDH17 gene. This gene is a member of the cadherin superfamily, genes ... 2004). "Ksp-cadherin is a functional cell-cell adhesion molecule related to LI-cadherin". Exp. Cell Res. 294 (2): 345-55. doi: ... "Entrez Gene: CDH17 cadherin 17, LI cadherin (liver-intestine)". Gessner R, Tauber R (2001). "Intestinal cell adhesion molecules ... The encoded protein is cadherin-like, consisting of an extracellular region, containing 7 cadherin domains, and a transmembrane ...
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 ...
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 ...
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 ...
Cadherin 9 is a protein that in humans is encoded by the CDH9 gene. An association with autism has been suggested. Cadherin ... "Entrez Gene: cadherin 9". 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 (June 1997). "Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial ... Thedieck C, Kalbacher H, Kuczyk M, Müller GA, Müller CA, Klein G (2007). Zoccali C (ed.). "Cadherin-9 is a novel cell surface ...
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. ...
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 3 is a protein that in humans is encoded by the CELSR3 gene. The protein encoded by ... "Entrez Gene: CELSR3 cadherin, EGF LAG seven-pass G-type receptor 3 (flamingo homolog, Drosophila)". Bonaldo MF, Lennon G, ... 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. ...
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 ...
Distinct E-cadherin-based complexes regulate cell behaviour through miRNA processing or Src and p120 catenin activity. ... However, in Eph4 cell line, PLEKHA7 is recruited to E-cadherin based AJ by Afadin, independently of p120. PLEKHA7 knockdown ... Therefore, PLEKHA7 stabilises both cadherins and nectins at AJ. Genome-wide association studies suggest that PLEKHA7 is ... Nectins are the second major class of transmembrane adhesion molecules at adherens junctions, besides cadherins. ...
... each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. ... These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown ... Wu Q, Maniatis T (Jul 1999). "A striking organization of a large family of human neural cadherin-like cell adhesion genes". ... Nollet F, Kools P, van Roy F (2000). "Phylogenetic analysis of the cadherin superfamily allows identification of six major ...
... each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. ... These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown ... Wu Q, Maniatis T (Jul 1999). "A striking organization of a large family of human neural cadherin-like cell adhesion genes". ... Nollet F, Kools P, van Roy F (2000). "Phylogenetic analysis of the cadherin superfamily allows identification of six major ...
Cadherins are present in more complex organisms as well. In mouse embryos, E-cadherin on cell membranes is responsible for the ... This is likely due to distinct cadherins, a calcium-binding membrane protein, expressed by different sponge species and ...
... each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. ... These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown ... Wu Q, Maniatis T (1999). "A striking organization of a large family of human neural cadherin-like cell adhesion genes". Cell. ... Nollet F, Kools P, van Roy F (2000). "Phylogenetic analysis of the cadherin superfamily allows identification of six major ...
... 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 ...
Cadherin_repeat; Cadherin tandem repeat domain. pfam07001. Location:452 → 550. BAT2_N; BAT2 N-terminus. ... Cadherin_repeat; Cadherin tandem repeat domain. pfam07001. Location:452 → 534. BAT2_N; BAT2 N-terminus. ... Cadherin_repeat; Cadherin tandem repeat domain. cl26464. Location:452 → 665. Atrophin-1; Atrophin-1 family. ... Cadherin_repeat; Cadherin tandem repeat domain. PHA03247. Location:454 → 645. PHA03247; large tegument protein UL36; ...
Compare Anti-M-cadherin Antibody Products from leading suppliers on Biocompare. View specifications, prices, citations, reviews ... Anti-M-cadherin Antibody Products. Listed below are anti-M-cadherin antibodies from multiple suppliers. M-cadherin is a ... reported alias name for the human gene CDH15, or cadherin 15. The 814-amino acid protein has a reported mass of 88,916 ...
Highly specific and rigorously validated in-house, Pan-Cadherin Antibody (CST #4068) is ready to ship. ... Polyclonal Antibody for studying N-Cadherin/P-Cadherin/E-Cadherin/R-cadherin. Cited in 59 publications. Validated for WB, IP, ... This change in cadherin expression is called the cadherin switch. N-cadherin cooperates with the FGF receptor, leading to ... Pan-Cadherin Antibody detects endogenous levels of E-, VE-, N-, and R-Cadherins.. Species Reactivity:. Human, Mouse, Rat, ...
... Proc Natl Acad Sci U S A. 2016 Jul 5;113(27): ...
Browse our VE-Cadherin Antibodies all backed by our Guarantee+. ... VE-Cadherin Antibodies. We offer VE-Cadherin Antibodies for use ... anti-cadherin 5, type 2, VE-cadherin (vascular epithelium) antibody, anti-cadherin-5 antibody, anti-CD144 antibody, anti-CD144 ... anti-VE-Cadherin antibody, anti-CDH5 antibody, anti-7B4 antibody, anti-7B4 antigen antibody, anti-cadherin 5, type 2 (vascular ... Choose from our VE-Cadherin polyclonal antibodies and browse our VE-Cadherin monoclonal antibody catalog. ...
One of such regulatory SNPs (rSNPs) is the E-cadherin (CDH1) promoter −160C/A SNP (rs16260) which is known to affect E- ... cadherin promoter transcription by displacing transcription factor binding and has been extensively scrutinized for its ... 4. E-Cadherin −160C/A SNP Affects E-Cadherin Transcriptional Activity. The E-cadherin −160C/A SNP is located at the −160 ... E-Cadherin −160C/A SNP and Gastrointestinal Tract Cancer. E-cadherin −160C/A SNP has been studied most intensively in gastric ...
In contrast, rescue was ineffective in mice lacking T-cadherin in addition to APN. These data suggest that T-cadherin protects ... We observed extensive colocalization of T-cadherin and APN on cardiomyocytes in vivo. In T-cadherin-deficient mice, APN failed ... T-cadherin is critical for adiponectin-mediated cardioprotection in mice J Clin Invest. 2010 Dec;120(12):4342-52. doi: 10.1172/ ... During ischemia-reperfusion injury, the absence of T-cadherin increased infarct size similar to that in APN-null mice. ...
J:319470 Polanco J, et al., Differential Spatiotemporal Expression of Type I and Type II Cadherins Associated With the ...
005319 B6.129-|i|Cdh1|sup|tm2Kem|/sup||/i|/J |p||strong||/strong|When mice of this strain are bred to a strain expressing Cre recombinase in specific tissues, this strain may useful in studies of various epithelial cell functions.|/p|
Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4. John M. ... Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4 ... Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4 ... Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4 ...
This entry represents the cytoplasmic C-terminal domain of some proto-cadherins. It is this region of the cadherins that allows ... Cadherin_C_2. PFAM accession number:. PF16492. Interpro abstract (IPR032455):. ... The domain within your query sequence starts at position 686 and ends at position 769; the E-value for the Cadherin_C_2 domain ... Cadherins are cell-surface receptors that function in cell adhesion, cell polarity, and tissue morphogenesis [ (PUBMED:1568244 ...
These cells express Cadherin 12 (CDH12, N-Cadherin 2), catenins, and other epithelial markers. CDH12-enriched tumors define ... Here, single nuclei RNA sequencing and spatial profiling identify a cancer cell population expressing Neural Type Cadherin 2 ... These cells express Cadherin 12 (CDH12, N-Cadherin 2), catenins, and other epithelial markers. CDH12-enriched tumors define ... 63/197,129 "USE OF CANCER CELL EXPRESSION OF CADHERIN 12 AND CADHERIN 18 TO TREAT MUSCLE INVASIVE AND METASTATIC BLADDER ...
Data from: Peptides derived from cadherin juxtamembrane region inhibit platelet function. Golla, Kalyan, Royal College of ... Sequential deletion of amino acids from the N- and C-termini of the inhibitory E-cadherin peptides identified the short ... We conclude that peptides derived from JMD of E-cadherin provide potential lead peptides for the development of anti-thrombotic ... We synthesized overlapping 12-15 amino acids peptides from E- and N-cadherin JMD and assessed their effect on platelet ...
View Mouse P-Cadherin (NP_001032898) VersaClone cDNA in cDNA Clones. ... CAD3; cadherin 3, P-cadherin (placental); cadherin 3, type 1, P-cadherin (placental); Cadherin-3; CDH3; CDHP; CDHPcalcium- ... the cadherin superfamily also includes desmosomal cadherins, protocadherins, 7TM cadherins, FAT family cadherins, and T- ... dependent adhesion protein, placental; HJMD; PCAD; PCadherin; P-Cadherin; PCADP-cadherin; Placental cadherin ...
This gene is a classical cadherin from the cadherin superfamily. The encoded protein is a calcium dependent cell-cell adhesion ... Recombinant protein of human cadherin 1, type 1, E-cadherin (epithelial) (CDH1) ... Transient overexpression lysate of cadherin 1, type 1, E-cadherin (epithelial) (CDH1) ... Transient overexpression lysate of cadherin 1, type 1, E-cadherin (epithelial) (CDH1) ...
Analysis of the role of cadherins in retinoblastoma tumor cell adhesion and growth. Lisa Ann Krisak, Thomas Jefferson ... Krisak, Lisa Ann, "Analysis of the role of cadherins in retinoblastoma tumor cell adhesion and growth" (2002). ETD Collection ...
