Cadherins: 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.Desmosomal Cadherins: A single-pass transmembrane glycoproteins that mediate CALCIUM-dependent CELL ADHESION and are core components of DESMOSOMES.Desmogleins: A group of desmosomal cadherins with cytoplasmic tails that resemble those of classical CADHERINS.Desmoplakins: Desmoplakins are cytoskeletal linker proteins that anchor INTERMEDIATE FILAMENTS to the PLASMA MEMBRANE at DESMOSOMES.Desmocollins: A group of desmosomal cadherins with cytoplasmic tails that are divergent from those of classical CADHERINS. Their intracytoplasmic domains bind PLAKOGLOBIN; PLAKOPHILINS; and DESMOPLAKINS.Catenins: 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.gamma Catenin: 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.Desmosomes: 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)alpha Catenin: A catenin that binds F-ACTIN and links the CYTOSKELETON with BETA CATENIN and GAMMA CATENIN.Desmoglein 2: A CALCIUM-dependent adhesion molecule of DESMOSOMES that also plays a role in embryonic STEM CELL proliferation.Cell Adhesion: Adherence of cells to surfaces or to other cells.Cytoskeletal Proteins: 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.Desmoglein 1: A desmosomal cadherin that is an autoantigen in the acquired skin disorder PEMPHIGUS FOLIACEUS.Intercellular Junctions: 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)beta Catenin: 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.Adherens Junctions: 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.Cell Adhesion Molecules: 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.Cell Aggregation: The phenomenon by which dissociated cells intermixed in vitro tend to group themselves with cells of their own type.Desmoglein 3: A desmosomal cadherin that is an autoantigen in the acquired skin disorder PEMPHIGUS VULGARIS.Armadillo Domain Proteins: 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.Trans-Activators: Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.Morphogenesis: 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.L Cells (Cell Line): A cultured line of C3H mouse FIBROBLASTS that do not adhere to one another and do not express CADHERINS.Plakophilins: Members of the armadillo family of proteins that are found in DESMOSOMES and interact with various proteins including desmocadherins; DESMOPLAKIN; ACTIN FILAMENTS; and KERATINS.Protein Structure, Tertiary: 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.Molecular Sequence Data: 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.Cell Communication: 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.Protein Binding: 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.Amino Acid Sequence: 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.Pemphigus: Group of chronic blistering diseases characterized histologically by ACANTHOLYSIS and blister formation within the EPIDERMIS.Receptor-Like Protein Tyrosine Phosphatases, Class 2: 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.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.Gene Expression Regulation, Developmental: 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.Xenopus Proteins: 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.Vinculin: 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.Receptor-Like Protein Tyrosine Phosphatases, Class 8: A subclass of receptor-like protein tryosine phosphatases that contain an extracellular RDGS-adhesion recognition motif and a single cytosolic protein tyrosine phosphate domain.Keratinocytes: 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, Cultured: 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.Actins: 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.Cell Polarity: 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.Epithelial Cells: 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.PhosphoproteinsRecombinant Fusion Proteins: 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.Cell-Matrix Junctions: Specialized areas at the CELL MEMBRANE where a cell attaches to the EXTRACELLULAR MATRIX or other substratum.In Situ Hybridization: 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.Signal Transduction: 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.Fluorescent Antibody Technique: 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.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Transfection: 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.Precipitin Tests: 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.DNA, Complementary: 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.Cell Movement: The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.Immunoblotting: 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.Integrins: 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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.rac1 GTP-Binding Protein: 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.Epidermis: 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).Acantholysis: 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.Gastrulation: 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.Cytoplasm: 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)Repetitive Sequences, Amino Acid: A sequential pattern of amino acids occurring more than once in the same protein sequence.Microscopy, Immunoelectron: 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.Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents.Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Mechanotransduction, Cellular: 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.Synaptophysin: 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.Models, Biological: 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.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.rho GTP-Binding Proteins: 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.Calcium: 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.Membrane Proteins: 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.Xenopus laevis: 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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Tumor Cells, Cultured: 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.Mutation: 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.Sequence Alignment: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Embryo, Nonmammalian: The developmental entity of a fertilized egg (ZYGOTE) in animal species other than MAMMALS. For chickens, use CHICK EMBRYO.cdc42 GTP-Binding Protein: 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.CHO Cells: 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.Intermediate Filaments: 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.Gene Expression: 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
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. ...
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. [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, ...
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 ...
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.
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
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 (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 ...
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.
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 ...
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 ...
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 ...
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 ...
There is increasing evidence supporting DNA virus regulation of the cell adhesion and tumour suppressor protein, E-cadherin. At the6 STF-62247 conveying cells. Upon inhibiting DNMT activity using 5-Aza-2-deoxycytidine, E-cadherin transcription was restored in the presence of HPV16 At the6. The E-cadherin promoter was not directly methylated, however a mutational analysis showed general promoter repression and reduced binding of the transactivators Sp1 and AML1 and the repressor Slug. Manifestation of At the7 with At the6 resulted in a further reduction in surface E-cadherin levels. This is usually the first statement of HPV16 At the6-mediated transcriptional repression of this adhesion molecule and tumour suppressor protein. Introduction Cervical malignancy is usually the second most common malignancy among women worldwide, with over 500,000 new cases being diagnosed annually [1]. The majority of cases of cervical malignancy are a result of contamination with high-risk, oncogenic human ...
TY - JOUR. T1 - Dysadherin, a cancer-associated cell membrane glycoprotein, down-regulates E-cadherin and promotes metastasis. AU - Ino, Yoshinori. AU - Gotoh, Masahiro. AU - Sakamoto, Michiie. AU - Tsukagoshi, Kiyomi. AU - Hirohashi, Setsuo. PY - 2002/1/8. Y1 - 2002/1/8. N2 - We report the cloning and characterization of a cancer-associated cell membrane glycoprotein recognized by mAb NCC-3G10. The antibody showed strong reactivity to a wide variety of cancer cells, but only to a limited number of normal cells including lymphocytes, endothelial cells, and basal cells of stratified squamous epithelium. The cDNA for the antigen encodes 178 aa, which includes a putative signal sequence, a potential O-glycosylated extracellular domain, a single transmembrane domain, and a short cytoplasmic tail. Transfection of the cDNA into PLC/PRF/5 liver cancer cells resulted in reduced cell-cell adhesiveness, based on both morphology and results of Ca2+-dependent cell aggregation assay. In transfected cells, ...
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, genes encoding calcium-dependent, membrane-associated glycoproteins. Mapped to a previously identified cluster of cadherin genes on chromosome 16q22.1, the gene localizes with superfamily members CDH1, CDH3, CDH5, CDH8 and CDH11. The protein consists of an extracellular domain containing 6 cadherin domains, a transmembrane region and a truncated cytoplasmic domain but lacks the prosequence and tripeptide HAV adhesion recognition sequence typical of most classical cadherins. Expression is exclusively in kidney, where the protein functions as the principal mediator of homotypic cellular recognition, playing a role in the morphogenic direction of tissue development. Alternatively spliced transcript variants encoding distinct isoforms have been identified. [provided by RefSeq, Mar 2011 ...
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin, and gamma-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with alpha-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show ...
Cell-surface markers of EMT. A change in expression of E-cadherin is the prototypical epithelial cell marker of EMT. E-cadherin is expressed in epithelial cells, and its expression is decreased during EMT in embryonic development, tissue fibrosis, and cancer (65). Moreover, loss of E-cadherin function promotes EMT (4, 66). In recent years, changes in the level of expression of different cadherins, so-called cadherin switches, have been increasingly used to monitor EMT. Indeed, the cadherin switch from E-cadherin to N-cadherin, which is expressed in mesenchymal cells, fibroblasts, cancer cells, and neural tissue, has often been used to monitor the progress of EMT during embryonic development and cancer progression. In addition, because OB-cadherin is a more definitive marker for activated fibroblasts, an E-cadherin-OB-cadherin switch is of interest for type 2 EMT associated with fibrogenesis (67). EMT is associated classically with a relocation of cells from a basement membrane microenvironment ...
