Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.
A single-pass transmembrane glycoproteins that mediate CALCIUM-dependent CELL ADHESION and are core components of DESMOSOMES.
A group of desmosomal cadherins with cytoplasmic tails that resemble those of classical CADHERINS.
Desmoplakins are cytoskeletal linker proteins that anchor INTERMEDIATE FILAMENTS to the PLASMA MEMBRANE at DESMOSOMES.
A group of desmosomal cadherins with cytoplasmic tails that are divergent from those of classical CADHERINS. Their intracytoplasmic domains bind PLAKOGLOBIN; PLAKOPHILINS; and DESMOPLAKINS.
A family of cytoskeletal proteins that play essential roles in CELL ADHESION at ADHERENS JUNCTIONS by linking CADHERINS to the ACTIN FILAMENTS of the CYTOSKELETON.
A multi-functional catenin that is highly homologous to BETA CATENIN. Gamma catenin binds CADHERINS and helps link their cytoplasmic tails to ACTIN in the CYTOSKELETON via ALPHA CATENIN. It is also found in DESMOSOMES where it mediates the link between DESMOSOMAL CADHERINS and DESMOPLAKIN.
A type of junction that attaches one cell to its neighbor. One of a number of differentiated regions which occur, for example, where the cytoplasmic membranes of adjacent epithelial cells are closely apposed. It consists of a circular region of each membrane together with associated intracellular microfilaments and an intercellular material which may include, for example, mucopolysaccharides. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990; Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
A catenin that binds F-ACTIN and links the CYTOSKELETON with BETA CATENIN and GAMMA CATENIN.
A CALCIUM-dependent adhesion molecule of DESMOSOMES that also plays a role in embryonic STEM CELL proliferation.
Adherence of cells to surfaces or to other cells.
Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.
A desmosomal cadherin that is an autoantigen in the acquired skin disorder PEMPHIGUS FOLIACEUS.
Direct contact of a cell with a neighboring cell. Most such junctions are too small to be resolved by light microscopy, but they can be visualized by conventional or freeze-fracture electron microscopy, both of which show that the interacting CELL MEMBRANE and often the underlying CYTOPLASM and the intervening EXTRACELLULAR SPACE are highly specialized in these regions. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p792)
A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.
Anchoring points where the CYTOSKELETON of neighboring cells are connected to each other. They are composed of specialized areas of the plasma membrane where bundles of the ACTIN CYTOSKELETON attach to the membrane through the transmembrane linkers, CADHERINS, which in turn attach through their extracellular domains to cadherins in the neighboring cell membranes. In sheets of cells, they form into adhesion belts (zonula adherens) that go all the way around a cell.
Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.
The phenomenon by which dissociated cells intermixed in vitro tend to group themselves with cells of their own type.
A desmosomal cadherin that is an autoantigen in the acquired skin disorder PEMPHIGUS VULGARIS.
A family of proteins that contain several 42-amino acid repeat domains and are homologous to the Drosophila armadillo protein. They bind to other proteins through their armadillo domains and play a variety of roles in the CELL including SIGNAL TRANSDUCTION, regulation of DESMOSOME assembly, and CELL ADHESION.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.
A cultured line of C3H mouse FIBROBLASTS that do not adhere to one another and do not express CADHERINS.
Members of the armadillo family of proteins that are found in DESMOSOMES and interact with various proteins including desmocadherins; DESMOPLAKIN; ACTIN FILAMENTS; and KERATINS.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Any of several ways in which living cells of an organism communicate with one another, whether by direct contact between cells or by means of chemical signals carried by neurotransmitter substances, hormones, and cyclic AMP.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Group of chronic blistering diseases characterized histologically by ACANTHOLYSIS and blister formation within the EPIDERMIS.
A subclass of receptor-like protein tryosine phosphatases that contain multiple extracellular immunoglobulin G-like domains and fibronectin type III-like domains. An additional memprin-A5-mu domain is found on some members of this subclass.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action during the developmental stages of an organism.
Proteins obtained from various species of Xenopus. Included here are proteins from the African clawed frog (XENOPUS LAEVIS). Many of these proteins have been the subject of scientific investigations in the area of MORPHOGENESIS and development.
A cytoskeletal protein associated with cell-cell and cell-matrix interactions. The amino acid sequence of human vinculin has been determined. The protein consists of 1066 amino acid residues and its gene has been assigned to chromosome 10.
A subclass of receptor-like protein tryosine phosphatases that contain an extracellular RDGS-adhesion recognition motif and a single cytosolic protein tyrosine phosphate domain.
Epidermal cells which synthesize keratin and undergo characteristic changes as they move upward from the basal layers of the epidermis to the cornified (horny) layer of the skin. Successive stages of differentiation of the keratinocytes forming the epidermal layers are basal cell, spinous or prickle cell, and the granular cell.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
Orientation of intracellular structures especially with respect to the apical and basolateral domains of the plasma membrane. Polarized cells must direct proteins from the Golgi apparatus to the appropriate domain since tight junctions prevent proteins from diffusing between the two domains.
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
Phosphoproteins are proteins that have been post-translationally modified with the addition of a phosphate group, usually on serine, threonine or tyrosine residues, which can play a role in their regulation, function, interaction with other molecules, and localization within the cell.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Specialized areas at the CELL MEMBRANE where a cell attaches to the EXTRACELLULAR MATRIX or other substratum.
A technique that localizes specific nucleic acid sequences within intact chromosomes, eukaryotic cells, or bacterial cells through the use of specific nucleic acid-labeled probes.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.
Established cell cultures that have the potential to propagate indefinitely.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A rac GTP-binding protein involved in regulating actin filaments at the plasma membrane. It controls the development of filopodia and lamellipodia in cells and thereby influences cellular motility and adhesion. It is also involved in activation of NADPH OXIDASE. This enzyme was formerly listed as EC 3.6.1.47.
The external, nonvascular layer of the skin. It is made up, from within outward, of five layers of EPITHELIUM: (1) basal layer (stratum basale epidermidis); (2) spinous layer (stratum spinosum epidermidis); (3) granular layer (stratum granulosum epidermidis); (4) clear layer (stratum lucidum epidermidis); and (5) horny layer (stratum corneum epidermidis).
Separation of the prickle cells of the stratum spinosum of the epidermis, resulting in atrophy of the prickle cell layer. It is seen in diseases such as pemphigus vulgaris (see PEMPHIGUS) and DARIER DISEASE.
A process of complicated morphogenetic cell movements that reorganizes a bilayer embryo into one with three GERM LAYERS and specific orientation (dorsal/ventral; anterior/posterior). Gastrulation describes the germ layer development of a non-mammalian BLASTULA or that of a mammalian BLASTOCYST.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A sequential pattern of amino acids occurring more than once in the same protein sequence.
Microscopy in which the samples are first stained immunocytochemically and then examined using an electron microscope. Immunoelectron microscopy is used extensively in diagnostic virology as part of very sensitive immunoassays.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The process by which cells convert mechanical stimuli into a chemical response. It can occur in both cells specialized for sensing mechanical cues such as MECHANORECEPTORS, and in parenchymal cells whose primary function is not mechanosensory.
A MARVEL domain-containing protein found in the presynaptic vesicles of NEURONS and NEUROENDOCRINE CELLS. It is commonly used as an immunocytochemical marker for neuroendocrine differentiation.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
A large family of MONOMERIC GTP-BINDING PROTEINS that are involved in regulation of actin organization, gene expression and cell cycle progression. This enzyme was formerly listed as EC 3.6.1.47.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The developmental entity of a fertilized egg (ZYGOTE) in animal species other than MAMMALS. For chickens, use CHICK EMBRYO.
A member of the Rho family of MONOMERIC GTP-BINDING PROTEINS. It is associated with a diverse array of cellular functions including cytoskeletal changes, filopodia formation and transport through the GOLGI APPARATUS. This enzyme was formerly listed as EC 3.6.1.47.
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
Cytoplasmic filaments intermediate in diameter (about 10 nanometers) between the microfilaments and the microtubules. They may be composed of any of a number of different proteins and form a ring around the cell nucleus.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Cadherins are a type of cell adhesion molecule that play a crucial role in the development and maintenance of intercellular junctions. They are transmembrane proteins that mediate calcium-dependent homophilic binding between adjacent cells, meaning that they bind to identical cadherin molecules on neighboring cells.