Cadherins and mechanotransduction by hair cells. / Müller, Ulrich.. In: Current Opinion in Cell Biology, Vol. 20, No. 5, ... Cadherins and mechanotransduction by hair cells. Current Opinion in Cell Biology. 2008 Oct;20(5):557-566. doi: 10.1016/j.ceb. ... Cadherins and mechanotransduction by hair cells. In: Current Opinion in Cell Biology. 2008 ; Vol. 20, No. 5. pp. 557-566. ... Müller, U 2008, Cadherins and mechanotransduction by hair cells, Current Opinion in Cell Biology, vol. 20, no. 5, pp. 557-566 ...
... also known as E-cadherin, cadherin-1, CDH1, and UVO is a member of the cadherin superfamily. ... CD324, also known as E-cadherin, cadherin-1, CDH1, and UVO is a member of the cadherin superfamily. It is a calcium-dependent, ... E-Cadherin, Cadherin-1, CDH1, and UVO Isotype Rat IgG1, κ Ave. Rating Submit a Review Product Citations publications MDCK ... PE anti-mouse/human CD324 (E-Cadherin). DECMA-1. FC. Alexa Fluor® 594 anti-mouse/human CD324 (E-Cadherin). DECMA-1. ICC, IHC-P ...
Cleavage of E-cadherin by ADAM10 mediates epithelial cell sorting downstream of EphB signalling ...
Both cadherins and catenins are localized in synaptic junctions (Fannon and Colman, 1996; Uchida et al., 1996). When cadherin ... To explore the specific functions of cadherin subtypes, we focused on cad8, a type-II classic cadherin, expressed in the spinal ... Here, we show that cadherin-8 (cad8), a type-II classic cadherin, is important for cold sensation, whose circuitry is ... 2006) Prototypical type I E-cadherin and type II cadherin-7 mediate very distinct adhesiveness through their extracellular ...
We studied the alterations of E-cadherin and β-catenin in a set of 50 primary gastric tumours by using loss of heterozygosity ( ... We also analyzed the aberrant E-cadherin mRNAs in the gastric tumours and found that 7 tumours (18%) had aberrant mRNAs in ... Our results support the hypothesis that alterations of E-cadherin and β-catenin play a role in the initiation and progression ... These aberrant mRNAs may produce abnormal E-cadherin molecules, resulting in weak cell-cell adhesion and invasive behaviour of ...
PE/Cyanine7 anti-human Cadherin 11 Antibody - Cadherins are calcium-dependent cell adhesion proteins. ... OSF-4, Osteoblast cadherin, OB-cadherin, CDH11, CDHOB, CAD11 Isotype Mouse IgG1, κ Ave. Rating Submit a Review Product ... View All Cadherin 11 Reagents Request Custom Conjugation Description. Clone. Applications. Purified anti-human Cadherin 11. ... Cadherin 11 is a type I transmembrane glycoprotein. It is a type II (atypical) cadherin, based on its lack of a HAV cell ...
The core of the AJ is the cadherin-catenin complex (Halbleib and Nelson, 2006; Ratheesh and Yap, 2012). Classical cadherins are ... The adhesive properties of classical cadherins are driven by the recruitment of cytosolic catenin proteins to the cadherin tail ... Guo, Z., Neilson, L. J., Zhong, H., Murray, P. S., Zanivan, S. and Zaidel-Bar, R. (2014). E-cadherin interactome complexity and ... Hazan, R. B., Kang, L., Roe, S., Borgen, P. I. and Rimm, D. L. (1997). Vinculin is associated with the E-cadherin adhesion ...
Keywords: Cadherins - blood, Breast Neoplasms - pathology, Disease-Free Survival, Kaplan-Meier Estimate, ROC Curve, Solubility ... Abnormal Expression of Serum Soluble E-Cadherin is Correlated with Clinicopathological Features and Prognosis of Breast Cancer ...
The objective of this project was to evaluate the biological activity of peptides derived from the EC-4 domain of E-cadherin in ... Inhibition of Cell Adhesion by Peptides Derived from the EC-4 Domain of E-Cadherin. ... of E-cadherin were more effective in inhibiting single cell adhesion than peptides from other domains (EC-1, EC-3) of E- ... cadherin. Peptide 8 had better activity than peptide 6. From overlapping hexapeptides derived from peptide 8, it was found that ...
... such as VE-cadherin, EphA2, MMP-2 and MMP-9. VE-cadherin belongs to the cadherin family and is specifically expressed in ... Most recent studies have shown that vascular endothelial-cadherin (VE-cadherin), epithelial cell kinase (EphA2), and matrix ... Association of VE-cadherin, EphA2, MMP-2 and MMP-9 proteins with VM. ... Association of VE-cadherin, EphA2, MMP-2 and MMP-9 proteins with VM. ...
Drosophila epithelial cadherin requires a novel regulatory region for cell migrati ... W hen it comes to cadherin regulation, it is not all about α- and β-catenins. ... Cadherins are used in cell-cell adhesion and migration in a variety of tissues. The cytoplasmic tail of cadherin contacts the ... The full-length cadherin-α-catenin fusion rescued cell-cell interactions and migration in tissues lacking wild-type DE-cadherin ...
Cadherin 10 antibody LS-C752184 is an unconjugated rabbit polyclonal antibody to human Cadherin 10 (CDH10). Validated for ELISA ... Polyclonal Rabbit anti‑Human CDH10 / Cadherin 10 Antibody (WB) LS‑C752184 Polyclonal Rabbit anti‑Human CDH10 / Cadherin 10 ... Cadherin 10 antibody LS-C752184 is an unconjugated rabbit polyclonal antibody to human Cadherin 10 (CDH10). Validated for ELISA ...
  • One of such regulatory SNPs (rSNPs) is the E-cadherin (CDH1) promoter −160C/A SNP (rs16260) which is known to affect E-cadherin promoter transcription by displacing transcription factor binding and has been extensively scrutinized for its association with several diseases especially malignancies. (hindawi.com)
  • CD324, also known as E-cadherin, cadherin-1, CDH1, and UVO is a member of the cadherin superfamily. (biolegend.com)
  • We define over 350 proteins in this interactome, nearly 200 of which are unique to CDH2 and not part of the E-cadherin (CDH1) interactome. (biorxiv.org)
  • CDH1 is a protein coding gene that encodes Cadherin-1. (cusabio.com)
  • Background: Inherited genetic factors such as E-cadherin (CDH1) promoter variants are believed to influence the risk towards sporadic diffuse gastric cancer (DGC). (icr.ac.uk)
  • The E-cadherin gene (CDH1) variants T340A and L599V in gastric and colorectal cancer patients in Korea. (ox.ac.uk)
  • INTRODUCTION: Germline mutations in E-cadherin (CDH1) have been reported in families with early onset, diffuse gastric cancer. (ox.ac.uk)
  • LOXL3 could interact with SNAIL, one of the most important EMT-TFs, thus repressed E-cadherin (CDH1) expression 16 . (researchsquare.com)
  • The CDH1 gene is located on chromosome 16 and normally encodes for a protein called E-cadherin. (pthealth.ca)
  • Immunohistochemical analysis of paraffin-embedded human breast carcinoma, using Pan-cadherin Antibody. (cellsignal.com)
  • Immunohistochemical analysis of paraffin-embedded human bronchioalveolar cell carcinoma using Pan-cadherin Antibody, showing membrane localization. (cellsignal.com)
  • Each VE-Cadherin 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 VE-Cadherin polyclonal antibodies and browse our VE-Cadherin monoclonal antibody catalog. (novusbio.com)
  • FF-21101 is a human-mouse chimeric monoclonal antibody directed against P-cadherin, conjugated with 111 In for dosimetry and biodistribution and 90 Y for therapy. (aacrjournals.org)
  • Cadherin 10 antibody LS-C752184 is an unconjugated rabbit polyclonal antibody to human Cadherin 10 (CDH10). (lsbio.com)
  • Cadherin-6 is a rabbit monoclonal antibody derived from cell culture supernatant that is concentrated, dialyzed, filter sterilized and diluted in buffer pH 7.5, containing BSA and sodium azide as a preservative. (affordableihcinstruments.com)
  • An anti-N-cadherin antibody can pull out β-catenin, whereas N-cadherin can also be pulled out using an anti-β-catenin antibody. (popcouncil.org)
  • Calcium-dependent intercellular adhesion of N-cadherin-expressing breast cancer and stromal cells was specifically inhibited by an anti N-cadherin monoclonal antibody. (elsevier.com)
  • This antibody was affinity purified using E-cadherin (a.a. 774-786) peptide. (ecmbio.com)
  • In western blots, the antibody detects a 120 kDa band corresponding to E-cadherin in human A431 cells, and does not detect VE-cadherin or N-Cadherin. (ecmbio.com)
  • 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)
  • These cells express Cadherin 12 ( CDH12, N-Cadherin 2 ), catenins, and other epithelial markers. (nature.com)
  • We demonstrate the presence of a previously uncharacterized epithelial cell phenotype marked by high expression of Cadherin 12 ( CDH12 , N-Cadherin 2), catenins and other epithelial markers. (nature.com)
  • Classical cadherins contain five extracellular cadherin repeats and a conserved cytoplasmic region that interacts with the actin cytoskeleton via catenins. (rndsystems.com)
  • The adhesive activities of cadherin are regulated by catenins, which bind the cytoplasmic domain of the cadherins. (jneurosci.org)
  • W hen it comes to cadherin regulation, it is not all about α- and β-catenins. (rupress.org)
  • Studies in tissue culture cells suggested that modulating the interaction between cadherin and the catenins would alter the adhesion strength of cadherin and facilitate migration. (rupress.org)
  • Vezatin is a ubiquitous protein of adherens cell±cell junctions, where it interacts with both myosin VIIA and the cadherin±catenins complex. (archives-ouvertes.fr)
  • Taken together, these data suggest that myosin VIIA, anchored by vezatin to the cadherin±catenins complex, creates a tension force between adherens junctions and the actin cytoskeleton that is expected to strengthen cell±cell adhesion. (archives-ouvertes.fr)
  • Furthermore, the assembly of AJs between Sertoli and germ cells was associated with a transient induction in the steady-state mRNA and protein levels of cadherins and catenins. (popcouncil.org)