Clone REA199 recognizes CD144 (VE-Cadherin), a 120 KDa type II cadherin. Cadherins are cell adhesion molecules and mediate Ca2+ dependent homophilic interactions. CD144 contains five extracellular cadherin (EC) domains and like other cadherins can interact directly via its C-terminus with cytoplasmic proteins such as β-catenin, plaktoglobin, and p120. Plaktoglobin und β-catenin bind to α-catenin, which in turn interacts with several actin-binding proteins, α-actinin, ajuba, zonula occludens-1 (ZO-1). Further indirect interactions of CD144 with partners such as SHP-2, VEGFR-2, Csk, and PAR-3, 6 allows CD144 to not only regulate the stability and strength of cell adhesion but also to serve functions such as sensing of shear forces, anti-proliferative, and anti-apoptotic effects. Additional information: Clone REA199 displays negligible binding to Fc receptors. - Schweiz
Cadherin 2, also known as N-cadherin, is a member of the cadherin superfamily of predominantly Ca2+-dependent cell surface adhesion proteins.30 In the heart, cadherin 2 is located at the intercalated disc, a complex and highly organized intercellular structure that ensures structural integrity and functional synchronization across the myocardium through the tight electromechanical coupling of cardiomyocytes.30,31 In the intercalated disc, intercellular communication and adhesion are achieved through 3 main junctional structures forming functional zones, the gap junctions, the fascia adherens junctions, and the desmosomes, with the latter 2 being the main contributors to cell-cell adhesion.30-32 In desmosomes, desmosomal cadherins (desmocollin and desmoglein) are mainly anchored to the intermediate filaments of the cytoskeleton through many intracellular protein partners, whereas in fascia adherens junctions, the classical cadherin, N-cadherin, is primarily anchored to the actin microfilaments of ...
This gene is a member of the protocadherin beta gene cluster, one of three related gene clusters tandemly linked on chromosome five. The gene clusters demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The beta cluster contains 16 genes and 3 pseudogenes, each encoding 6 extracellular cadherin domains and a cytoplasmic tail that deviates from others in the cadherin superfamily. The extracellular domains interact in a homophilic manner to specify differential cell-cell connections. Unlike the alpha and gamma clusters, the transcripts from these genes are made up of only one large exon, not sharing common 3 exons as expected. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins. Their specific functions are unknown but they most likely play a critical role in the establishment and function of specific cell-cell neural connections ...
Cadherins play an important role in morphogenesis and have recently been implicated in the regulation of cell proliferation, however the mechanisms by which they function are poorly understood. In the vertebrate CNS, loss of ,italic,N-cadherin (N-cad),,/, results in impaired neuroepithelial integrity. Zebrafish ,italic,N-cad,,/, null mutants also exhibit a transient increase in neurons and in cell proliferation in the neural tube. Here, we investigate the cellular and molecular basis for this phenotype, using multiple ,italic,N-cad,,/, alleles with distinct molecular properties. We confirm that cell proliferation is enhanced in ,italic,N-cad,,/, mutants, but contrary to previous findings, we observe that the increase is sustained over multiple stages of development. At the cellular level, loss of ,italic,N-cad,,/, results in a shorter cell cycle. Furthermore, we demonstrate that hyperproliferation is not linked to abnormal beta-catenin localization, suggesting that Wnt signaling is not ...
Cadherins play an important role in morphogenesis and have recently been implicated in the regulation of cell proliferation, however the mechanisms by which they function are poorly understood. In the vertebrate CNS, loss of ,italic,N-cadherin (N-cad),,/, results in impaired neuroepithelial integrity. Zebrafish ,italic,N-cad,,/, null mutants also exhibit a transient increase in neurons and in cell proliferation in the neural tube. Here, we investigate the cellular and molecular basis for this phenotype, using multiple ,italic,N-cad,,/, alleles with distinct molecular properties. We confirm that cell proliferation is enhanced in ,italic,N-cad,,/, mutants, but contrary to previous findings, we observe that the increase is sustained over multiple stages of development. At the cellular level, loss of ,italic,N-cad,,/, results in a shorter cell cycle. Furthermore, we demonstrate that hyperproliferation is not linked to abnormal beta-catenin localization, suggesting that Wnt signaling is not ...
Cadherin like 23 (or Cadherin 23) is, like other members of the cadherin family, a calcium-dependent cell adhesion glycoprotein that preferentially…
Sigma-Aldrich offers abstracts and full-text articles by [Maria Sideridou, Roubini Zakopoulou, Konstantinos Evangelou, Michalis Liontos, Athanassios Kotsinas, Emmanouil Rampakakis, Sarantis Gagos, Kaoru Kahata, Kristina Grabusic, Kalliopi Gkouskou, Ioannis P Trougakos, Evangelos Kolettas, Alexandros G Georgakilas, Sinisa Volarevic, Aristides G Eliopoulos, Maria Zannis-Hadjopoulos, Aristidis Moustakas, Vassilis G Gorgoulis].
RESULTS: COL6A3 was highly expressed in tissues and cells of bladder cancer. COL6A3 silencing could inhibit the cell proliferation and angiopoiesis. In addition, COL6A3 silencing obviously suppressed the levels of matrix metalloproteinase-2 (MMP2), Matrix metalloproteinase-9 (MMP9), and vimentin. On the contrary, the levels of epithelium-specific cell-cell adhesion molecule (E-cadherin) and tumor inhibitor of metalloproteinase-1 (TIMP-1) were significantly increased. Furthermore, we found that COL6A3 silencing reduced the activity of p-Smad2, p-Smad3, and transforming growth factor β (TGF-β ...
Our in vitro results revealed that, in HNSCC cells, the selective Cox-2 inhibitors led to the suppression of the EMT by restoring the expression of E-cadherin through the downregulation of its transcriptional repressors. Moreover, the extent of the effect of Cox-2 inhibition was shown to depend on the baseline expression levels of both E-cadherin and Cox-2 in each cell; i.e., tumor cells expressing lower E-cadherin and higher Cox-2 are expected to be more sensitive to Cox-2 inhibition in terms of the restoration of E-cadherin expression. Such a finding is consistent with a previous study of bladder cancer cells using another Cox-2 inhibitor, etodolac. In that study, etodolac upregulated E-cadherin expression only in T24 cells, which express the highest level of Cox-2 and the lowest level of E-cadherin; it did not do so in 5637 cells or K47 cells, which express a lower level of Cox-2 and a higher level of E-cadherin [42]. Interestingly, using the same three bladder cancer cell lines and three ...
Cadherin-17 is a protein that in humans is encoded by the CDH17 gene. This gene is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. The encoded protein is cadherin-like, consisting of an extracellular region, containing 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. GRCh38: Ensembl release 89: ENSG00000079112 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000028217 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Kremmidiotis G, Baker E, Crawford J, Eyre HJ, Nahmias J, Callen DF (Aug 1998). "Localization of human cadherin genes to chromosome ...
The anterior-posterior axis of the vertebrate embryo undergoes a dramatic elongation during early development. Convergence and extension of the mesoderm, occurring during gastrulation, initiates the narrowing and lengthening of the embryo. However the lengthening of the axis continues during post-gastrula stages in the tailbud region, and is thought to involve convergent extension movements as well as other cell behaviors specific to posterior regions. We demonstrate here, using a semi-dominant N-cadherin allele, that members of the classical cadherin subfamily of cell-cell adhesion molecules are required for tailbud elongation in the zebrafish. In vivo imaging of cell behaviors suggests that the extension of posterior axial mesodermal cells is impaired in embryos that carry the semi-dominant N-cadherin allele. This defect most likely results from a general loss of cell-cell adhesion in the tailbud region. Consistent with these observations, N-cadherin is expressed throughout the tailbud during post
Differentiation and proliferation of hematopoietic progenitors take place in the bone marrow and is a tightly controlled process. Cell adhesion molecules of the integrin and immunoglobulin families have been shown to be involved in these processes, but almost nothing was known about the involvement of the cadherin family in the hematopoietic system. A PCR screening of RNA of human bone marrow mononuclear cells with specific primers for classical cadherins revealed that E-cadherin, which is mainly expressed by cells of epithelial origin, is also expressed by bone marrow cells. Western blot analysis and immunofluorescence staining of bone marrow sections confirmed this unexpected finding. A more detailed analysis using immunoaffinity columns and dual color flow cytometry showed that the expression of E-cadherin is restricted to defined maturation stages of the erythropoietic lineage. Erythroblasts and normoblasts express E-cadherin, mature erythrocytes do not. A functional role of E-cadherin in ...
The embryonic myotome is the source of all epaxial and hypaxial skeletal muscles. The mechanisms underlying myotome development were recently reevaluated (Brent and Tabin, 2002; Buckingham, 2001; Hollway and Currie, 2003; Kalcheim and Ben-Yair, 2005). Studies in avian embryos showed that the dorsomedial lip (DML) of the dermomyotome (DM) and, later, the ventrolateral lip (VLL) contribute to myotome growth in medial and lateral orientations, respectively (Denetclaw et al., 2001; Denetclaw et al., 1997; Denetclaw and Ordahl, 2000; Ordahl et al., 2001). Our studies distinguished at least two separable waves that account for the formation of the postmitotic myotome. A first wave of pioneer myoblasts constitutes the medial region of the epithelial somite with cells expressing Myod and Myf5. Upon sclerotome dissociation, pioneers delaminate, migrate towards the rostral somitic domain, and, from this region, generate myofibers in rostrocaudal and mediolateral directions (Kahane et al., 1998b; Kahane et ...