There are several types of cadherins, including classical cadherins, desmosomal cadherins, and protocadherins, each with distinct functions and localization in tissues. Classical cadherins, also known as type I cadherins, are the most well-studied and are essential for the formation of adherens junctions, which help to maintain cell-to-cell contact and tissue architecture.

Desmosomal cadherins, on the other hand, are critical for the formation and maintenance of desmosomes, which are specialized intercellular junctions that provide mechanical strength and stability to tissues. Protocadherins are a diverse family of cadherin-related proteins that have been implicated in various developmental processes, including neuronal connectivity and tissue patterning.

Mutations in cadherin genes have been associated with several human diseases, including cancer, neurological disorders, and heart defects. Therefore, understanding the structure, function, and regulation of cadherins is essential for elucidating their roles in health and disease.

Desmosomal cadherins, also known as desmocadherins, are a subfamily of the cadherin superfamily of calcium-dependent adhesion molecules. They are primarily responsible for cell-cell adhesion in tissues that undergo mechanical stress, such as epithelial and cardiac tissue.

Desmosomal cadherins include desmocadherin-1 (Desmoglein-1) and desmocadherin-2 (Desmocollin-2), which are located in the desmosomes of adjacent cells. Desmosomes are specialized intercellular junctions that provide strong adhesion and help maintain tissue integrity during mechanical stress.