  • The research presented here demonstrated that BMP-2 not only modulated N-cadherin function by decreasing the overall association of catenins with N-cadherin, but also regulated the intracellular levels and distribution of $\beta$-catenin-levels were maintained in BMP-2 treated cultures, but were redistributed to a cytoplasmic, non-N-cadherin-associated pool. (jefferson.edu)
  • Cadherins form protein complexes with cytoplasmic proteins (catenins) that convert the specific, homophilic-binding capacity of the extracellular domain into stable cell adhesion. (embl.de)
  • This gene is a novel mucin-like gene that is a member of the cadherin superfamily. (nih.gov)
  • The cadherin superfamily comprises a large number of cell surface glycoproteins with one or more cadherin repeats, which are involved in Ca2 + -dependent cell-cell adhesion. (rndsystems.com)
  • In addition to the classical cadherins, the cadherin superfamily also includes desmosomal cadherins, protocadherins, 7TM cadherins, FAT family cadherins, and T-cadherin. (rndsystems.com)
  • This gene is a classical cadherin from the cadherin superfamily. (origene.com)
  • Recent findings indicate that two members of the cadherin superfamily are components of the mechanotransduction machinery in sensory hair cells of the vertebrate inner ear. (elsevier.com)
  • Member of the cadherin superfamily. (biolegend.com)
  • These microvilli drive nutrient absorption and are arranged in a hexagonal pattern maintained by intermicrovillar links formed by 2 nonclassical members of the cadherin superfamily of calcium-dependent cell adhesion proteins: protocadherin-24 (PCDH24, also known as CDHR2) and the mucin-like protocadherin (CDHR5). (nicoyalife.com)
  • This gene encodes a member of the desmoglein family and cadherin cell adhesion molecule superfamily of proteins. (nih.gov)
  • We aim to understand how the diversity of sequences and structures in the cadherin superfamily contributes to their diverse signaling and adhesion functions mediated in the animal kingdom. (harvard.edu)
  • While encoding nonpolymorphic tandem repeats rich in proline, serine and threonine similar to mucin proteins, the gene also contains sequence encoding calcium-binding motifs found in all cadherins. (nih.gov)
  • We studied the alterations of E-cadherin and β-catenin in a set of 50 primary gastric tumours by using loss of heterozygosity (LOH) analysis, gene mutation screening, detection of aberrant transcripts and immunohistochemistry (IHC). (biomedcentral.com)
  • Myosin VIIa, harmonin and cadherin 23, three Usher I gene products that cooperate to shape the sensory hair cell bundle. (pasteur.fr)
  • Results: Hypermethylation of E-cadherin gene promoter was detected in 32 (26.7%) of the 120 pterygial specimens. (elsevier.com)
  • Conclusions: Our study demonstrates E-cadherin gene promoter hypermethylation were associated with low or absent expression of E-cadherin. (elsevier.com)
  • Exome sequencing led to the identification of a novel homozygous nonsense variant in the first exon of the cadherin-11 gene (CDH11), which results in a prematurely truncated form of the protein. (mpg.de)
  • We also located the mouse R-cadherin gene to chromosome 2. (houstonmethodist.org)
  • In total, 7 of 25 diffuse-type cancers harbored genetic alterations in the E-cadherin gene. (unisi.it)
  • Our observations suggest that inactivation of the E-cadherin gene occurs only in a subset of diffuse-type gastric cancers, as the majority of cases did not contain genetic alterations or identifiable protein abnormalities. (unisi.it)
  • Failure to express E-cadherin may result from mutations of the E-cadherin gene (HSECAD). (ox.ac.uk)
  • Results: DNA methylation was detected in 49% tissue samples and 40% peripheral blood samples in p15 gene & 63% tissue samples and 44% peripheral blood samples in E cadherin gene. (journalcra.com)
  • Kappa coefficient is 0.346 for p15 gene and 0.277 for E cadherin. (journalcra.com)
  • Elevated expression levels of the CDH2 gene and its protein product, N-cadherin were found in self-seeded cells. (bmj.com)
  • We show that inhibition of E-cadherin-mediated cell-cell contact in ES cells using gene knockout (Ecad(-/-)), RNA interference (EcadRNAi), or a transhomodimerization-inhibiting peptide (CHAVC) results in cellular proliferation and maintenance of an. (ox.ac.uk)
  • The protocadherin-α (Pcdha) family of clustered protocadherins consists of 14 cadherin-related molecules generated from a single gene cluster. (jneurosci.org)
  • James recognized a gene called VE-cadherin that only appears in endothelial cells, making it an ideal marker. (technologyreview.com)
  • E-cadherin gene polymorphisms and susceptibility to urolithiasis in Iraqi children. (cdc.gov)
  • 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 to as the cadherin adhesome. (wikipedia.org)
  • The intracellular portion of classical cadherins interacts with a complex of proteins that allows connection to the actin cytoskeleton. (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)
  • Cadherins are synthesized as polypeptides and undergo many post-translational modifications to become the proteins which mediate cell-cell adhesion and recognition. (wikipedia.org)
  • Protocadherins (Pcdhs) are cell adhesion and signaling proteins used by neurons to develop and maintain neuronal networks, relying on trans homophilic interactions between their extracellular cadherin (EC) repeat domains. (biorxiv.org)
  • Synthetic JMD peptides derived from cadherin cell adhesion proteins have previously been shown to modulate platelet function. (datadryad.org)
  • Classic cadherins, another family of cell-cell adhesion proteins, have also been implicated in synaptic contact formation. (jneurosci.org)
  • In addition, the expression of VE-cadherin, EphA2, MMP-2 and MMP-9 proteins associated with formation of pancreatic cancer vasculogenic mimicry. (spandidos-publications.com)
  • Rg3 treatment reduced the levels of vasculogenic mimicry in nude mouse xenografts in vitro and in vivo, while the expression of VE-cadherin, EphA2, MMP-2 and MMP-9 mRNA and proteins was downregulated by Rg3 treatment in vitro and in tumor xenografts. (spandidos-publications.com)
  • Cadherins are calcium-dependent cell adhesion proteins. (biolegend.com)
  • Classical cadherins are single-pass transmembrane proteins with an extracellular domain that mediates calcium-dependent homotypic interactions. (biorxiv.org)
  • The adhesive properties of classical cadherins are driven by the recruitment of cytosolic catenin proteins to the cadherin tail: p120-catenin (CTNND1) binds to the juxta-membrane domain and β-catenin (CTNNB1) binds to the distal part of the tail. (biorxiv.org)
  • A two page magazine article featuring cadherin proteins. (drawbio.com)
  • Cadherins ( Ca lcium dependant ad hesion molecules) are a class of type-1 transmembrane proteins . (blogspot.com)
  • One is a group of proteins called cadherins. (blogspot.com)
  • The aim of the present study was to examine the role of the junctional proteins beta-catenin and E-cadherin during preimplantation in vitro embryo development in sheep, comparing the competence of adult and prepubertal oocytes. (uniss.it)
  • Introduction Cadherins constitute a large family of cell-cell adhesion proteins that are represented in both vertebrates and invertebrates 1 2 The "classical" type I and type II cadherins are found only in vertebrates and contain an extracellular region consisting of a tandem repeat of five extracellular cadherin immunoglobulin-like domains (EC1-EC5) that extend from the cell surface (Fig. 1A). (scienceofgreathealth.com)
  • The positions of the strands were determined by the Definition of Secondary Structure of Proteins … This model of human E-cadherin was used to consider possible interaction sites in cadherinCintegrin binding with special reference to solvent-exposed acidic residues on loop structures. (pik-75.info)
  • All the clustered protocadherin genes encode type I transmembrane proteins with six extracellular cadherin domains ( Wu and Maniatis, 1999 ). (jneurosci.org)
  • classical cadherins are probably the most important proteins in adhering like cells, (homophilic adhesion), b/c they only like to bind to other cadherins of the same type. (flashcardmachine.com)
  • these linkages are almost always indirect, and depend on the intracellular anchorage proteins assembling on the tail of the cadherin. (flashcardmachine.com)
  • Cadherins are a group of transmembrane proteins that serve as the major adhesion molecules located within adherens junctions. (embl.de)
  • Cadherins are evolutionary related to the desmogleins which are component of intercellular desmosome junctions involved in the interaction of plaque proteins. (embl.de)
  • However, proteins are designated as members of the broadly defined cadherin family if they have one or more cadherin repeats. (embl.de)
  • This entry represents the extracellular repeated domains found in cadherins and related proteins. (embl.de)
  • 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)
  • The encoded protein is a calcium dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. (origene.com)
  • Recombinant protein containing the extracellular cadherin domain 1 of Cadherin 11 fused to maltose binding protein. (biolegend.com)
  • Removing the cytoplasmic tail of cadherin in the α-catenin fusion protein blocked migration in the ovary, though adhesion was normal. (rupress.org)
  • Here we show that harmonin, a PDZ domain-containing protein, and cadherin 23 are both present in the growing stereocilia and that they bind to each other. (pasteur.fr)