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The progression from Cervical Intraepithelial Neoplasia (CIN) to carcinoma in situ (CIS) to invasive squamous cell carcinoma (SCC) is associated with Epithelial to Mesenchymal Transition (EMT). EMT is triggered by secreted growth factors of tumor and host cells. Epidermal Growth Factor (EGF) and Epidermal Growth Factor Receptor (EGFR) are up-regulated in stromal invasion and metastasis, and up-regulate the zinc-finger transcription factor Snail-1, which mediates EMT by inducing E-cadherin down-regulation of and vimentin up-regulation. Adhesion molecules and E-cadherin loss are associated with the acquisition of invasive capacity, high tumor grade and poor prognosis.. In a large series of cervical lesions (CIN1, 2, 3, CIS, SCC), we investigated EMT immuno-expression with a panel of pertinent Antibodies, namely EGFR, Snail-1, E-cadherin, Vimentin, p16, p53. In this series we were able to conclude that. reduced E-Cad expression and acquisition of VIM expression were significantly higher in the ...
Intercellular adhesion and electrical excitability are considered separate cellular properties. Studies of myelinated fibres, however, show that voltage-gated sodium channels (VGSCs) aggregate with cell adhesion molecules at discrete subcellular locations, such as the nodes of Ranvier. Demonstration of similar macromolecular organization in cardiac muscle is missing. Here we combine nanoscale-imaging (single-molecule localization microscopy; electron microscopy; and angle view scanning patch clamp) with mathematical simulations to demonstrate distinct hubs at the cardiac intercalated disc, populated by clusters of the adhesion molecule N-cadherin and the VGSC NaV1.5. We show that the N-cadherin-NaV1.5 association is not random, that NaV1.5 molecules in these clusters are major contributors to cardiac sodium current, and that loss of NaV1.5 expression reduces intercellular adhesion strength. We speculate that adhesion/excitability nodes are key sites for crosstalk of the contractile and ...
Purpose: To predict lymph node metastasis and prognosis in head and neck squamous cell carcinoma (HNSCC). Results: The combination of membranous E-cadherin and membranous epidermal growth factor receptor (EGFR) quantified by QD technology with age, gender, and grade had greater predictive power than any of the single biomarkers or the two combined biomarkers quantified by conventional immunohistochemistry (IHC). The predictive power of this model was validated in another independent sample set; the predictive sensitivity of this model for LNM was 87.5%, with specificity up to 97.4%, and accuracy 92.9%. Furthermore, a higher membranous E-cadherin level was significantly correlated with better overall and disease-free survival (OS, DFS; P = 0.002, 0.033, respectively), while lower cytoplasmic vimentin and membranous EGFR levels were significantly correlated with better OS (P = 0.016 and 0.021, respectively). The combined biomarkers showed a stronger prognostic value for OS and DFS than any of the ...
This gene is a member of the cadherin superfamily of calcium-dependent cell-cell adhesion molecules. This non-classical cadherin appears to be exclusively expressed in the mitral and tufted cells in the main and accessory olfactory bulbs of the brain, suggesting a possible role in the formation and maintenance of neuronal networks. Alternatively spliced transcript variants encoding different isoform have been identified ...
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By Ramis-Conde, Ignacio Drasdo, Dirk; Anderson, Alexander R A; Chaplain, Mark A J ABSTRACT In this article, we show, using a mathematical multiscale model, how cell adhesion may be regulated by interactions between E-cadherin and beta-catenin and how the control of cell adhesion may be related to cell migration, to the epithelial- mesenchymal transition and to invasion in populations of eukaryotic cells. E-cadherin mediates cell-cell adhesion and plays a critical role in the formation and maintenance of junctional contacts between cells. Loss of E-cadherin-mediated adhesion is a key feature of the epithelial-mesenchymal transition. beta-catenin is an intracellular protein associated with the actin cytoskeleton of a cell. E- cadherins bind to beta-catenin to form a complex which can interact both with neighboring cells to form bonds, and with the cytoskeleton of the cell. When cells detach from one another, beta-catenin is released into the cytoplasm, targeted for degradation, and downregulated. ...
A-CAM (adherens-junction-specific cell adhesion molecule) is a calcium-dependent adhesion molecule which is associated with intercellular adherens junctions in various tissues (Volk & Geiger, 1986, J. Cell Biol. 103, 1441-1450 and 1451-1464). In the present report, we have investigated the distribution of A-CAM during avian morphogenesis by immunofluorescence microscopy and immunoblotting. A-CAM appeared at the onset of gastrulation on developing mesodermal and endodermal cells and was then expressed on tissues derived from the three primary germ layers. During embryonic life, A-CAM was constitutively expressed in a number of tissues including the central and peripheral nervous system, myocardium, muscles, notochord, skin and lens whereas it was found transiently in many tissues ranging from the nephritic tubules and the endoderm of visceral arches to ectodermal placodes. In the adult, in addition to the nervous system, A-CAM was restricted to the skin, lens, heart and testis, and exhibited an ...
Full-length coding sequences of two novel human cadherin cDNAs were obtained by sequence analysis of several EST clones and 5 and 3 rapid amplification of cDNA ends (RACE) products. Exons for a third cDNA sequence were identified in a public-domain
ED01-03 Preclinical data have generated an interesting hypothesis that suggests that the sensitivity of NSCLC, pancreatic and colon cell lines and/or tumor xenografts to EGFR inhibitors is dependant upon the degree to which they have undergone an epithelial to mesenchymal transition (EMT). NSCLC lines which express the epithelial cell junction protein E-cadherin showed greater sensitivity to EGFR inhibition in vitro and in xenografts. In contrast, NSCLC lines having undergone EMT, expressing vimentin and/or fibronectin, were insensitive to the growth inhibitory effects of erlotinib. In the E-cadherin positive cells inhibition of EGFR activity leads to a reduction in the phosphorylation of Akt. In contrast, however, those cells that have lost E-cadherin expression and gained the expression of mesenchymal markers, do not show a reduction in phosphorylation of Akt even though EGFR is present and can be inhibited. Interestingly the E-cadherin expressing cells also express ErbB3 and we believe that ...
Chemotaxis is the stimulated directional migration of cells in response to chemotactic factors, manifested for instance during leukocyte interaction with chemoattractants in inflammation. The N-formyl-Met-Leu-Phe (fMLF) bacterial peptide family is particularly potent in attracting and activating neutrophilic granulocytes. To accomplish defined circumstances for recruitment and activation of cells, we fabricated semitransparent gold-coated glass coverslips functionalized with chemoattractant fMLF receptor peptide agonist analogues. Peptides based on a common leading four-amino-acid sequence Gly-Gly-Gly-Cys were thus coupled to two potent fMLF receptor agonists, N-formyl-Tyr-Nle-Phe-Leu- Nle-Gly-Gly-Gly-Cys and N-formyl-Met-Leu-Phe-Gly-Gly-Gly-Cys, and a formylated control peptide, N-formyl-Gly-Gly-Gly-Cys. They were anchored via the SH group of Cys either directly to the gold surface or a mixed self-assembled monolayer composed of maleimide- and hydroxyl-terminated oligo(ethylene glycol) ...
E-cadherin and its transcriptional repressor Snail1 (Snai1) are two factors that control epithelial phenotype. Expression of Snail1 promotes the conversion of epithelial cells to mesenchymal cells, and occurs concomitantly with the downregulation of E-cadherin and the upregulation of expression of mesenchymal genes such as those encoding fibronectin and LEF1. We studied the molecular mechanism controlling the expression of these genes in mesenchymal cells. Forced expression of E-cadherin strongly downregulated fibronectin and LEF1 RNA levels, indicating that E-cadherin-sensitive factors are involved in the transcription of these genes. E-cadherin overexpression decreased the transcriptional activity of the fibronectin promoter and reduced the interaction of beta-catenin and NF-kappaB with this promoter. Similar to beta-catenin, NF-kappaB was found, by co-immunoprecipitation and pull-down assays, to be associated with E-cadherin and other cell-adhesion components. Interaction of the NF-kappaB p65 ...