Desmosomal cadherins have a unique structure, with an extracellular domain containing multiple cadherin repeats that mediate homophilic interactions between adjacent cells. They also have a cytoplasmic domain that interacts with desmoplakin, a protein that links the desmosomal cadherins to the intermediate filament cytoskeleton.

Mutations in desmosomal cadherins have been associated with several human genetic disorders, including skin blistering diseases and arrhythmogenic right ventricular cardiomyopathy (ARVC), a heart condition that can lead to sudden cardiac death.

Desmogleins are a group of proteins that are part of the desmosomes, which are structures that help to strengthen and maintain the integrity of epithelial tissues. Desmogleins play a crucial role in cell-to-cell adhesion by forming intercellular junctions known as desmoglein adherens junctions. These junctions help to anchor intermediate filaments, such as keratin, to the plasma membrane and provide structural support to epithelial cells.

There are four main types of desmogleins (Dsg1-4), each with distinct expression patterns in different tissues. For example, Dsg1 is primarily expressed in the upper layers of the epidermis, while Dsg3 is found in the lower layers and in mucous membranes. Mutations in desmoglein genes have been associated with several skin disorders, including pemphigus vulgaris and pemphigus foliaceus, which are autoimmune blistering diseases characterized by the loss of cell-to-cell adhesion in the epidermis.

Desmoplakins are important proteins that play a crucial role in the structural integrity and function of certain types of cell-to-cell junctions called desmosomes. Desmosomes are specialized structures that connect adjacent cells in tissues that undergo significant mechanical stress, such as the skin, heart, and gut.

Desmoplakins are large proteins that are composed of several domains, including a plakin domain, which interacts with other desmosomal components, and a spectrin-like repeat domain, which binds to intermediate filaments. By linking desmosomes to the intermediate filament network, desmoplakins help to provide mechanical strength and stability to tissues.

Mutations in the genes that encode desmoplakins have been associated with several human genetic disorders, including arrhythmogenic right ventricular cardiomyopathy (ARVC), a heart condition characterized by abnormal heart rhythms and structural changes in the heart muscle, and epidermolysis bullosa simplex (EBS), a skin disorder characterized by blistering and fragility of the skin.

Desmocollins are a type of cadherin, which is a transmembrane protein involved in cell-cell adhesion. Specifically, desmocollins are found in the desmosomes, which are specialized structures that help to mechanically connect adjacent epithelial cells. There are three main isoforms of desmocollin (Desmocollin-1, -2, and -3) that are encoded by different genes. Mutations in the genes encoding desmocollins have been associated with several skin blistering disorders, including certain forms of epidermolysis bullosa.

Catenins are a type of protein that play a crucial role in cell adhesion and signal transduction. They are named for their ability to link together (or "catenate") proteins called cadherins, which are important for the formation of tight junctions between cells. Catenins help to anchor cadherins to the cytoskeleton, providing structural support and stability to tissues.

There are several different types of catenins, including alpha-catenin, beta-catenin, gamma-catenin (also called plakoglobin), and delta-catenin. Alpha-catenin links cadherins to the actin cytoskeleton, while beta-catenin and gamma-catenin can also interact with transcription factors in the nucleus to regulate gene expression.

Mutations in catenin genes have been associated with various human diseases, including cancer. For example, abnormal activation of the Wnt signaling pathway, which involves beta-catenin, has been implicated in several types of cancer. Additionally, mutations in alpha-E-catenin, a type of alpha-catenin found in epithelial cells, have been linked to colorectal cancer.

Gamma-catenin, also known as plakoglobin, is a protein that is involved in cell adhesion and the regulation of gene expression. It is a member of the catenin family, which includes beta-catenin and alpha-catenin. Gamma-catenin is found at adherens junctions, where it interacts with cadherins to help maintain cell-cell adhesion. It also plays a role in the Wnt signaling pathway, where it can bind to TCF/LEF transcription factors and regulate the expression of target genes. Mutations in the gene that encodes gamma-catenin have been associated with several types of cancer, including colon cancer and melanoma.

Desmosomes are specialized intercellular junctions that provide strong adhesion between adjacent epithelial cells and help maintain the structural integrity and stability of tissues. They are composed of several proteins, including desmoplakin, plakoglobin, and cadherins, which form complex structures that anchor intermediate filaments (such as keratin) to the cell membrane. This creates a network of interconnected cells that can withstand mechanical stresses. Desmosomes are particularly abundant in tissues subjected to high levels of tension, such as the skin and heart.

Alpha-catenin is a protein that plays a crucial role in cell adhesion and the maintenance of the cytoskeleton. It is a component of the cadherin-catenin complex, which is responsible for forming tight junctions between cells, known as adherens junctions. Alpha-catenin binds to beta-catenin, which in turn interacts with cadherins, transmembrane proteins that mediate cell-cell adhesion. This interaction helps to link the actin cytoskeleton to the cadherin-catenin complex, providing strength and stability to adherens junctions. Additionally, alpha-catenin has been implicated in various signaling pathways related to cell growth, differentiation, and migration.