  • Moreover, we demonstrate that harmonin b is an F-actin-bundling protein, which is thus likely to anchor cadherin 23 to the stereocilia microfilaments, thereby identifying a novel anchorage mode of the cadherins to the actin cytoskeleton. (pasteur.fr)
  • Many studies have revealed that E-cadherin associated protein expression decreases in many tumors and pterygia. (elsevier.com)
  • However, no studies have examined the reason for E-cadherin protein inactivation in pterygia. (elsevier.com)
  • Therefore, this study aimed to analyze the association of E-cadherin promoter hypermethylation with protein inactivation in pterygial tissues. (elsevier.com)
  • Methods: E-cadherin methylation-status and the expression of E-cadherin and β-catenin protein were studied using methylation-specific PCR and immunohistochemistry, respectively, on 120 pterygial specimens and 30 normal conjunctivas. (elsevier.com)
  • A total of 79 (65.8%) pterygial specimens tested positive for E-cadherin protein expression and 41 (34.2%) specimens tested negative. (elsevier.com)
  • Moreover, loss of E-cadherin protein may contribute to aberrant localization of β-catenin. (elsevier.com)
  • Herein, we demonstrate that BFT specifically cleaves within 1 min the extracellular domain of the zonula adherens protein, E-cadherin. (elsevier.com)
  • Furthermore, studies by cross-linking using dithiobis(succinimidylpropionate) confirmed that the cadherin/catenin complex between Sertoli cells as well as between Sertoli and germ cells indeed structurally linked to actin but not to vimentin (an intermediate filament protein) or to tubulin (a microtubule protein). (popcouncil.org)
  • Thus, the cell binding specificity of R-cadherin is entirely conserved between the two species, suggesting a conserved role for this protein in morphogenesis. (houstonmethodist.org)
  • RESULTS: Absent or decreased E-cadherin protein expression was found in 27 (38%) of 68 colorectal cancers and the pattern of expression did not differ significantly among the three tumour groups. (ox.ac.uk)
  • The application of neutron spin echo spectroscopy is described to reveal the activation of nanoscale motions of the actin-binding domain in the cadherin-catenin complex and provides a protein dynamics and entropic explanation for the observed force-sensitive binding behavior of a mechanosensitive protein complex. (semanticscholar.org)
  • Our results enable us to elucidate fundamental systems of cadherin style and provide book insights regarding the feasible evolutionary systems that underlie the framework and function of the important protein family members. (scienceofgreathealth.com)
  • It is believed that P-cadherin is not just an adhesion molecule, also acting as a signalling protein involved in breast tissue remodelling, and that its soluble fragment present in human milk might result from the proteolysis of the extracellular domain name [58,59]. (clarkfrancis.com)
  • test and controlling for plate to plate variability, average values of cell adhesion to mutated E-cadherin-Fc fusion protein were compared with average values of cell adhesion to wild-type E-cadherin-Fc to determine whether adhesion to the mutant was significantly different from adhesion to wild-type. (pik-75.info)
  • Human E-cadherin was modeled based on GluA3 the murine E-cadherin crystal structure (available from the Protein Data Bank, http://www.rcsb.org/pdb, under accession no. 1EDH) 19. (pik-75.info)
  • This thesis research investigates the regulation of N-cadherin-dependent cell adhesion by bone morphogenetic protein-2 (BMP-2) during chondrogenesis and the signaling events downstream of BMP-2 and/or N-cadherin required for chondrogenesis. (jefferson.edu)
  • The thesis research presented here demonstrated that within 24 hours of BMP-2 treatment, C3H10T1/2 cells in high density micromass culture exhibit a 4-fold upregulation of N-cadherin mRNA, and by day 5 an 8-fold upregulation of N-cadherin protein. (jefferson.edu)
  • BMP-2 upregulation of N-cadherin expression and resultant chondrogenesis required mitogsn activated protein kinase (MAPK) activity and tyrosine phosphorylation as downstream events. (jefferson.edu)
  • Other laboratories have recently reported that N-cadherin dependent cell adhesion requires intracellular associations with $\alpha $-, $\beta$-, and $\gamma$-catenin, and that the protein adenomatous polyposis coli (APC) may play a role in regulating these interactions. (jefferson.edu)
  • Haas, Andrew Robert, "Chondrogenic induction by bone morphogenetic protein-2: Involvement of N-cadherin-associated functions" (1997). (jefferson.edu)
  • He then genetically engineered a green fluorescent protein to turn on in embryonic stem cells only when VE-cadherin is expressed, signaling in real time that the stem cell has differentiated into an endothelial cell. (technologyreview.com)
  • When there is a mutation, the function of the E-cadherin protein is disrupted, often resulting in cancer. (pthealth.ca)
  • All lobular carcinoma tumors were defined by loss of cell-to-cell adhesion protein E-cadherin through varied routes of genomic disruption. (cancer.gov)
  • From these observations, we proposed that each cadherin subtype might be used for linking a selected set of neurons belonging to the same functional group, because of its homophilic binding specificity. (jneurosci.org)
  • Cadherins are membrane glycoproteins that mediate homophilic cell-cell adhesion and play critical roles in cell differentiation and morphogenesis. (affordableihcinstruments.com)
  • Besides mediating cell-cell adhesion through homophilic interactions, E-cadherin mediates contact inhibition of cell growth, and loss of E-cadherin is associated with tumorigenesis. (huabio.com)
  • Cadherins cluster to form foci of homophilic binding units. (ecmbio.com)
  • Here, we show that cadherin-11 (also known as osteoblast-cadherin) was highly expressed in prostate cancer cell line derived from bone metastases and had strong homophilic binding to recombinant cadherin-11 in vitro. (elsevier.com)
  • Sotomayor, M. Heterophilic and homophilic cadherin interactions in intestinal intermicrovillar links are species dependent. (nicoyalife.com)
  • Cadherins are expressed in tissue-restricted patterns and typically mediate homophilic adhesion. (pik-75.info)
  • site is distinct from the homophilic binding site on E-cadherin. (pik-75.info)
  • The extracellular domains of cadherins form parallel dimers that possess intrinsic homophilic-binding activity. (embl.de)
  • The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. (drawbio.com)
  • The classic cadherin subfamily includes N-, P-, R-, B- and E-cadherins as well as about ten other members which are found in adherens junctions (AJ), E-cadherin is found at the junctions of epithelial cells. (huabio.com)
  • Is the cadherin/catenin complex a functional unit of cell-cell actin-based adherens junctions in the rat testis? (popcouncil.org)
  • Much controversy exists regarding the presence of the cadherin/catenin complex and its intracellular attachment site in the testis, which is the functional unit for actin-based cell-cell adherens junctions (AJs) in multiple epithelia. (popcouncil.org)
  • How is cadherin recruited to the adherens junction? (mechanobio.info)
  • Although this process is fundamental to the development of multicellular organisms, it is also a key occurrence in many diseases, including cancers of epithelial origin E-cadherin is a central component of adherens junctions (AJs), which act as structural and signaling hubs in epithelial cells that oppose EMT. (elsevier.com)
  • Intercellullar junctions formed by cadherins, including desmosomes and adherens junctions, comprise two dimensional arrays of "trans" dimers formed between monomers emanating from opposing cell surfaces. (elsevier.com)
  • Vascular endothelial (VE)-cadherin, the major adherens junction adhesion molecule in endothelial cells, interacts with p120-catenin and β-catenin through its cytoplasmic tail. (elsevier.com)
  • Molecular and functional analysis of cadherin-based adherens junctions. (embl.de)
  • Adherens junctions are specialized forms of cadherin-based adhesive contacts important for tissue organization in developing and adult organisms. (embl.de)
  • Role of N-Cadherin cis and trans interfaces in the dynamics of adherens junctions in living cells. (mpg.de)
  • Renewed analysis with respect to putative relations to Wnt signaling revealed that P-cadherin (CDH3) had three mutations in the coding region of the extracellular domain and was associated with high Wnt signaling. (uu.nl)
  • Loss of the cell adhesion molecule E-cadherin has been observed in a variety of human carcinomas, and germline E-cadherin mutations have been found in several familial cases of diffuse gastric cancer. (unisi.it)
  • We use these findings to design site-directed mutations which transform a monomeric EC2-EC3 domain cadherin construct into a strand-swapped dimer. (scienceofgreathealth.com)
  • E-cadherin germline mutations in familial gastric cancer. (cancer.gov)
  • germ line mutations of which cadherin can predispose one to familial gastric carcinoma? (flashcardmachine.com)
  • This linkage between transmembranous cadherins and actin filaments of the cytoskeleton is necessary to form strong cell-cell adhesion. (biomedcentral.com)
  • The cytoplasmic tail of cadherin contacts the actin cytoskeleton through α- and β-catenin. (rupress.org)
  • If the link between DE-cadherin and the actin cytoskeleton needs to be tempered in vivo, the tempering must happen downstream of α-catenin. (rupress.org)
  • 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. (ecmbio.com)