Mouse Monoclonal Anti-E-Cadherin Antibody (67A4) [FITC]. Epithelial Cell Marker, Adherens Junctions Marker. Validated: Flow. Tested Reactivity: Human. 100% Guaranteed.
The AlphaLISA® immunoassay kit for human E-cadherin enables the detection and quantitation of human E-cadherin in serum, buffered solution, and cell culture supernatants using a homogeneous AlphaLISA assay (no wash steps).
Immunohistochemical images of VE-cadherin at 5 and 20 weeks of age. (A) 5W of heterozygotes, (B) 5W of homozygotes, (C) 20W of heterozygotes, (D) 20W of homozyg
E- and N-cadherin expression in metastatic lesions. Sections of salivary glands (Sal, top left), pancreas (top right); axillary lymph nodes (LN, bottom right),
Intraperitoneal "seeding" is a distinctive pattern of dissemination that is unique to EOC and markedly differs from the hematogenous or lymphatic metastasis found for many other types of tumors. A key and initial rate-limiting step in the "seeding" of EOC is the survival of floating tumor cells in the peritoneal fluid. It is widely recognized that aggregation enables floating tumor cells to escape anoikis, although it is unclear whether tumor cells shed into the peritoneal fluid as aggregates or shed as single cells that then assemble into aggregates (3). The mechanisms that mediate adhesion between floating EOC cells are poorly understood. EOC cells express several integrins and extracellular matrix (ECM) proteins, and interactions between α5β1 integrin and fibronectin have been reported to mediate assembly of EOC cells into spheroids (22). Cadherins are transmembrane glycoproteins that have well-established functions in mediating homophilic cell adhesion (7). The role of cadherins in ...
The first step in the EMT is the loss of cell-cell cohesion, primarily by removal of cadherins. This step has been coined the "activation" step (Boyer et al., 1999). Although several mechanisms have been proposed for the loss of cadherins during the EMT, one possibility is that proteases cleave cadherins and subsequently release them from the cell surface (Werb, 1997; Werb and Yan, 1998). Recently, several cell surface proteins (DiStefano et al., 1993; Pan and Rubin, 1997; Black et al., 1997; Kahn et al., 1998), including cadherins (Volk et al., 1990; Paradies and Grunwald, 1993; Lochter et al., 1997; Herren et al., 1998; Bergers and Coussens, 2000), have been shown to be removed by proteolytic "sheddase" activity (Hooper et al., 1997). Although MMP-2 cleaves several cell surface proteins (reviewed in McCawley and Matrisian, 2001), there is no report of its processing cell-cell adhesion molecules, such as cadherins. Moreover, it is expressed late in the process, as the cells begin to disperse, ...
Nasopharyngeal carcinoma (NPC) is a unique tumour due to its aetiology, incidence pattern and its consistent association with Epstein-Barr virus (EBV). EBV encodes many viral proteins, which targets crucial cell cycle regulatory proteins. Cadherins are a family of transmembrane glycoproteins, which mediates Ca;{2+}-dependent intercellular adhesion. Epithelial (E)-cadherin is an important member of this family, which is expressed predominantly on the surface of epithelial cells. E-cadherin acts as an invasion/metastasis-suppressor gene, hence knowledge of the molecular mechanism that controls its expression or function is of primary importance in understanding the process of tumor invasion. Loss of E-cadherin function has been shown to potentiate tumor cell invasion and interestingly, a large number of invasive tumors do not involve mutation of E-cadherin, but rather down regulation of expression. Hence in this study, an attempt was made to evaluate the protein level expression pattern of ...
Drosophila four-jointed was shown to phosphorylate cadherin proteins within the Golgi apparatus, specifically the cadherin domains of the planar polarity (PCP) genes Fat and Daschous [1]. Mouse FJX1 inhibits dendrite extension in the hippocampus [2]. Mouse knockouts have abnormal hippocampus morphology and cultured hippocampal neurons show increased dendrite branching and extension. Addition of FJX1 protein to hippocampal cultures had the opposite effect, suggesting that FJX1 may act extracellularly. ...
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part1_c5.f6ea0ca.27fcf0de_boundary Content-Type: text/plain; charset=US-ASCII Content-Transfer-Encoding: 7bit We use Zymeds cadherins, fresh slides (a must) protease 1 4-8 min, 32 min incubation, Hope this helps. Dana --part1_c5.f6ea0ca.27fcf0de_boundary Content-Type: text/html; charset=US-ASCII Content-Transfer-Encoding: 7bit ,HTML,,FONT FACE=arial,helvetica,,FONT SIZE=2,We use Zymeds cadherins, fresh slides (a must) protease 1 4-8 min, 32 min ,BR,incubation, Hope this helps. Dana,/FONT,,/HTML, --part1_c5.f6ea0ca.27fcf0de_boundary ...
Mechanised forces are included at cadherin-based adhesion things to regulate morphology and strength of cell-cell junctions and organization of linked F-actin. Structured buy Ibutamoren mesylate (MK-677) Lighting Microscopy (SIM) signifies that these stress delicate protein focus at places within FAJs that are distinctive from the primary cadherin complicated protein. Furthermore, localization research using mutated variations … Read more Mechanised forces are included at cadherin-based adhesion things to regulate morphology. Read More ...
Mechanised forces are included at cadherin-based adhesion things to regulate morphology and strength of cell-cell junctions and organization of linked F-actin. Structured buy Ibutamoren mesylate (MK-677) Lighting Microscopy (SIM) signifies that these stress delicate protein focus at places within FAJs that are distinctive from the primary cadherin complicated protein. Furthermore, localization research using mutated variations … Read more Mechanised forces are included at cadherin-based adhesion things to regulate morphology. Read More ...
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Cadherins are a group of proteins that help cells stick together. They are the main components of certain types of junctions between cells. These connections help define how a cell will be integrated into a structure, like a layer of skin or an organ.
RecName: Full=Cadherin-1;AltName: Full=Epithelial cadherin; Short=E-cadherin;AltName: Full=Uvomorulin;AltName: Full=CAM 120/80;AltName: CD_antigen=CD324;Contains: RecName: Full=E-Cad/CTF1;Contains: RecName: Full=E-Cad/CTF2;Contains: RecName: Full=E-Cad/CTF3;Flags: ...
Construction of plasmids. The SYT-SSX expression vectors pCXN2-SYT-SSX1 and pCXN2-SYT-SSX2 were graciously provided by Dr. Shinya Tanaka (Hokkaido University, Sapporo, Japan; ref. 21). The inserts were digested by EcoRI and NotI and subcloned into vectors pcDNA4/myc-His and pcDNA4/TO/myc-His (Invitrogen, Carlsbad, CA). We also generated deletion mutants SYT-SSX1RD(−)/HisMyc and SYT-SSX2RD(−)/HisMyc lacking the COOH-terminal repression domain of SSX (also known as SSXRD) and a full-length SYT expression vector, pcDNA4/SYT/HisMyc. The full-length cDNAs for SSX1 and SSX2 were amplified using as template cDNA from K562 leukemia cells, and these cDNA fragments were cloned into pcDNA4/myc-His. The full-length Snail and Slug cDNAs were amplified from HeLa cells. The amplified fragments were subcloned into the expression vector p3xFLAG-CMV-10 (Sigma, St. Louis, MO).. Luciferase reporter gene constructs containing wild-type human E-cadherin promoter sequences (from −76 to −490) were generated by ...
Downregulated E-Cadherin Expression Indicates Worse Prognosis in Asian Patients with Colorectal Cancer: Evidence from Meta-Analysis. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
The second problem when trying to control the disease is the difficulty of spotting HDGC early. In fact its initial symptoms are very non-specific (stomach acidity and burping for example), so easy to miss. And without clear symptomology, early detection relies on searching gastric cells for lack of e-cadherin on the membrane (a malfunctioning e-cadherin also leaves the membrane to go inside the cell to be destroyed) with results that are not always reliable.. As consequence there has been a major effort to improve HDGC detection, and it is here that Sanches algorithm steps in. This new method has many advantages - it is semi-automated what allows, on one hand, the human operators to resort to their experience to choose the more representative cells, and on the other to rely on the computer to normalise results from cells with very different sizes and shapes, and work even with very heterogeneous cell populations. Resorting to images assured that the cells were hardly altered. All of these ...