Desmoglein 2 is a type of desmoglein protein that is primarily found in the desmosomes of epithelial cells. Desmosomes are specialized structures that help to anchor intermediate filaments to the cell membrane and provide strength and stability to tissues that undergo mechanical stress, such as the skin and heart.

Desmoglein 2 plays a critical role in maintaining cell-cell adhesion by forming intercellular junctions called desmosomal cadherins. These junctions help to hold adjacent cells together and contribute to the integrity of epithelial tissues. Mutations in the gene that encodes Desmoglein 2 have been associated with several skin disorders, including pemphigus vulgaris, a blistering autoimmune disease that affects mucous membranes and the skin. In this condition, antibodies target Desmoglein 2, leading to loss of cell-cell adhesion and formation of blisters.

Cell adhesion refers to the binding of cells to extracellular matrices or to other cells, a process that is fundamental to the development, function, and maintenance of multicellular organisms. Cell adhesion is mediated by various cell surface receptors, such as integrins, cadherins, and immunoglobulin-like cell adhesion molecules (Ig-CAMs), which interact with specific ligands in the extracellular environment. These interactions lead to the formation of specialized junctions, such as tight junctions, adherens junctions, and desmosomes, that help to maintain tissue architecture and regulate various cellular processes, including proliferation, differentiation, migration, and survival. Disruptions in cell adhesion can contribute to a variety of diseases, including cancer, inflammation, and degenerative disorders.

Cytoskeletal proteins are a type of structural proteins that form the cytoskeleton, which is the internal framework of cells. The cytoskeleton provides shape, support, and structure to the cell, and plays important roles in cell division, intracellular transport, and maintenance of cell shape and integrity.

There are three main types of cytoskeletal proteins: actin filaments, intermediate filaments, and microtubules. Actin filaments are thin, rod-like structures that are involved in muscle contraction, cell motility, and cell division. Intermediate filaments are thicker than actin filaments and provide structural support to the cell. Microtubules are hollow tubes that are involved in intracellular transport, cell division, and maintenance of cell shape.

Cytoskeletal proteins are composed of different subunits that polymerize to form filamentous structures. These proteins can be dynamically assembled and disassembled, allowing cells to change their shape and move. Mutations in cytoskeletal proteins have been linked to various human diseases, including cancer, neurological disorders, and muscular dystrophies.

Desmoglein 1 is a type of desmosomal cadherin, which is a transmembrane protein involved in cell-to-cell adhesion. It is primarily expressed in the upper layers of the epidermis and plays a crucial role in maintaining the integrity and stability of the skin. Desmoglein 1 forms desmosomes, specialized intercellular junctions that connect adjacent keratinocytes and help to resist shearing forces.

Desmoglein 1 is also a target for autoantibodies in certain blistering diseases, such as pemphigus foliaceus, where the binding of these antibodies to desmoglein 1 results in the loss of cell-to-cell adhesion and formation of skin blisters.

Intercellular junctions are specialized areas of contact between two or more adjacent cells in multicellular organisms. They play crucial roles in maintaining tissue structure and function by regulating the movement of ions, molecules, and even larger cellular structures from one cell to another. There are several types of intercellular junctions, including:

1. Tight Junctions (Zonulae Occludentes): These are the most apical structures in epithelial and endothelial cells, forming a virtually impermeable barrier to prevent the paracellular passage of solutes and water between the cells. They create a tight seal by connecting the transmembrane proteins of adjacent cells, such as occludin and claudins.
2. Adherens Junctions: These are located just below the tight junctions and help maintain cell-to-cell adhesion and tissue integrity. Adherens junctions consist of cadherin proteins that form homophilic interactions with cadherins on adjacent cells, as well as intracellular adaptor proteins like catenins, which connect to the actin cytoskeleton.
3. Desmosomes: These are another type of cell-to-cell adhesion structure, primarily found in tissues that experience mechanical stress, such as the skin and heart. Desmosomes consist of cadherin proteins (desmocadherins) that interact with each other and connect to intermediate filaments (keratin in epithelial cells) via plakoglobin and desmoplakin.
4. Gap Junctions: These are specialized channels that directly connect the cytoplasm of adjacent cells, allowing for the exchange of small molecules, ions, and second messengers. Gap junctions consist of connexin proteins that form hexameric structures called connexons in the plasma membrane of each cell. When two connexons align, they create a continuous pore or channel between the cells.

In summary, intercellular junctions are essential for maintaining tissue structure and function by regulating paracellular transport, cell-to-cell adhesion, and intercellular communication.

Beta-catenin is a protein that plays a crucial role in gene transcription and cell-cell adhesion. It is a key component of the Wnt signaling pathway, which regulates various processes such as cell proliferation, differentiation, and migration during embryonic development and tissue homeostasis in adults.