  • beta catenin is an element of the anchoring complex between cadherins+cytoskeleton. (flashcardmachine.com)
  • Strategies Components Mouse anti-N-cadherin antibodies and 3,3′,5,5′-Tetramethylbenzidine (TMB) alternative for ELISA had been bought from Sigma-Aldrich (Poznan, Poland). (fk866.net)
  • Reduced expression of E-cadherin and β-catenin was identified at the frequency of 42% and 28%, respectively. (biomedcentral.com)
  • An association was found between reduced expression of E-cadherin and β-catenin. (biomedcentral.com)
  • Moreover, an association was detected between reduced expression of E-cadherin and diffuse histotype. (biomedcentral.com)
  • Altered vasculogenic mimicry formation was assessed using immunohistochemistry and PAS staining and associated with the expression of vascular endothelial-cadherin (VE-cadherin), epithelial cell kinase (EphA2), matrix metalloproteinase (MMP)-2 and MMP-9. (spandidos-publications.com)
  • In conclusion, ginsenoside Rg3 effectively inhibited the formation of pancreatic cancer vasculogenic mimicry by downregulating the expression of VE-cadherin, EphA2, MMP9 and MMP2. (spandidos-publications.com)
  • The expression of this particular cadherin in osteoblastic cell lines along with its upregulation during differentiation suggests a specific function in bone development and maintenance. (biolegend.com)
  • Pre-treatment tumor samples were assessed for P-cadherin expression by immunohistochemistry (IHC). (aacrjournals.org)
  • The revelation of the genetic and molecularbasis of gastric cancer has helped the development of targetedtherapies which has the potential to improve survival.Decreased expression of Epithelial cadherin (E-cadherin)in gastric carcinoma is one such genetic alteration whichcould help in targeted therapy and prognostication. (who.int)
  • Theobjective of the present study was to identify E- cadherinimmunohistochemical expression in gastric carcinoma and itscorrelation with histopathological features.Material and Methods: Gastric biopsies and surgicalspecimens from a tertiary care center in South Indiawere included and assessed by light microscopy andimmunohistochemistry (IHC).Results: Aberrant E-cadherin staining was seen in 42.8% ofgastric adenocarcinoma. (who.int)
  • In this study, there was no significant associationbetween E-cadherin with age, gender, nature of the specimen,site of the tumor, size of the tumor, lymph node status andtumor invasion.Conclusion: This study emphasizes the importance ofidentification of aberrant E-cadherin expression in gastriccarcinomas which in turn helps in selecting patients for noveltherapies which might improve the prognosis of this gravedisease. (who.int)
  • The expression of Cadherin-6 is associated with tumor progression in renal cell carcinoma. (affordableihcinstruments.com)
  • E-cadherin expression is frequently down-regulated or extinguished in malignancy which strongly correlates with poor prognosis. (huabio.com)
  • This study aimed to detect the expression of E-Cadherin in endometrial tumors, using immunohistochemistry. (sustech.edu)
  • Positive expression of E-Cadherin was found in 17 (42.5%) sample, and negative expression found in 3 (7.5%) sample in both benign and malignant tumors. (sustech.edu)
  • This result showed insignificant association of E-Cadherin expression and endometrial tumors (P. value = 1.00). (sustech.edu)
  • The study concludes there is no association between E-cadherin expression and endometrial tumors. (sustech.edu)
  • To examine whether PKCK2 activity could determine the type of cadherin expressed, we first increased intracellular PKCK2 activity in TE2 cells by overexpressing the PKCK2a catalytic subunit using lentivirus and found that high PKCK2 activity could switch cadherin expression from type E to N and confer anoikis resistance. (elsevier.com)
  • In addition, N-cadherin expression correlated with PKB/Akt activation and increased invasiveness. (elsevier.com)
  • In breast and other tumor types, loss of E-cadherin expression has been seen in high grade tumors and correlates with increased invasiveness. (elsevier.com)
  • Here we show high levels of expression of N-cadherin in the most invasive breast cancer cell lines which was inversely correlated with their expression of E-cadherin. (elsevier.com)
  • Although the function of this cadherin (also termed Osteoblast-Cadherin) is not completely understood, its prevalent expression in osteoblastic cell lines and up-regulation during differentiation suggest a specific function in bone formation and development. (mpg.de)
  • Allele loss, replication errors and loss of expression of E-cadherin in colorectal cancers. (ox.ac.uk)
  • BACKGROUND: Loss of E-cadherin expression has been implicated in the development of invasive characteristics in colorectal carcinomas. (ox.ac.uk)
  • and to examine differences in E-cadherin expression and genetic changes at HSECAD between three different groups of colorectal cancer--replication error positive (RER+) sporadic cancers, RER--sporadic cancers and ulcerative colitis associated cancers. (ox.ac.uk)
  • Overall, there was no correlation between allelic loss or exon 16 replication errors and immunohistochemical E-cadherin expression. (ox.ac.uk)
  • CONCLUSIONS: (1) Loss of E-cadherin expression probably does not occur as a result of mutation at the HSECAD locus in colorectal cancers. (ox.ac.uk)
  • However, the incidence of PC3 metastasis to bone in this model was reduced greatly when the expression of cadherin-11 by those cells was silenced. (elsevier.com)
  • The clinical relevance of cadherin-11 in prostate cancer metastases was further studied by examining the expression of cadherin-11 in human prostate cancer specimens. (elsevier.com)
  • Cadherin-11 was not expressed by normal prostate epithelial cells but was detected in prostate cancer, with its expression increasing from primary to metastatic disease in lymph nodes and especially bone. (elsevier.com)
  • Cadherin-11 expression was not detected in metastatic lesions that occur in other organs. (elsevier.com)
  • We therefore studied the expression and distribution of E-cadherin during the major transition from maternal to embryonic genome. (uniss.it)
  • Considering the broad expression of E-cadherin in epithelia, this exploratory study encourages further evaluation of the 163+ 37235A-allele as a susceptibility variant in other carcinomas. (icr.ac.uk)
  • Elevated expression level of vascular endothelial (VE)-cadherin has been implicated in cancer neovascularization, growth, and progression. (jispcd.org)
  • There were statistically significant differences between tumor grade and the expression levels of VE-cadherin ( P = 0.000), between tumor grade and VM formation ( P = 0.000), and also between tumor grade and microvessel density (MVD) ( P = 0.000). (jispcd.org)
  • Our results may disclose a definite relationship between VE-cadherin expression level, VM, epithelial-mesenchymal transition, cancer stem cells, and MVD in MEC samples. (jispcd.org)
  • 2004. The dietary phytochemical chlorophyllin alters E-cadherin and beta-catenin expression in human colon cancer cells. . (oregonstate.edu)
  • Cadherins expression profile in high quality and in infiltrative tumours was equivalent, almost all expressing P-cadherin, of E-cadherin expression position regardless. (clarkfrancis.com)
  • Furthermore, the expression of P-cadherin was associated to a 8 almost.5 odds ratio for vascular invasion. (clarkfrancis.com)
  • neither there was a statistical significant association between the expression of E-cadherin in main tumours and in their neoplastic intravascular emboli and lymph node metastases. (clarkfrancis.com)
  • The P-cadherin/E-cadherin combined expression patterns were significantly associated with histological grade of carcinomas, mode of growth and presence of necrosis. (clarkfrancis.com)
  • Pulsatile flow-induced shear stress in large vessels affects VE-Cadherin and Neuregulin-1 expression in endothelial cells. (aps.org)
  • We investigated the effect of realistic healthy and unhealthy large vessel shear stresses on the endothelial cells' expression of vascular endothelial cadherin (VE-Cad) and neuregulin-1 (NRG-1). (aps.org)
  • Exogenous expression of H-cadherin in CHO cells regulates contact inhibition of cell growth by inducing p21 expression. (elsevier.com)
  • Dive into the research topics of 'Exogenous expression of H-cadherin in CHO cells regulates contact inhibition of cell growth by inducing p21 expression. (elsevier.com)
  • Compared with primary tumors, N-cadherin expression was significantly increased in matched recurrent tumor tissues. (bmj.com)
  • which cancers is reduced surface expression of E-cadherin noted in? (flashcardmachine.com)
  • and (3) recombinant expression of a dominant negative N-cadherin mutant molecule inhibited chondrogenesis. (jefferson.edu)
  • The results presented here indicate that BMP-2 requires the upregulation of N-cadherin expression and function to induce chondrogenesis, and alterations in N-cadherin dependent cell-cell adhesion at the cadherin-catenin complex level occur as cells begin to differentiate. (jefferson.edu)
  • We have shown that E Cadherin expression closely associates with tumor progression and survival. (marian.edu)
  • In the presence of CsA, E-cadherin is not effectively cleared from the membrane, β-catenin does not enter the nucleus and there is no effective expression of Bra. (biomedcentral.com)
  • Cancer cells that were cultured with CAFs had down-regulated E-cadherin expression compared to cancer cells that were cultured with normal fibroblasts. (news-medical.net)