Disassembly of CAJs and abrogation of cadherin‐mediated cell-cell adhesion is involved in changes of cell state including differentiation, apoptosis and tumor metastasis. For example, induction of apoptotic cell death or Ca2+ imbalance involves cleavage of cadherins and disassembly of CAJs (Herren et al., 1998; Ito et al., 1999; Vallorosi et al., 2000; Steinhusen et al., 2001). Furthermore, in the case of metastasis of epithelia tumors, inhibition of E‐cadherin‐mediated cell-cell adhesion is promoted by cleavage and secretion of extracytoplasmic E‐cadherin by MMPs (Lochter et al., 1997; Christofori and Semb, 1999; Noe et al., 2001). Although in some cell cultures PS1 was found mainly in the ER-Golgi system (De Strooper et al., 1997; Cupers et al., 2001), in cell cultures with extensive cell-cell contacts and in tissues PS1 concentrates mainly at the plasma membrane (Georgakopoulos et al., 1999; Nowotny et al., 2000; Xia et al., 2001) and, in the brain, this protein concentrates at ...
Cadherins, Ca2+-dependent adhesion molecules, are crucial for cell-cell junctions and remodeling. Cadherins form inter-junctional lattices by the formation of both cis and trans dimers. Here, we directly visualize and quantify the spatiotemporal dynamics of wild-type and dimer mutant N-cadherin interactions using time-lapse imaging of junction assembly, disassembly and a FRET reporter to assess Ca2+-dependent interactions. A trans dimer mutant (W2A) and a cis mutant (V81D/V174D) exhibited an increased Ca2+-sensitivity for the disassembly of trans dimers compared to the WT, while another mutant (R14E) was insensitive to Ca2+-chelation. Time-lapse imaging of junction assembly and disassembly, monitored in 2D and 3D (using cellular spheroids), revealed kinetic differences in the different mutants as well as different behaviors in the 2D and 3D environment. Taken together, these data provide new insights into the role that the cis and trans dimers play in the dynamic interactions of cadherins ...
article{2941298, abstract = {The epithelial-to-mesenchymal transition (EMT) confers an aggressive subtype associated with chemotherapy resistance in epithelial cancers. However, the mechanisms underlying the EMT and its associated signaling dysfunctions are still poorly understood. In two genetic models of MCF-7 breast cancer cells induced to EMT by WISP-2 silencing and Snail transformation, we investigated the status of several signaling elements downstream of G-protein receptors (GPR) and their functional roles in the invasive growth potential. We report that the E-cadherin repressors Slug, Zeb1/2 and Twist are overexpressed in these EMT cells characterized by a triple negative phenotype (loss of estrogen ER alpha and progesterone PRA/PRB receptors, no HER2 amplification), combined with loss of the alternative GPR30 estrogen receptor and induction of the invasive growth in collagen type I gels. Ectopic Snail expression suppressed WISP-2 transcripts and downregulated WISP-2 gene promoter ...
The epithelial-to-mesenchymal transition (EMT) confers an aggressive subtype associated with chemotherapy resistance in epithelial cancers. However, the mechanisms underlying the EMT and its associated signaling dysfunctions are still poorly understood. In two genetic models of MCF-7 breast cancer cells induced to EMT by WISP-2 silencing and Snail transformation, we investigated the status of several signaling elements downstream of G-protein receptors (GPR) and their functional roles in the invasive growth potential. We report that the E-cadherin repressors Slug, Zeb1/2 and Twist are overexpressed in these EMT cells characterized by a triple negative phenotype (loss of estrogen ERα and progesterone PRA/PRB receptors, no HER2 amplification), combined with loss of the alternative GPR30 estrogen receptor and induction of the invasive growth in collagen type I gels. Ectopic Snail expression suppressed WISP-2 transcripts and down-regulated WISP-2 gene promoter expression in transfected cells. ...
The CD103 antigen was originally described as the human mucosal antigen 1 (HML-1) and was subsequently proved to be the integrin αE subunit. CD103 is composed of a 150 kDa chain associated with a 25 kDa chain by a disulfide bond. It is expressed as a heterodimer in association with the integrin β7 chain. CD103 is expressed on mucosa-associated T lymphocytes and activated cells. This human intra-epithelial lymphocyte marker is expressed in very few resting peripheral blood lymphocytes. αEβ7 binds to E-cadherin on epithelial cells. Activation and TGFβ-1 induce CD103 expression ...
Complete information for [email protected] gene (Gene Cluster), Protocadherin Alpha Cluster, Complex Locus, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
D. Leckband and Sivasankar, S., "Biophysics of cadherin adhesion", in Adherens junctions: from molecular mechanisms to tissue development and disease, Springer Netherlands, 2012, pp. 63-88. ...
E-cadherin function leads to the density-dependent contact inhibition female viagra of cell growth. We report two cases, in which OGCs appear in common microenvironment despite different tumoural histology. Adipocyte size (microscopy), CD36 protein content (enzyme-linked immunosorbent assay) and ACS and DGAT ...
1I7X: The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin.
Sigma-Aldrich offers abstracts and full-text articles by [Michelle R Emond, Sayantanee Biswas, Cheasequah J Blevins, James D Jontes].
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Antibody Sampler Kit for studying Catenin-alphaE/Catenin-beta/E-Cadherin/N-Cadherin/P-Cadherin/R-cadherin in the Adhesion research area.
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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 ...
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 ...
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
CONTEXT: Appropriate cell-to-cell adhesion is fundamental for the epithelial phenotype of pituitary cells. Loss of the adhesion protein E-cadherin has been associated with invasiveness, metastasis, and poor prognosis in cancers of epithelial origin. In somatotroph adenomas, a variable and reduced expression of E-cadherin has been demonstrated. In addition, nuclear translocation of E-cadherin was found to correlate with pituitary tumor invasion.. OBJECTIVE: The objective was to examine the protein expression of E-cadherin in somatotroph pituitary adenomas in relation to adenoma size, invasiveness, and somatostatin analog (SMS) efficacy.. PATIENTS AND METHODS: Eighty-three patients were included, and 29 were treated preoperatively with SMS. Adenoma E-cadherin protein expression was analyzed by Western blot (61 patients) and immunohistochemistry (IHC) (80 patients) with antibodies directed against both extracellular and intracellular domains (IHC). The acute (direct surgery group) and long-term ...
TY - JOUR. T1 - Abnormal expression and function of the E-cadherin-catenin complex in gastric carcinoma cell lines. AU - Jawhari, A. U.. AU - Noda, M.. AU - Farthing, M. J.G.. AU - Pignatelli, M.. PY - 1999/1/1. Y1 - 1999/1/1. N2 - Dysfunction of the cadherin-catenin complex, a key component of adherens junctions, is thought to confer invasive potential to cells. The aim of this study is to examine the expression and function of the E-cadherin/catenin complex in gastric carcinoma cell lines. Expression of E-cadherin, α, β and γ-catenin and p120(ctn), and of the adenomatous polyposis coil protein (APC), together with function of the cadherin-catenin complex was examined in a panel of gastric carcinoma cell lines, using immunocytochemistry, Western blotting and a cell-cell aggregation assay. Protein interactions were examined by sequential immunoprecipitation and immunoblotting with antibodies to E-cadherin, α, β and γ-catenin, p120(ctn) and APC. Abnormalities of E-cadherin, α- and ...
The extracellular segment of the receptor-type type protein tyrosine phosphatase PTPmu, possesses an MAM domain, an immunoglobulin domain, and four fibronectin type-III repeats. It binds homophilically, i.e., PTPmu on the surface of one cell binds to PTPmu on an apposing cell, and the binding site lies within the immunoglobulin domain. The intracellular segment of PTPmu has two PTP domains and a juxtamembrane segment that is homologous to the conserved intracellular domain of the cadherins. In cadherins, this segment interacts with proteins termed catenins to mediate association with the actin cytoskeleton. In this article, we demonstrate that PTPmu associates with a complex containing cadherins, alpha- and beta-catenin in mink lung (MvLu) cells, and in rat heart, lung, and brain tissues. Greater than 80% of the cadherin in the cell is cleared from Triton X-100 lysates of MvLu cells after immunoprecipitation with antibodies to PTPmu; however, the complex is dissociated when lysates are prepared in
Hereditary breast cancer syndromes are associated with an increased risk of breast cancer and constitute a unique patient population, making up approximately 5%-10% of breast cancer cases in the United States. By virtue of the germline mutations that define these syndromes, invasive breast cancers in these patients have unique mechanisms that can be rationally targeted for therapeutic opportunities distinct from standard of care treatments in nongermline mutation associated breast cancers. This review intends to describe existing data on several of the most common hereditary breast cancer syndromes, including BRCA-related breast cancer syndrome, Li-Fraumeni syndrome, Cowden syndrome, Peutz-Jeghers syndrome, and hereditary diffuse gastric cancer syndrome, specifically focusing on rational therapeutics utilized in these distinct patient subgroups and completed or ongoing clinical trials evaluating their efficacy ...