In the absence of Wnt signals, beta-catenin forms a complex with other proteins, including adenomatous polyposis coli (APC) and axin, which targets it for degradation by the proteasome. When Wnt ligands bind to their receptors, this complex is disrupted, allowing beta-catenin to accumulate in the cytoplasm and translocate to the nucleus. In the nucleus, beta-catenin interacts with T cell factor/lymphoid enhancer-binding factor (TCF/LEF) transcription factors to activate the transcription of target genes involved in cell fate determination, survival, and proliferation.

Mutations in the genes encoding components of the Wnt signaling pathway, including beta-catenin, have been implicated in various human diseases, such as cancer, developmental disorders, and degenerative conditions.

Adherens junctions are specialized types of cell-cell contacts that play a crucial role in maintaining the integrity and stability of tissues. They are composed of transmembrane cadherin proteins, which connect to the actin cytoskeleton inside the cell through intracellular adaptor proteins such as catenins.

The cadherins on opposing cells interact with each other to form adhesive bonds that help to anchor the cells together and regulate various cellular processes, including cell growth, differentiation, and migration. Adherens junctions are essential for many physiological processes, such as embryonic development, wound healing, and tissue homeostasis, and their dysfunction has been implicated in a variety of diseases, including cancer and degenerative disorders.

Cell adhesion molecules (CAMs) are a type of protein found on the surface of cells that mediate the attachment or adhesion of cells to either other cells or to the extracellular matrix (ECM), which is the network of proteins and carbohydrates that provides structural and biochemical support to surrounding cells.

CAMs play crucial roles in various biological processes, including tissue development, differentiation, repair, and maintenance of tissue architecture and function. They are also involved in cell signaling, migration, and regulation of the immune response.

There are several types of CAMs, classified based on their structure and function, such as immunoglobulin-like CAMs (IgCAMs), cadherins, integrins, and selectins. Dysregulation of CAMs has been implicated in various diseases, including cancer, inflammation, and neurological disorders.

Cell aggregation is the process by which individual cells come together and adhere to each other to form a group or cluster. This phenomenon can occur naturally during embryonic development, tissue repair, and wound healing, as well as in the formation of multicellular organisms such as slime molds. In some cases, cell aggregation may also be induced in the laboratory setting through the use of various techniques, including the use of cell culture surfaces that promote cell-to-cell adhesion or the addition of factors that stimulate the expression of adhesion molecules on the cell surface.

Cell aggregation can be influenced by a variety of factors, including the type and properties of the cells involved, as well as environmental conditions such as pH, temperature, and nutrient availability. The ability of cells to aggregate is often mediated by the presence of adhesion molecules on the cell surface, such as cadherins, integrins, and immunoglobulin-like cell adhesion molecules (Ig-CAMs). These molecules interact with each other and with extracellular matrix components to promote cell-to-cell adhesion and maintain the stability of the aggregate.

In some contexts, abnormal or excessive cell aggregation can contribute to the development of diseases such as cancer, fibrosis, and inflammatory disorders. For example, the aggregation of cancer cells can facilitate their invasion and metastasis, while the accumulation of fibrotic cells in tissues can lead to organ dysfunction and failure. Understanding the mechanisms that regulate cell aggregation is therefore an important area of research with potential implications for the development of new therapies and treatments for a variety of diseases.

Desmoglein 3 is a type of desmoglein protein that is primarily found in the upper layers of the epidermis, specifically in the desmosomes of the skin. Desmogleins are part of the cadherin family of cell adhesion molecules and play a crucial role in maintaining the structural integrity and cohesion of tissues, particularly in areas subjected to mechanical stress.

Desmoglein 3 is essential for the formation and maintenance of desmosomal junctions in stratified squamous epithelia, such as the skin and mucous membranes. It is involved in cell-to-cell adhesion by forming calcium-dependent homophilic interactions with other Desmoglein 3 molecules on adjacent cells.

Mutations in the gene encoding Desmoglein 3 have been associated with several skin disorders, including pemphigus vulgaris, a severe autoimmune blistering disease that affects the mucous membranes and skin. In pemphigus vulgaris, autoantibodies target Desmoglein 3 (and sometimes Desmoglein 1) molecules, leading to loss of cell-to-cell adhesion and formation of blisters and erosions.

Armadillo (ARM) domain proteins are a family of conserved cytoskeletal proteins characterized by the presence of armadillo repeats, which are structural motifs involved in protein-protein interactions. These proteins play crucial roles in various cellular processes such as signal transduction, cell adhesion, and intracellular transport.

The ARM domain is composed of multiple tandem repeats (usually 4 to 12) of approximately 40-42 amino acid residues. Each repeat forms a pair of antiparallel alpha-helices that stack together to create a superhelix structure, which provides a binding surface for various partner proteins.