  • Binding of p-120 catenin and β {\displaystyle \beta } -catenin to the homodimer increases the stability of the classical cadherin. (wikipedia.org)
  • We analysed the concentration of beta-catenin and E-cadherin in immature and in vitro-matured oocytes. (uniss.it)
  • The loss of E-cadherin from the plasma membrane is an early indication of EMT and a marker of poor prognosis in many cancers making the trafficking of E-cadherin an area of great interest. (elsevier.com)
  • The aim of the study was to assess the accuracy of some specific biochemical indicators in discriminating between Helicobacter pylori-associated gastritis and H. pylori-associated stomach cancer [‎serum gastrin level, serum soluble E-cadherin and tissue COX-2 activity, as well as serodiagnostic markers for H. pylori infection]‎ in order to find a simple diagnostic test that can reasonably predict the development of gastric cancer. (who.int)
  • We suggest that close follow-up together with periodic endoscopic examination for all patients with persistent H. pylori infection and serum soluble E-cadherin level above 5 µg/mL is essential. (who.int)
  • In structure, they share cadherin repeats, which are the extracellular Ca2+-binding domains. (wikipedia.org)
  • Similar to classical cadherins, desmosomal cadherins have a single transmembrane domain, five EC repeats, and an intracellular domain. (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)
  • Cadherin repeats. (embl.de)
  • Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium. (embl.de)
  • Abstract Cadherins are cell-adhesion molecules that control morphogenesis, cell migration, and cell shape changes during multiple developmental processes. (mpg.de)
  • abstract = "R-cadherin was originally identified as a chicken cadherin expressed by the retina. (houstonmethodist.org)
  • Our results support the hypothesis that alterations of E-cadherin and β-catenin play a role in the initiation and progression of gastric cancer. (biomedcentral.com)
  • Western blot image of human A431 cells that were probed with rabbit polyclonal anti-E-Cadherin (a.a. 774-786) at 1:250 (lane 1), 1:1000 (lane 2), and 1:4000 (lane 3) or mouse monoclonal anti-E-cadherin (Cytoplasmic) at 1:250 (lane 4) and 1:1000 (lane 5). (ecmbio.com)
  • Listed below are anti-M-cadherin antibodies from multiple suppliers. (biocompare.com)
  • Our VE-Cadherin Antibodies can be used in a variety of model species: Human, Mouse, Rat. (novusbio.com)
  • describe the preparation and application of antibodies directed against a synthetic, 24 amino acid long, peptide corresponding to the conserved cytoplasmic C terminus of N-cadherin. (zfin.org)
  • They demonstrate that the antibodies to the synthetic peptide react extensively with all known members of the cadherin family and, in addition, recognize novel cadherins in a variety of cells and tissues, suggesting that these antibodies indeed exhibit pan-cadherin reactivity. (zfin.org)
  • Overexpression of P-cadherin, a calcium-dependent cell-to-cell adhesion glycoprotein, correlates with increased tumor cell invasiveness in breast, colon, lung and pancreatic tumors. (aacrjournals.org)
  • Within this series, a substantial Wortmannin ic50 overexpression of P-cadherin by luminal epithelial cells was seen in carcinomas, in comparison with harmless mammary tumours. (clarkfrancis.com)
  • In vivo experimental results showed that overexpression of N-cadherin promoted tumor self-seeding and facilitated the survival of CTCs. (bmj.com)
  • It is a type II (atypical) cadherin, based on its lack of a HAV cell adhesion recognition sequence that is specific to type I cadherins. (biolegend.com)
  • Conserved anchor residues - Trp2 in type I cadherins or Trp2 and Trp4 in type II - dock into a complementary pocket in the partner molecule 3-6. (scienceofgreathealth.com)
  • The A* strand which comprises residues 1-3 represents the N-terminal segment of a strand that in type I cadherins spans residues 1-10 and includes a break at residues 4-6 due to the presence of prolines at positions 5 and 6 which provides a hinge that mediates conformational changes necessary for strand swapping (Fig. 1). (scienceofgreathealth.com)
  • Both diffuse and intestinal-type tumors exhibited low rates of LOH, suggesting that allelic loss at the locus is not a common mechanism for E-cadherin inactivation during gastric tumorigenesis. (unisi.it)
  • The Crystal Structure of Human E-cadherin Domains 1 and 2, and Comparison with other Cadherins in the Context of Adhesion Mechanism. (drawbio.com)
  • E-cadherin synthetic peptide corresponding to amino acids in the C-terminal region in human E-cadherin. (ecmbio.com)
  • Modeling of Human E-Cadherin. (pik-75.info)
  • Using the program O (T.A. Jones, Uppsala University, and M. Kjelgaard, Aahus University), sequence substitution of human E-cadherin residues into the murine E-cadherin structure was performed. (pik-75.info)
  • The side chain conformation of human E-cadherin residues was chosen Roflumilast to be similar to that of the murine E-cadherin residues while potential close contact was avoided. (pik-75.info)
  • Results Sequence Analysis and Modeling of Human E-Cadherin. (pik-75.info)
  • The amino acid sequence of the first domain of human E-cadherin was aligned with that of murine E- and N-cadherin, and there did not appear to be any deletions or insertions (Fig. 1 A). Domain 1 of human E-cadherin shares 89% amino acid sequence identity with domain 1 of murine E-cadherin. (pik-75.info)
  • Therefore, the structure of human E-cadherin is predicted to be very similar to that of murine E-cadherin. (pik-75.info)
  • As the core structure of the Roflumilast Roflumilast barrel is predicted to be highly conserved, we developed a model of human E-cadherin based on the murine E-cadherin structure (Fig. 1 B). Figure 1 Structural analysis of human E-cadherin. (pik-75.info)
  • A) Amino acid alignment of domain 1 of human E-cadherin with human P-cadherin and murine E- and N-cadherin. (pik-75.info)
  • Cadherin 2 (CDH2). (biolegend.com)
  • We combine quantitative mass spectrometry with proximity labeling to identify the N-cadherin (CDH2) interactome. (biorxiv.org)
  • Summary Statement Proximity proteomics reveals a specific and specialized N-cadherin (CDH2) interactome along the cell-cell contacts of primary cardiomyocytes. (biorxiv.org)
  • Classical cadherins maintain the tone of tissues by forming a homodimer in cis while desmosomal cadherins are heterodimeric. (wikipedia.org)
  • Although classical cadherins take a role in cell layer formation and structure formation, desmosomal cadherins focus on resisting cell damage. (wikipedia.org)
  • Desmosomal cadherins are responsible to maintain the function of desmosomes that is to overturn the mechanical stress of the tissues. (wikipedia.org)
  • Two types of desmosomal cadherins exist, and they are called desmogleins and desmocollins that contain an intracellular anchor and cadherin like sequence (ICS). (wikipedia.org)
  • E-cadherin may be a marker for both tumor metastasis and prognosis. (elsevier.com)
  • The combined results suggest a functional role for N-cadherin in cohesion of breast tumor cells which, in addition promotes their interaction with the surrounding stromal cells, thereby facilitating invasion and metastasis. (elsevier.com)
  • The current study aimed to study the presence of VE-cadherin in VM channels and tumor cells in different grades of MEC. (jispcd.org)
  • Soluble N-cadherin triggered NK cell functional exhaustion by interacting with the killer cell lectin-like receptor subfamily G member 1 (KLRG1) receptor and therefore protected tumor cells from NK cell killing in the circulation. (bmj.com)
  • Conclusion Together, our findings illustrate an unknown mechanism by which CTCs evaded NK cell-mediated immune surveillance, and indicate that targeting N-cadherin is an effective strategy to prevent CTCs from homing to primary tumor. (bmj.com)
  • The cross-talk between tumor cells and natural killer (NK) cells in the circulation can trigger NK cell functional exhaustion via N-cadherin/KLRG1 axis, thus enabling CTCs to avoid immune attack. (bmj.com)
  • when tumor stem cells derived from GBM were grown in the presence of human endothelial cells, a fraction of them acquired endothelial markers (CD31, CD105, VE-cadherin, and vWF). (hindawi.com)
  • Calcium-dependent cell adhesion molecules (cadherins) are involved in maintaining the epithelial structure of a number of tissues including the mammary gland. (elsevier.com)
  • Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. (ecmbio.com)
  • Background Cadherins are calcium-dependent cell-to-cell adhesion glycoproteins playing a critical role in the formation and maintenance of normal tissue architecture. (clarkfrancis.com)
  • 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)
  • These aberrant mRNAs may produce abnormal E-cadherin molecules, resulting in weak cell-cell adhesion and invasive behaviour of carcinoma cells. (biomedcentral.com)
  • A key event is the strand-swap dimerization of the extracellular ectodomains of two cadherin molecules from apposing cells. (elsevier.com)
  • Furthermore, whether germ and Sertoli cells are equipped with the necessary AJ-associated signaling molecules to regulate this cadherin/catenin complex during spermatogenesis is not known. (popcouncil.org)
  • Experiments in epithelial cells expressing cadherin tagged to a photoconvertible fluropohore for easy tracking, have shown AJs to be highly dynamic structures that continuously turnover cadherin molecules. (mechanobio.info)