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E-cadherin is a calcium dependent cell adhesion molecule, important in cell to cell interactions in epithelial tissues. The present study examined E-cadherin expression in normal salivary glands, pleomorphic adenoma, Warthins tumor, mucoepidermoid carcinoma, acinic cell carcinoma, adenoid cystic carcinoma and adenocarcinoma of salivary glands in paraffin sections using a monoclonal antibody (5H9). This study is firstly reported E-cadherin expression in the salivary gland and tumors.,BR,In normal submandibular and parotid gland, E-cadherin staining was confined to the cell membrane of acinar and ductal cells. In excretory ducts, high columnar cells showed the strongest reaction at the basal aspect and ductal basal cells were weakly positive or negative, the basement membrane zone lacked staining. No E-cadherin reaction was observed in modified myoepithelial cells and plasmacytoid cells. In pleomorphic adenoma and mucoepidermoid carcinoma, E-cadherin was positive at the lateral cell membrane or ...
TY - JOUR. T1 - Regulation of epithelial-mesenchymal transition in breast cancer cells by cell contact and adhesion. AU - Cichon, Magdalena A.. AU - Nelson, Celeste M.. AU - Radisky, Derek C. PY - 2015/2/9. Y1 - 2015/2/9. N2 - Epithelial-mesenchymal transition (EMT) is a physiological program that is activated during cancer cell invasion and metastasis. We show here that EMT-related processes are linked to a broad and conserved program of transcriptional alterations that are influenced by cell contact and adhesion. Using cultured human breast cancer and mouse mammary epithelial cells, we find that reduced cell density, conditions under which cell contact is reduced, leads to reduced expression of genes associated with mammary epithelial cell differentiation and increased expression of genes associated with breast cancer. We further find that treatment of cells with matrix metalloproteinase-3 (MMP-3), an inducer of EMT, interrupts a defined subset of cell contact-regulated genes, including genes ...
Desmosomes are molecular complexes of cell adhesion proteins and linking proteins that attach the cell surface adhesion proteins to intracellularkeratin cytoskeletal filaments.. The cell adhesion proteins of the desmosome, desmoglein and desmocollin, are members of the cadherin family of cell adhesion molecules. They aretransmembrane proteins that bridge the space between adjacent epithelial cellsby way of homophilic binding of their extracellular domains to other desmosomal cadherins on the adjacent cell. Both have five extracellular domains, and have calcium-binding motifs.. The extracellular domain of the desmosome is called the Extracellular Core Domain (ECD) or the Desmoglea, and is bisected by an electron-dense midline where the desmoglein and desmocollin proteins bind to each other. These proteins can bind in a W, S, or λ manner.. On the cytoplasmic side of the plasma membrane, there are two dense structures called the Outer Dense Plaque (ODP) and the Inner Dense Plaque (IDP). These are ...
Cadherin-1 also known as CAM 120/80 or epithelial cadherin (E-cadherin) or uvomorulin is a protein that in humans is encoded by ... E-cadherin (epithelial) is the most well-studied member of the cadherin family. It consists of 5 cadherin repeats (EC1 ~ EC5) ... E-cadherin can sequester β-catenin on the cell membrane by the cytoplasmic tail of E-cadherin. Loss of E-cadherin expression ... "Entrez Gene: CDH1 cadherin 1, type 1, E-cadherin (epithelial)".. *^ Fleming TP, Papenbrock T, Fesenko I, Hausen P, Sheth B ( ...
... has a functional role in metastasis of tumor similar to E-selectin.[20] P-selectin is expressed on the surface of both stimulated endothelial cell and activated platelet and helps cancer cells invade into bloodstream for metastasis and provided locally with multiple growth factors respectively.[21] Moreover, it has been known that platelet facilitates tumor metastasis by forming complexes with tumor cells and leukocytes in the vasculature thus preventing recognition by macrophage, this is thought to contribute to the seeding of tumor microemboli to distant organs.[22] In vivo mice experiment showed that reduction in circulating platelets could reduce cancer metastasis.[23] The oligosaccharide sialylated Lewis x (sLe(x)) is expressed on the surface of tumor cells and can be recognized by E-selectin and P-selectin, playing on a key role in metastasis of the tumor. However, in the 4T1 breast cancer cell line, E-selectin reactivity is sLe(x) dependent while P-selectin reactivity is ...
This gene encodes a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium- ... "Entrez Gene: CDH8 cadherin 8, type 2".. *^ Pagnamenta AT, Khan H, Walker S, Gerrelli D, Wing K, Bonaglia MC, et al. (Jan 2011 ... cadherin binding. Cellular component. • axon terminus. • integral component of membrane. • synaptic cleft. • membrane. • plasma ... Cadherin-8 is a protein that in humans is encoded by the CDH8 gene.[5][6][7] ...
... is a calcium-binding protein of the sarcoplasmic reticulum. The protein helps hold calcium in the cisterna of the sarcoplasmic reticulum after a muscle contraction, even though the concentration of calcium in the sarcoplasmic reticulum is much higher than in the cytosol. It also helps the sarcoplasmic reticulum store an extraordinarily high amount of calcium ions. Each molecule of calsequestrin can bind 18 to 50 Ca2+ ions.[1] Sequence analysis has suggested that calcium is not bound in distinct pockets via EF-hand motifs, but rather via presentation of a charged protein surface. Two forms of calsequestrin have been identified. The cardiac form Calsequestrin-2 (CASQ2) is present in cardiac and slow skeletal muscle and the fast skeletal form Calsequestrin-1(CASQ1) is found in fast skeletal muscle. The release of calsequestrin-bound calcium (through a calcium release channel) triggers muscle contraction. The active protein is not highly structured, more than 50% of it adopting a ...
The VCAM-1 protein mediates the adhesion of lymphocytes, monocytes, eosinophils, and basophils to vascular endothelium. It also functions in leukocyte-endothelial cell signal transduction, and it may play a role in the development of atherosclerosis and rheumatoid arthritis. Upregulation of VCAM-1 in endothelial cells by cytokines occurs as a result of increased gene transcription (e.g., in response to Tumor necrosis factor-alpha (TNF-α) and Interleukin-1 (IL-1)) and through stabilization of Messenger RNA (mRNA) (e.g., Interleukin-4 (IL-4)). The promoter region of the VCAM-1 gene contains functional tandem NF-κB (nuclear factor-kappa B) sites. The sustained expression of VCAM-1 lasts over 24 hours. Primarily, the VCAM-1 protein is an endothelial ligand for VLA-4 (Very Late Antigen-4 or integrin α4β1) of the β1 subfamily of integrins. VCAM-1 expression has also been observed in other cell types (e.g., smooth muscle cells). It has also been shown to interact with EZR[7] and Moesin.[7] CD106 ...
... is a multistructural and multifunctional cell surface molecule involved in cell proliferation, cell differentiation, cell migration, angiogenesis, presentation of cytokines, chemokines, and growth factors to the corresponding receptors, and docking of proteases at the cell membrane, as well as in signaling for cell survival. All these biological properties are essential to the physiological activities of normal cells, but they are also associated with the pathologic activities of cancer cells. Experiments in animals have shown that targeting of CD44 by antibodies, antisense oligonucleotides, and CD44-soluble proteins markedly reduces the malignant activities of various neoplasms, stressing the therapeutic potential of anti-CD44 agents. High levels of the adhesion molecule CD44 on leukemic cells are essential to generate leukemia.[24] Furthermore, because alternative splicing and posttranslational modifications generate many different CD44 sequences, including, perhaps, tumor-specific ...
N-cadherin mediates cell-cell interactions, stimulates axonal guidance guides neural progenitor cell migration ... "A self-renewing division of zebrafish Müller glial cells generates neuronal progenitors that require N-cadherin to regenerate ...
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 ...
Desmocollin-3 is a calcium-dependent glycoprotein that is a member of the desmocollin subfamily of the cadherin superfamily. ... 2001). "Down-regulation of the desmosomal cadherin desmocollin 3 in human breast cancer". Int. J. Oncol. 19 (1): 169-74. doi: ... 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 ...
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 ... King IA, Angst BD, Hunt DM, Kruger M, Arnemann J, Buxton RS (Nov 1997). "Hierarchical expression of desmosomal cadherins during ... Desmocollin-2 is a cadherin-type protein that functions to link adjacent cells together in specialized regions known as ...
EBs are formed by the homophilic binding of the Ca2+ dependent adhesion molecule E-cadherin, which is highly expressed on ... 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 ...