Examples of ARM domain proteins include:

1. β-catenin and plakoglobin (also known as γ-catenin): These proteins are essential components of the Wnt signaling pathway, where they interact with transcription factors to regulate gene expression. They also play a role in cell adhesion by binding to cadherins at the plasma membrane.
2. Paxillin: A focal adhesion protein that interacts with various structural and signaling molecules, including integrins, growth factor receptors, and kinases, to regulate cell migration and adhesion.
3. Importin-α: A nuclear transport receptor that recognizes and binds to cargo proteins containing a nuclear localization signal (NLS), facilitating their import into the nucleus through interaction with importin-β and the nuclear pore complex.
4. DEC1 (also known as STRA13): A transcriptional repressor involved in cell differentiation, apoptosis, and circadian rhythm regulation.
5. HEF1/NEDD9: A scaffolding protein that interacts with various signaling molecules to regulate cell migration, adhesion, and survival.
6. p120-catenin: A member of the catenin family that regulates cadherin stability and function in cell adhesion.

These proteins have been implicated in several human diseases, including cancer, cardiovascular disease, and neurological disorders.

Trans-activators are proteins that increase the transcriptional activity of a gene or a set of genes. They do this by binding to specific DNA sequences and interacting with the transcription machinery, thereby enhancing the recruitment and assembly of the complexes needed for transcription. In some cases, trans-activators can also modulate the chromatin structure to make the template more accessible to the transcription machinery.

In the context of HIV (Human Immunodeficiency Virus) infection, the term "trans-activator" is often used specifically to refer to the Tat protein. The Tat protein is a viral regulatory protein that plays a critical role in the replication of HIV by activating the transcription of the viral genome. It does this by binding to a specific RNA structure called the Trans-Activation Response Element (TAR) located at the 5' end of all nascent HIV transcripts, and recruiting cellular cofactors that enhance the processivity and efficiency of RNA polymerase II, leading to increased viral gene expression.

Morphogenesis is a term used in developmental biology and refers to the process by which cells give rise to tissues and organs with specific shapes, structures, and patterns during embryonic development. This process involves complex interactions between genes, cells, and the extracellular environment that result in the coordinated movement and differentiation of cells into specialized functional units.

Morphogenesis is a dynamic and highly regulated process that involves several mechanisms, including cell proliferation, death, migration, adhesion, and differentiation. These processes are controlled by genetic programs and signaling pathways that respond to environmental cues and regulate the behavior of individual cells within a developing tissue or organ.

The study of morphogenesis is important for understanding how complex biological structures form during development and how these processes can go awry in disease states such as cancer, birth defects, and degenerative disorders.

Plakophilins are a group of proteins that play a crucial role in the structure and function of desmosomes, which are specialized cell-cell junctions found in epithelial and cardiac muscle cells. Desmosomes help to maintain the integrity and stability of tissues by providing strong adhesive connections between adjacent cells.

Plakophilins are members of the armadillo protein family and have several important functions within desmosomes:

1. Scaffolding: Plakophilins act as scaffolding proteins, helping to organize and link various components of the desmosome together. They bind to desmocollin and desmoglein adhesion molecules, as well as to other structural proteins such as plakoglobin and intermediate filaments.
2. Signal transduction: Plakophilins also play a role in signal transduction pathways related to cell growth, differentiation, and survival. They can interact with various signaling molecules, including kinases, phosphatases, and transcription factors, thereby modulating their activity.
3. Regulation of desmosome assembly and disassembly: Plakophilins are involved in the regulation of desmosome formation and breakdown. They can bind to proteins that promote desmosome assembly or disassembly, depending on cellular conditions and requirements.

There are four main isoforms of plakophilin (PKP1-4) in humans, each with distinct expression patterns and functions. Mutations in the genes encoding plakophilins have been associated with various genetic disorders, including arrhythmogenic right ventricular cardiomyopathy (ARVC), ectodermal dysplasia-syndactyly syndrome (EDSS), and skin fragility-woolly hair syndrome (SFWHS).

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Cell communication, also known as cell signaling, is the process by which cells exchange and transmit signals between each other and their environment. This complex system allows cells to coordinate their functions and maintain tissue homeostasis. Cell communication can occur through various mechanisms including:

1. Autocrine signaling: When a cell releases a signal that binds to receptors on the same cell, leading to changes in its behavior or function.
2. Paracrine signaling: When a cell releases a signal that binds to receptors on nearby cells, influencing their behavior or function.
3. Endocrine signaling: When a cell releases a hormone into the bloodstream, which then travels to distant target cells and binds to specific receptors, triggering a response.
4. Synaptic signaling: In neurons, communication occurs through the release of neurotransmitters that cross the synapse and bind to receptors on the postsynaptic cell, transmitting electrical or chemical signals.
5. Contact-dependent signaling: When cells physically interact with each other, allowing for the direct exchange of signals and information.