  • Using micropatterning to isolate the role of cell-cell adhesion from cell-extracellular matrix adhesion, we demonstrate that endothelial cells required cell-cell contact and vascular endothelial cadherin engagement to transduce stretch into proliferative signals. (princeton.edu)
  • We used EGFR FISH Probe to detect EGFR amplification and anti-CD31, CD105, VE-cadherin, and vWF to identify endothelial cells. (hindawi.com)
  • In the bracket (right), en face staining, frozen cryosection of aortic ring, phase contrast micrograph of mouse aortic endothelial cells from EC-PhAM mice (MAEC EC-PhAM ), epifluorescence image of MAEC EC-PhAM , en face lesser curvature, and en face thoracic aorta are shown. (jci.org)
  • 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)
  • This mechanism, applicable to type I classical cadherins, confers high specificity and fast association rates. (elsevier.com)
  • To examine the binding specificity of mouse R-cadherin, L cells expressing this cadherin (mRL) were mixed with L cells expressing chicken R-cadherin (cRL), mouse N-cadherin (mNL), mouse E-cadherin (mEL) and mouse P-cadherin (mPL). (houstonmethodist.org)
  • The dashed box indicates … A considerable body of evidence demonstrates that cell-cell adhesive specificity is determined by the identity of the EC1 domain which contains the cadherin-cadherin binding interface 5 6 8 Vincristine sulfate Cadherins within the same subfamily (eg. (scienceofgreathealth.com)
  • Here, we report that the glycosyl phosphatidylinositol-anchored cell surface glycoprotein T-cadherin (encoded by Cdh13) protects against cardiac stress through its association with APN in mice. (nih.gov)
  • Cadherin 11 is a type I transmembrane glycoprotein. (biolegend.com)
  • The E-cadherin-catenin complex plays a crucial role in epithelial cell-cell adhesion and in the maintenance of tissue architecture. (biomedcentral.com)
  • An intact E-cadherin - catenin complex is required for maintenance of normal intercellular adhesion. (biomedcentral.com)
  • β-Catenin, in turn recruits αE-catenin (CTNNA1) to the cadherin-catenin complex. (biorxiv.org)
  • The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation. (drawbio.com)
  • Is the cadherin/catenin complex a functional unit of cell-cell actin-b" by Nikki P.Y. Lee, Dolores D. Mruk et al. (popcouncil.org)
  • These analyses reveal, to our knowledge for the first time, that the testis may indeed be using the cadherin/catenin complex as one of the functional units to regulate AJ dynamics between Sertoli and germ cells in addition to α 6 β 1 , integrin and the nectin/afadin complex. (popcouncil.org)
  • These results thus unequivocally demonstrate that the cadherin/catenin complex, which can be up-regulated by testosterone, is indeed present between Sertoli and germ cells and is used for the assembly of functional AJs. (popcouncil.org)
  • protocadherins are located in the brain, (50+ non-classical cadherins in brain alone), desmocollins and desmogleins form desmosome junctions, and T-cadherins have signalling functions in nerve and muscle cells. (flashcardmachine.com)
  • Here we have determined crystal structures of P-cadherin in six different conformational states to elaborate a motion picture of its adhesive dimerization at the atomic level. (elsevier.com)
  • The snapshots revealed that cell-adhesive dimerization is facilitated by several intermediate states collectively termed X-dimer in analogy to other classical cadherins. (elsevier.com)
  • Based on previous studies and on the combined structural, kinetic, thermodynamic, biochemical, and cellular data reported herein, we propose that the adhesive dimerization of human P-cadherin is achieved by a stepwise mechanism analogous to that of assembly chaperones. (elsevier.com)
  • Trans cadherin interactions result in an adhesive dimer interface between the interacting EC1 domains. (mechanobio.info)
  • Here we use bioengineering approaches to identify the roles of cadherin-catenin interactions in promoting strong cellular adhesion and the ability of the cells to spread on an adhesive surface. (elsevier.com)
  • Surprisingly, p120 binding to the cadherin tail had no effect on the strength of adhesion when the available adhesive area was limited. (elsevier.com)
  • Instead, the binding of VE-cadherin to p120 regulates adhesive contact area in a Rac1-dependent manner. (elsevier.com)
  • Cadherins depend on calcium for their function: calcium ions bind to specific residues in each cadherin repeat to ensure its proper folding, to confer rigidity upon the extracellular domain and is essential for cadherin adhesive function and for protection against protease digestion. (embl.de)
  • Most recent studies have shown that vascular endothelial-cadherin (VE-cadherin), epithelial cell kinase (EphA2), and matrix metalloproteinase (MMPs) play a crucial role in VM formation ( 13 - 21 ). (spandidos-publications.com)
  • Together, these data suggest that vascular endothelial cadherin has an important role in mechanotransduction and that endothelial and smooth muscle cells use different mechanisms to respond to stretch. (princeton.edu)
  • The full-length cadherin-α-catenin fusion rescued cell-cell interactions and migration in tissues lacking wild-type DE-cadherin or β-catenin. (rupress.org)
  • It is this mature, curved form of cadherin that engages in trans interactions. (mechanobio.info)
  • The outermost EC domain (EC1) of cadherins engage in trans interactions by forming a dimer interface. (mechanobio.info)
  • Here we report Monte Carlo simulations performed on a 2D lattice constructed to account for the anisotropy in cadherin cis interactions. (elsevier.com)
  • Cytoplasmic interactions can influence the function of the ectodomain by a number of potential mechanisms, including redistribution of binding sites into clusters, providing cytoskeletal anchorage, and mediating physiological regulation of cadherin function. (embl.de)
  • The Ca$\sp{2+}$-dependent cell adhesion molecule, N-cadherin, plays a functional role in chondrogenesis. (jefferson.edu)
  • As E-cadherin is an epithelial adhesion molecule, this change allows the cancer cells cultured with CAF to migrate more easily, contributing to metastasis. (news-medical.net)
  • Box plots representing the levels of soluble N-cadherin (sN-CAD) in the sera of 87 control subjects and 73 sarcoma patients. (biomedcentral.com)
  • Background An increasing variety of publications are suggesting that galectin-3 (Gal-3) and soluble cadherin fragments, such as for example E-cadherin (sE-CAD) and N-cadherin (sN-CAD), could be considered as cancers markers. (fk866.net)
  • Typical cadherins are different from other types of cadherins and consist of one or more extracellular repeat domains. (wikipedia.org)
  • The extracellular domains of CDH23 and PCDH15 differ in their structure from classical cadherins and their cytoplasmic domains bind to distinct effectors, suggesting that evolutionary pressures have shaped the two cadherins for their function in mechanotransduction. (elsevier.com)
  • The results showed that peptide 6 (LVVQAADLQG) derived from the EC-2 domain and peptide 8 derived from the EC-4 domain (YTALIIATDN) of E-cadherin were more effective in inhibiting single cell adhesion than peptides from other domains (EC-1, EC-3) of E-cadherin. (ku.edu)
  • In the closed monomers of cadherin, β-strand A of the EC1 domain is held under conformational strain through anchoring via tryptophan-2 at one end and Ca2+-bound-glutamine-11 at the other end This conformation favors the 'swapping' of β-strands on apposing cadherin EC1 domains. (mechanobio.info)
  • Cell adhesion simply by classical cadherins is mediated by dimerization of their EC1 domains through the "swapping" of N-terminal β-strands. (scienceofgreathealth.com)
  • Cadherin ectodomains bind between cells through the interaction of their EC1 domains which exchange or swap their N-terminal β-strand (the A* strand). (scienceofgreathealth.com)
  • Interestingly, all 11 substituted residues are solvent-exposed based on the crystal structure of the two NH2-terminal domains of murine E-cadherin 19. (pik-75.info)
  • The seven strands in the cadherin domain form two antiparallel sheets, one formed by strands D, E, and B and the other by strands A, G, F, and C. Without the conserved intersheet disulfide bond present in Ig domains, the strands in cadherin domains have a more cylindrical arrangement that has been termed a barrel. (pik-75.info)
  • Residue D29 is conserved among cadherin domains (Fig. 1 A). Based on our model, Roflumilast the side chain of D29 is predicted to point into the core of the structure and hydrogen bond to Y36. (pik-75.info)
  • CADG : Dystroglycan-type cadherin-like domains. (embl-heidelberg.de)
  • how do the intracellular domains of cadherins work? (flashcardmachine.com)
  • Crystal structures have revealed that multiple cadherin domains form Ca2+-dependent rod-like structures with a conserved Ca2+-binding pocket at the domain-domain interface. (embl.de)
  • We also analyzed the aberrant E-cadherin mRNAs in the gastric tumours and found that 7 tumours (18%) had aberrant mRNAs in addition to the normal mRNA. (biomedcentral.com)
  • Aberrant localization of β-catenin was higher in the E-cadherin negative group than in E-cadherin positive group. (elsevier.com)
  • p15 and E-cadherin aberrant methylation are very frequent in adult acute monocytic leukemia. (jahjournal.org)
  • Both cadherins had been found to become co-expressed in carcinomas with aberrant P-cadherin appearance and conserved E-cadherin. (clarkfrancis.com)