He is known for his identification of the cadherin class of adhesion molecules. Takeichi was born in Aichi prefecture, Japan ... "The sticky business of discovering cadherins". The Journal of Cell Biology. 170 (4): 514. doi:10.1083/jcb1704fta1. "細胞から個体へ - 脇 ...
Müller, U (October 2008). "Cadherins and mechanotransduction by hair cells". Current Opinion in Cell Biology. 20 (5): 557-566. ...
Cadherins are calcium-dependent adhesion molecules. Cadherins are extremely important in the process of morphogenesis - fetal ... Cadherin molecules form the actual anchor by attaching to the cytoplasmic plaque, extending through the membrane and binding ... Together with an alpha-beta catenin complex, the cadherin can bind to the microfilaments of the cytoskeleton of the cell. This ... Similarly to desmosomes and hemidesmosomes, their transmembrane anchors are composed of cadherins in those that anchor to other ...
Amagai M (1999). "Autoimmunity against desmosomal cadherins in pemphigus". J. Dermatol. Sci. 20 (2): 92-102. doi:10.1016/S0923- ...
The encoded protein has a signal peptide, 27 cadherin repeat domains and a unique cytoplasmic region. This particular cadherin ... Protein dachsous homolog 1, also known as protocadherin-16 (PCDH16) or cadherin-19 (CDH19) or cadherin-25 (CDH25) or fibroblast ... cadherin-1 (FIB1), is a protein that in humans is encoded by the DCHS1 gene. This gene is a member of the cadherin superfamily ... 2001). "Identification of three novel non-classical cadherin genes through comprehensive analysis of large cDNAs". Brain Res. ...
... forms distinct complexes with cadherins and desmosomal cadherins. Plakoglobin is a major cytoplasmic component of ... is required for its high affinity binding to the cytoplasmic domains of E-cadherin and desmosomal cadherin Dsg2, and the tumor ... interacts with E-cadherin and N-cadherin". The Journal of Cell Biology. 118 (3): 671-9. doi:10.1083/jcb.118.3.671. PMC 2289540 ... interacts with E-cadherin and N-cadherin". The Journal of Cell Biology. 118 (3): 671-9. doi:10.1083/jcb.118.3.671. PMC 2289540 ...
P-cadherins), neural (N-cadherins), retinal (R-cadherins), brain (B-cadherins and T-cadherins), and muscle (M-cadherins). Many ... Each cadherin exhibits a unique pattern of tissue distribution, such as epithelial (E-cadherins), placental ( ... The classic cadherins (E-, N- and P-) are concentrated at the intermediate cell junctions, which link to the actin filament ... Soncin, F.; Ward, M.C. (2011). "The Function of E-Cadherin in Stem Cell Pluripotency and Self-Renewal". Genes. 2 (1): 229-259. ...
These neural cadherin-like cell adhesion proteins most likely play a critical role in the establishment and function of ... 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 ... Yagi T, Takeichi M (2000). "Cadherin superfamily genes: functions, genomic organization, and neurologic diversity". Genes Dev. ...
N-cadherin, a classical cadherin from the cadherin superfamily, is composed of five extracellular cadherin repeats, a ... N-cadherin, also known as Cadherin-2 (CDH2) or neural cadherin (NCAD) is a protein that in humans is encoded by the CDH2 gene. ... N-cadherin, as well as other cadherins, interact with N-cadherin on an adjacent cell in an anti-parallel conformation, thus ... N-cadherin complexed to catenins has been described as a master regulator of intercalated disc function. N-cadherin appears at ...
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 ... Ahmed AF, de Bock CE, Lincz LF, Pundavela J, Zouikr I, Sontag E, Hondermarck H, Thorne RF (Jun 2015). "FAT1 cadherin acts ...
... cadherin 10". Suzuki S, Sano K, Tanihara H (April 1991). "Diversity of the cadherin family: evidence for eight new cadherins in ... Cadherin 10 is a protein that in humans is encoded by the CDH10 gene. An association with autism has been suggested. Cadherin ... 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". Suzuki S, Sano K, Tanihara H (April 1991). "Diversity of the cadherin family: evidence for eight new cadherins in ... Cadherin 9 is a protein that in humans is encoded by the CDH9 gene. An association with autism has been suggested. Cadherin ... Ali J, Liao F, Martens E, Muller WA (June 1997). "Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial ... "Cadherin-9 is a novel cell surface marker for the heterogeneous pool of renal fibroblasts". PLoS One. 2 (7): e657. doi:10.1371/ ...
Other catenin, cadherin or cell cycle regulators may also be useful in treating a variety of cancers. While recent studies in ... A tumor cell line with defective δ-catenin, low levels of E-cadherin and poor cell-to-cell adhesion could be restored to normal ... Through the interaction of β-catenin and α-catenin, actin and E-cadherin are linked, providing the cell with a means of stable ... In F9 cells lacking both β-catenin and plakoglobin, very little E-cadherin and α-catenin accumulated at the cell surface. Mice ...
"Distinct E-cadherin-based complexes regulate cell behaviour through miRNA processing or Src and p120 catenin activity". Nature ... Therefore, PLEKHA7lstabilises both cadherins and nectins at AJ. Genome-wide association studies suggest that PLEKHA7 is ... However, in Eph4 cell line, PLEKHA7 is recruited to E-cadherin based AJ by Afadin, independently of p120. PLEKHA7 knockdown ... "Mayo Clinic researchers find new code that makes reprogramming of cancer cells possible". Distinct E-cadherin-based complexes ...
Loss of E-cadherin-dependent cell-cell adhesion due to mutation of the beta-catenin gene in a human 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- ... Loss of E-cadherin-dependent cell-cell adhesion due to mutation of the beta-catenin gene in a human cancer cell line, HSC-39. ... Loss of E-cadherin-dependent cell-cell adhesion due to mutation of the beta-catenin gene in a human cancer cell line, HSC-39. ...
... the cadherins associated with PTPmu are now found in a tyrosine- phosphorylated form, indicating that the cadherins may be an ... In cadherins, this segment interacts with proteins termed catenins to mediate association with the actin cytoskeleton. In this ... Greater than 80% of the cadherin in the cell is cleared from Triton X-100 lysates of MvLu cells after immunoprecipitation with ... Consistent with their ability to interact in vivo, PTPmu, cadherins, and catenins all localized to points of cell-cell contact ...
Cadherin-associated Protein, Catenin beta 1, Catenin beta-1, CATNB, CTNNB, CTNNB1) SKU: C2069-51C() ... Anti-Catenin, beta (Beta Catenin, Cadherin-associated Protein, Catenin beta 1, Catenin beta-1, CATNB, CTNNB, CTNNB1) SKU: C2069 ... Anti-Catenin, beta (Beta Catenin, Cadherin-associated Protein, Catenin beta 1, Catenin beta-1, CATNB, CTNNB, CTNNB1) ...
... and E-cadherin in epithelial cells before adhesion (Adams et al., 1998). This difference argues for a tethering in the mobility ... Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green ...
The main difference between the two groups of cadherins is the classical cadherins contain five cadherin repeats with the third ... Cadherins are a family of transmembrane proteins formed from multiple repeats of cadherin-specific motif (a recurrent molecular ... β-Catenin binds directly to the cadherin cytoplasmic domain, with the α-catenin binding to it, connecting the cadherin protein ... Cadherins are classified into two groups: Classical Cadherins and Protocadherins. ...
Cadherins are a group of proteins that help cells stick together. They are the main components of certain types of junctions ... Classical cadherins include E-cadherin, N-cadherin, P-cadherin and N-cadherin 2. They all have a similar structure, with five ... Cadherin structure. Cadherins are named for calcium dependent adhesion. The external domain of a cadherin molecule - the part ... Cadherins role in cancer. E-cadherin, a member of the cadherin family, has a very important role in organizing the epithelium ...
Epithelial cadherin; Uvomorulin E-cadherin, a 120 kDa molecule, is a prototypical member of the classical cadherin family of ... Thus, E-cadherin and other members of the cadherin family play a crucial role in establishing and maintaining the integrity of ... E-cadherin, a 120 kDa molecule, is a prototypical member of the classical cadherin family of single-pass transmembrane proteins ... E-cadherin is the main adhesion molecule of the adherens junctions of epithelial cells, and via catenins it is linked to the ...
Knockdown of desmosomal cadherins affects gastrulation movements. In situ hybridisation images for gata1 at 30% epiboly (A) and ... Knockdown of desmosomal cadherins causes epiboly defects. A and C show morphants at 6 hpf whose blastomeres became detached and ... Desmosomal cadherins are expressed from early development onwards. Semi-quantitative RT-PCR analysis of zfDsc, zfDsga, zfDsgb ... Knockdown of desmosomal cadherins affects desmosome structure. A. Apical junctional complex between cells of the EL of wild ...