Cell communication is essential for various physiological processes such as growth, development, differentiation, metabolism, immune response, and tissue repair. Dysregulation in cell communication can contribute to diseases, including cancer, diabetes, and neurological disorders.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Pemphigus is a group of rare, autoimmune blistering diseases that affect the skin and mucous membranes. In these conditions, the immune system mistakenly produces antibodies against desmoglein proteins, which are crucial for maintaining cell-to-cell adhesion in the epidermis (outermost layer of the skin). This results in the loss of keratinocyte cohesion and formation of flaccid blisters filled with serous fluid.

There are several types of pemphigus, including:

1. Pemphigus vulgaris - The most common form, primarily affecting middle-aged to older adults, with widespread erosions and flaccid blisters on the skin and mucous membranes (e.g., mouth, nose, genitals).
2. Pemphigus foliaceus - A more superficial form, mainly involving the skin, causing crusted erosions and scaly lesions without mucosal involvement. It is more prevalent in older individuals and in certain geographical regions like the Middle East.
3. Paraneoplastic pemphigus - A rare type associated with underlying neoplasms (cancers), such as lymphomas or carcinomas, characterized by severe widespread blistering of both skin and mucous membranes, along with antibodies against additional antigens besides desmogleins.
4. IgA pemphigus - A less common form characterized by localized or generalized erosions and blisters, with IgA autoantibodies targeting the basement membrane zone.

Treatment for pemphigus typically involves high-dose systemic corticosteroids, often in combination with immunosuppressive agents (e.g., azathioprine, mycophenolate mofetil, rituximab) to control the disease activity and prevent complications. Regular follow-ups with dermatologists and oral specialists are essential for monitoring treatment response and managing potential side effects.

Receptor-like protein tyrosine phosphatases, class 2 (RPTPs-Class 2) are a subfamily of receptor-like protein tyrosine phosphatases that play crucial roles in various cellular processes, including cell growth, differentiation, and migration. These transmembrane enzymes are characterized by the presence of two extracellular fibronectin type III domains, a single membrane-spanning region, and one or two intracellular protein tyrosine phosphatase (PTP) domains.

RPTPs-Class 2 include four members in humans: PTPRD, PTPRF, PTPRG, and PTPRH. These enzymes can dephosphorylate and modulate the activity of various proteins involved in signal transduction pathways by removing phosphate groups from tyrosine residues. By doing so, RPTPs-Class 2 help regulate the balance between kinase-mediated phosphorylation and phosphatase-mediated dephosphorylation events, which is essential for proper cellular function.

Mutations in RPTPs-Class 2 genes have been associated with various human diseases, including cancer, neurological disorders, and developmental abnormalities. Therefore, understanding the structure, regulation, and functions of these enzymes can provide valuable insights into disease mechanisms and potential therapeutic strategies.

The cytoskeleton is a complex network of various protein filaments that provides structural support, shape, and stability to the cell. It plays a crucial role in maintaining cellular integrity, intracellular organization, and enabling cell movement. The cytoskeleton is composed of three major types of protein fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. These filaments work together to provide mechanical support, participate in cell division, intracellular transport, and help maintain the cell's architecture. The dynamic nature of the cytoskeleton allows cells to adapt to changing environmental conditions and respond to various stimuli.

Developmental gene expression regulation refers to the processes that control the activation or repression of specific genes during embryonic and fetal development. These regulatory mechanisms ensure that genes are expressed at the right time, in the right cells, and at appropriate levels to guide proper growth, differentiation, and morphogenesis of an organism.

Developmental gene expression regulation is a complex and dynamic process involving various molecular players, such as transcription factors, chromatin modifiers, non-coding RNAs, and signaling molecules. These regulators can interact with cis-regulatory elements, like enhancers and promoters, to fine-tune the spatiotemporal patterns of gene expression during development.

Dysregulation of developmental gene expression can lead to various congenital disorders and developmental abnormalities. Therefore, understanding the principles and mechanisms governing developmental gene expression regulation is crucial for uncovering the etiology of developmental diseases and devising potential therapeutic strategies.

"Xenopus proteins" refer to the proteins that are expressed or isolated from the Xenopus species, which are primarily used as model organisms in biological and biomedical research. The most commonly used Xenopus species for research are the African clawed frogs, Xenopus laevis and Xenopus tropicalis. These proteins play crucial roles in various cellular processes and functions, and they serve as valuable tools to study different aspects of molecular biology, developmental biology, genetics, and biochemistry.

Some examples of Xenopus proteins that are widely studied include:

1. Xenopus Histones: These are the proteins that package DNA into nucleosomes, which are the fundamental units of chromatin in eukaryotic cells. They play a significant role in gene regulation and epigenetic modifications.
2. Xenopus Cyclins and Cyclin-dependent kinases (CDKs): These proteins regulate the cell cycle and control cell division, differentiation, and apoptosis.
3. Xenopus Transcription factors: These proteins bind to specific DNA sequences and regulate gene expression during development and in response to various stimuli.
4. Xenopus Signaling molecules: These proteins are involved in intracellular signaling pathways that control various cellular processes, such as cell growth, differentiation, migration, and survival.
5. Xenopus Cytoskeletal proteins: These proteins provide structural support to the cells and regulate their shape, motility, and organization.
6. Xenopus Enzymes: These proteins catalyze various biochemical reactions in the cell, such as metabolic pathways, DNA replication, transcription, and translation.