  • Moreover, this implies that, in queens, the aberrant appearance of P-cadherin is certainly an improved marker of mammary carcinomas intense behaviour compared to the reduced amount of E-cadherin appearance. (clarkfrancis.com)
  • To demonstrate the role of N-cadherin (N-cad) in maintaining the progenitor status of primary human limbal epithelial cells in vitro. (fujita-hu.ac.jp)
  • The objective of this project was to evaluate the biological activity of peptides derived from the EC-4 domain of E-cadherin in inhibiting E-cadherin-mediated cell-cell adhesion. (ku.edu)
  • Here, we show that planar polarization of flows emerges from polarized fluctuations in the levels of E-cadherin clusters that produce transient and oscillating asymmetries of coupling. (pasteur.fr)
  • The cadherin family is essential in maintaining the cell-cell contact and regulating cytoskeletal complexes. (wikipedia.org)
  • It has been observed that cells containing a specific cadherin subtype tend to cluster together to the exclusion of other types, both in cell culture and during development. (wikipedia.org)
  • 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)
  • It is this region of the cadherins that allows cell-adhesion and the essential feature of metazoan multicellularity. (embl.de)
  • In addition to cell adhesion, cadherins also mediate morphogenesis, cytoskeletal organization, and cell migration. (rndsystems.com)
  • These studies show that cadherin 23 (CDH23) and protocadherin 15 (PCDH15) form several of the extracellular filaments that connect the stereocilia and kinocilium of a hair cell into a bundle. (elsevier.com)
  • Müller, U 2008, ' Cadherins and mechanotransduction by hair cells ', Current Opinion in Cell Biology , vol. 20, no. 5, pp. 557-566. (elsevier.com)
  • It has the ability to inhibit cell proliferation by the upregulation of p27 involved in the cell cycle regulation [ 5 ], although the mechanism by which E-cadherin regulates p27 is still unclear. (biomedcentral.com)
  • Classic cadherins, comprising multiple subtypes, mediate selective cell-cell adhesion based on their subtype-specific binding nature. (jneurosci.org)
  • Human lung cancer cell line H460 cells were stained with Cadherin 11 (clone 16G5) PE/Cyanine7 (filled histogram) or mouse IgG1, κ PE/Cyanine7 isotype control (open histogram). (biolegend.com)
  • Cadherins are used in cell-cell adhesion and migration in a variety of tissues. (rupress.org)
  • Orderly assembly of classical cadherins governs cell adhesion and tissue maintenance. (elsevier.com)
  • It has been found to be related to fetal kidney development and has been identified as a major cadherin in renal proximal tubules where conventional renal cell carcinoma originates. (affordableihcinstruments.com)
  • Western blot analysis of E-Cadherin on A431 cell lysate. (huabio.com)
  • E-cadherin is shown here to be a cellular substrate for a bacterial toxin and represents the identification of a mechanism of action, cell-surface proteolytic activity, for a bacterial toxin. (elsevier.com)
  • To further expand and validate these in vitro biochemical studies, immunofluorescent histochemistry was performed, which colocalized N-cadherin and β-catenin to the same site of Sertoli-Sertoli and Sertoli-germ cell AJs, possibly ectoplasmic specializations near the basal compartment, at the lower third of the seminiferous epithelium in vivo as well as between Sertoli cells cultured in vitro. (popcouncil.org)
  • A stromal cell line also expressed N-cadherin in accordance with its fibroblastic morphology. (elsevier.com)
  • N-cadherin localized to areas of cell-cell contact in all cells that expressed it. (elsevier.com)
  • in contrast, E-cadherin expressing cell lines did not co-aggregate with stromal cells. (elsevier.com)
  • Lateral "cis" interfaces between cadherins from the same cell surface have been proposed to play a role in cadherin clustering. (elsevier.com)
  • L cell transfected with the mouse R-cadherin cDNA acquired a cadherin-mediated cell-cell adhesiveness as found for other cadherins. (houstonmethodist.org)
  • Auditory cortex interneuron development requires cadherins operating hair-cell mechanoelectrical transduction. (ifm-institute.org)
  • In fact, in adults, the majority of embryos showed the proper distribution of E-cadherin just beneath the membrane surfaces of all blastomeres and the percentage of embryos with this distribution increased with the increase in cell number during development. (uniss.it)
  • type I) are very similar in sequence and in structure yet the small differences between them are adequate to operate a vehicle cell patterning behavior 12 13 Including the difference in the binding affinities between N- and E-cadherin can be on the purchase of just one 1 kcal.mol-1 12. (scienceofgreathealth.com)
  • Furthermore, P-cadherin appearance was positive in every mucinous carcinomas and carcinosarcomas an undeniable fact that factors to a basal/myoepithelial cell histogenesis origins or type of differentiation of the tumour types [16,60,61], since P-cadherin is certainly a well-recognized biomarker of basal mammary carcinomas in human beings [6,62-65]. (clarkfrancis.com)
  • Abrogation of E-cadherin-mediated cell-cell contact in mouse embryonic stem cells results in reversible LIF-independent self-renewal. (ox.ac.uk)
  • We have previously demonstrated that differentiation of embryonic stem (ES) cells is associated with downregulation of cell surface E-cadherin. (ox.ac.uk)
  • In this study, we assessed the function of E-cadherin in mouse ES cell pluripotency and differentiation. (ox.ac.uk)
  • what does the type of cadherins involved dictate concerning cell-cell anchoring junctions? (flashcardmachine.com)
  • Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. (embl.de)
  • Solution structure of the epithelial cadherin domain responsible for selective cell adhesion. (embl.de)
  • Glycosyltransferase POMGNT1 deficiency strengthens N-cadherin-mediated cell-cell adhesion. (mpg.de)
  • We conclude that high intracellular PKCK2activity confers anoikis resistance on esophageal cancer cells by inducing E- to N-cadherin switching. (elsevier.com)
  • In T-cadherin-deficient mice, APN failed to associate with cardiac tissue, and its levels dramatically increased in the circulation. (nih.gov)
  • Lymphocytes extracted from rejecting renal tissue are known to express the α E β 7 -integrin (CD103), a receptor for E-cadherin expressed on epithelial cells. (lww.com)
  • The capacity of CD103+ T cells to bind E-cadherin on tubular epithelial cells may be an important factor in the pathogenesis of specific tissue damage observed in acute renal allograft rejection. (lww.com)
  • There are multiple classes of cadherin molecule, each designated with a prefix (generally noting the type of tissue with which it is associated). (blogspot.com)
  • Objectives: To study Methylation in the promoter region of p15 and E Cadherin genes from tissue samples of head & neck cancer and compare it with peripheral blood. (journalcra.com)
  • In lactating or pseudo-lactating mammary tissue, P-cadherin immunoreactivity was observed in the cytoplasm of luminal epithelial cells and in luminal secretion, in line with data from previous studies in human breast [58] and canine mammary gland [59]. (clarkfrancis.com)
  • The E-cadherin staining was limited to the membrane of the epithelial layer. (elsevier.com)
  • Further investigation using this system resulted in a model whereby cadherins are constantly and spontaneously recruited to the plasma membrane , form lateral catenin-dependent associations and are subsequently released from these clusters in an active, ATP-dependent manner. (mechanobio.info)
  • Additionally, immunofluorescence data demonstrated that cells lacking PIPKIγ lost E-cadherin at the plasma membrane. (elsevier.com)
  • Wagoner, MP , Ling, K & Anderson, RA 2008, Tracking the transport of E-cadherin to and from the plasma membrane . (elsevier.com)
  • In light of this, several groups have proposed that in carcinomas, E-cadherin functions as an invasion suppressor molecule such that its loss permits or enhances the invasion of adjacent normal tissues. (biomedcentral.com)
  • We sought to determine the prevalence and nature of E-cadherin alterations in 'sporadic' gastric carcinomas. (unisi.it)
  • Moreover, P-cadherin positive carcinomas had an eightfold likelihood of developing neoplastic emboli than unfavorable tumours. (clarkfrancis.com)
  • Conclusions The full total outcomes demonstrate a romantic relationship between P-cadherin appearance and intense natural behavior of feline mammary carcinomas, recommending that P-cadherin may be regarded an indicator of poor prognosis within this pet species. (clarkfrancis.com)
  • Further analysis with follow-up research in feline types should be executed to be able to measure the prognostic worth of P-cadherin appearance in E-cadherin positive carcinomas. (clarkfrancis.com)
  • Nevertheless, the association between P-cadherin appearance as well as the histological kind of carcinomas had not been achieved in today's study, is not yet confirmed in human beings [5] and isn't consensual in various other pet models such as for example canines [16,56]. (clarkfrancis.com)
  • Then cells were intracellularly stained with purified 2.5 µg/ml of CD324 (E-Cadherin, clone DECMA-1) in blocking buffer overnight at 4°C followed by 2.5 µg/ml of DyLight™ 594 Goat anti-rat IgG (minimal x-reactivity) incubation for 1 hour at 4°C. Nuclei were counterstained with DAPI and are shown in blue. (biolegend.com)
  • Be the first to review Mouse P-Cadherin (NP_001032898) VersaClone cDNA and earn rewards! (rndsystems.com)
  • Have you used Mouse P-Cadherin (NP_001032898) VersaClone cDNA? (rndsystems.com)