Cadherins are transmembrane proteins that mediate cell-cell adhesion in animals [PMID: 22833291]. Cadherin-16 (CDH16) or kidney ... CDH16/Ksp-cadherin is expressed in the developing thyroid gland and is strongly down-regulated in thyroid carcinomas.. ... Expression of Ksp-cadherin during kidney development and in renal cell carcinoma.. Br. J. Cancer 92 2010-7 2005 ... CDH16 colocalises with CDH1/E-cadherin on the basolateral plasma membrane of thyrocytes, and might play a role during thyroid ...
Crystal structures of cadherin-23 and Drosophila N-cadherin reveal unique features of atypical cadherins. (a) Structures of ... VE-cadherin exchanges Trp2 and Trp4 like type II cadherins, but the interface is limited to the apex of the domain, as in type ... Classical cadherins from adhesive dimers by exchange of the N-terminal β-strand. (a) A classical cadherin trans dimer is shown ... In type I cadherins, residue Trp2 in domain EC1 is swapped between binding partners. In type II cadherins, two Trp residues, ...
... cadherin 9, type 2 (T1-cadherin) CDH10 - cadherin 10, type 2 (T2-cadherin) CDH4 - R-cadherin (retinal) CDH5 - VE-cadherin ( ... N-cadherins are found in neurons CDH12 - cadherin 12, type 2 (N-cadherin 2) CDH3 - P-cadherin (placental): P-cadherins are ... cadherin 7, type 2 CDH8 - cadherin 8, type 2 CDH11 - OB-cadherin (osteoblast) CDH13 - T-cadherin - H-cadherin (heart) CDH15 - M ... KSP-cadherin CDH17 - LI cadherin (liver-intestine) CDH18 - cadherin 18, type 2 CDH19 - cadherin 19, type 2 CDH20 - cadherin 20 ...
Dystroglycan-type cadherin-like (IPR006644). Short name: Cadg Overlapping homologous superfamilies *Cadherin-like superfamily ( ... Cadherin-like domains in alpha-dystroglycan, alpha/epsilon-sarcoglycan and yeast and bacterial proteins.. Curr. Biol. 12 R197-9 ... In animals, cadherin domain-containing proteins are adhesion molecules that modulate a wide variety of processes including cell ... Crystal structures have revealed that multiple cadherin domains form Ca2+-dependent rod-like structures with a conserved Ca2+- ...
T-cadherin also known as cadherin 13, H-cadherin (heart) (CDH13) is a unique member of cadherin superfamily because it lacks ... T-cadherin expression results in LDL-induced migration of T-cadherin expressing cells compared to control. It is likely that T- ... T-cadherin expression was found to be altered in tumor vessels: in Lewis carcinoma lung metastasis the expression of T-cadherin ... T-cadherin is a GPI-anchored member of cadherin superfamily, which lacks a direct contact with cytoskeleton and therefore is ...
Cadherins are Ca2+ dependent cell-cell adhesion molecules that mediate adhesion between cells and tissues in organisms. They ... E-Cadherin. This cadherin is present in epithelial cells, hence the name E-Cadherin. Defects in E-Cadherin adhesion have been ... N-Cadherin. This cadherin is present in neurons, fibroblasts, and muscle cells, hence the name N-Cadherin. Defects in N- ... P-Cadherin P-Cadherins are found in placenta and mutations in this cadherin have been associated with hypotrichosis with ...
... Galina Reshetnikova Institute of Cytology, Russian ...
E-cadherin (epithelial-cadherin), encoded by the CDH1 gene, is a transmembrane glycoprotein playing a crucial role in ... E-cadherin has been reported to be a tumor suppressor and to be down regulated in gastric cancer. Besides genetic mutations in ... In addition, expression of E-cadherin could be mediated by infectious agents such as H. pylori (Helicobacter pylori). As E- ... E-Cadherin and Gastric Cancer: Cause, Consequence, and Applications. Xin Liu and Kent-Man Chu ...
Using human AECs and cell lines, we demonstrate that cadherin-26 (CDH26) is abundantly expressed in differentiated AECs, ... localizes to the cell apices near ciliary membranes, and has functional cadherin domains with homotypic binding. We find a ... 2: Cadherin-26 (CDH26) localizes to the apical membrane.. a Immunofluorescence for E-cadherin (green), CDH26 (red), acetylated ... including classical cadherins, protocadherins, and atypical cadherins. Atypical cadherins such as FAT111 and flamingo12 have ...
CDH5 or VE-Cadherin is a 140 kDa protein belonging to the cadherin family of cell adhesion molecules which interact ... VE-cadherin is the major component of endothelial adherens junctions and is specific to endothelial cells ... CD144 (VE-Cadherin) Antigen. CD144, also called Cadherin 5, CDH5 or VE-Cadherin is a 140 kDa protein belonging to the cadherin ... VE-cadherin is the major component of endothelial adherens junctions and is specific to endothelial cells. It is present in all ...
that glucose-induced insulin secretion in individual β-cells can be directly linked to specific cadherin-cadherin ligation ... From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion. Trends Genet 1993;9:317-321pmid: ... Molecular basis for the regulation of islet beta cell mass in mice: the role of E-cadherin. Diabetologia 2013;56:856-866pmid: ... Integrins and cadherins join forces to form adhesive networks. J Cell Sci 2011;124:1183-1193pmid:21444749. ...
Abcams E Cadherin ELISA Kit (ab100678) suitable for Cell culture supernatant, Serum, Plasma in mouse. Reliably quantify 6 pg/ ... Abcams E-Cadherin Mouse ELISA (Enzyme-Linked Immunosorbent Assay) kit is an in vitro enzyme-linked immunosorbent assay for the ... Furthermore, E Cadherin plays a crucial role in the maintenance of the epithelial junctional complex and is as such an ... Standards and samples are pipetted into the wells and E-Cadherin present in a sample is bound to the wells by the immobilized ...
Rabbit polyclonal pan Cadherin antibody validated for IHC and tested in Human, Mouse, Rat, Chk, Cow, Dog, Xl and Mk. Immunogen ... This antibody recognizes members of the Cadherin family of proteins including E-cadherin, N-cadherin, P-cadherin and R-cadherin ... In adhesion junctions cadherins are bound to beta and gamma catenins which in turn bind to alpha catenin, an actin binding ... Cadherins are expressed in a tissue specific manner and and are required for assembly of cells into solid tissue. Individual ...
Down-regulation of E-cadherin expression has been observed in a number of carcinomas and is usually associated with advanced ... cadherin is a 120 kDa transmembrane cell adhesion molecule. It has a significant function in intercellular adhesion of ... Anti-E-cadherin, NCH-38 recognizes the 120 kDa mature form and 82 kDa fragment of E-cadherin in Western blots of A431 cells ... FLEX Monoclonal Mouse Anti-Human E-Cadherin Clone NCH-38 Ready-to-Use (Dako Omnis) - EN / FR / DE Instructions for Use, Code ...
... we demonstrate that beta-catenin is the linker protein between E-cadherin and alpha-catenin and that E-cadherin does not bind ... to approximately 2000-kDa complex bound to E-cadherin and an approximately 220-kDa pool that did not contain E-cadherin. Only ... Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex. T S Jou, D B Stewart, J Stappert, W J ... We show that a 25-amino acid sequence in the cytoplasmic domain of E-cadherin and the amino-terminal domain of alpha-catenin ...
The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin. ... EPITHELIAL-CADHERIN B, D 151 Mus musculus Fragment: CYTOPLASMIC DOMAIN Gene Name(s): Cdh1 ...
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  • Microenvironmental protection of CML stem and progenitor cells from tyrosine kinase inhibitors through N-cadherin and Wnt-β-catenin signaling. (scienceopen.com)
  • After pervanadate treatment of MvLu cells, which inhibits cellular tyrosine phosphatase activity including PTPmu, the cadherins associated with PTPmu are now found in a tyrosine- phosphorylated form, indicating that the cadherins may be an endogenous substrate for PTPmu. (scienceopen.com)
  • In the obtained transfectants, E-cadherin-dependent cell-cell adhesiveness was recovered, as revealed by cell compaction, cell aggregation, and immunoflourescence staining. (asm.org)
  • Consistent with their ability to interact in vivo, PTPmu, cadherins, and catenins all localized to points of cell-cell contact in MvLu cells, as assessed by immunocytochemical staining. (scienceopen.com)
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