Overall, Xenopus proteins are essential tools for understanding fundamental biological processes and have contributed significantly to our current knowledge of molecular biology, genetics, and developmental biology.

Vinculin is a protein found in many types of cells, including muscle and endothelial cells. It is primarily located at the sites of cell-cell and cell-matrix adhesions, where it plays important roles in cell adhesion, mechanotransduction, and cytoskeletal organization. Vinculin interacts with several other proteins, including actin, talin, and integrins, to form a complex network that helps regulate the connection between the extracellular matrix and the intracellular cytoskeleton. Mutations in the vinculin gene have been associated with certain inherited diseases, such as muscular dystrophy-cardiomyopathy syndrome.

Receptor-like protein tyrosine phosphatases, class 8 (RPTPs μ/β) are a subfamily of the receptor-like protein tyrosine phosphatase superfamily. These transmembrane proteins contain two extracellular carbonic anhydrase-like domains, a single membrane-spanning region, and one intracellular protein tyrosine phosphatase domain. They are involved in the regulation of various cellular processes, including cell growth, differentiation, and migration, by dephosphorylating specific tyrosine residues on target proteins. RPTPs μ/β have been implicated in the development and function of the nervous system, and their dysregulation has been associated with several neurological disorders and cancers.

Keratinocytes are the predominant type of cells found in the epidermis, which is the outermost layer of the skin. These cells are responsible for producing keratin, a tough protein that provides structural support and protection to the skin. Keratinocytes undergo constant turnover, with new cells produced in the basal layer of the epidermis and older cells moving upward and eventually becoming flattened and filled with keratin as they reach the surface of the skin, where they are then shed. They also play a role in the immune response and can release cytokines and other signaling molecules to help protect the body from infection and injury.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Actin is a type of protein that forms part of the contractile apparatus in muscle cells, and is also found in various other cell types. It is a globular protein that polymerizes to form long filaments, which are important for many cellular processes such as cell division, cell motility, and the maintenance of cell shape. In muscle cells, actin filaments interact with another type of protein called myosin to enable muscle contraction. Actins can be further divided into different subtypes, including alpha-actin, beta-actin, and gamma-actin, which have distinct functions and expression patterns in the body.

Cell polarity refers to the asymmetric distribution of membrane components, cytoskeleton, and organelles in a cell. This asymmetry is crucial for various cellular functions such as directed transport, cell division, and signal transduction. The plasma membrane of polarized cells exhibits distinct domains with unique protein and lipid compositions that define apical, basal, and lateral surfaces of the cell.

In epithelial cells, for example, the apical surface faces the lumen or external environment, while the basolateral surface interacts with other cells or the extracellular matrix. The establishment and maintenance of cell polarity are regulated by various factors including protein complexes, lipids, and small GTPases. Loss of cell polarity has been implicated in several diseases, including cancer and neurological disorders.

Epithelial cells are types of cells that cover the outer surfaces of the body, line the inner surfaces of organs and glands, and form the lining of blood vessels and body cavities. They provide a protective barrier against the external environment, regulate the movement of materials between the internal and external environments, and are involved in the sense of touch, temperature, and pain. Epithelial cells can be squamous (flat and thin), cuboidal (square-shaped and of equal height), or columnar (tall and narrow) in shape and are classified based on their location and function.

Phosphoproteins are proteins that have been post-translationally modified by the addition of a phosphate group (-PO3H2) onto specific amino acid residues, most commonly serine, threonine, or tyrosine. This process is known as phosphorylation and is mediated by enzymes called kinases. Phosphoproteins play crucial roles in various cellular processes such as signal transduction, cell cycle regulation, metabolism, and gene expression. The addition or removal of a phosphate group can activate or inhibit the function of a protein, thereby serving as a switch to control its activity. Phosphoproteins can be detected and quantified using techniques such as Western blotting, mass spectrometry, and immunofluorescence.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

Cell-matrix junctions, also known as focal adhesions, are specialized structures found at the interface between cells and the extracellular matrix (ECM). These junctions play a critical role in cell adhesion, migration, and signaling. They are formed by the interaction of transmembrane receptors called integrins with ECM proteins such as collagen, fibronectin, and laminin.

The intracellular portion of integrins is linked to the cytoskeleton via a complex network of adaptor proteins, including talin, vinculin, paxillin, and focal adhesion kinase (FAK). This connection allows for the transmission of forces between the ECM and the cytoskeleton, which is essential for cell movement and maintenance of tissue structure.

Cell-matrix junctions also serve as sites of signal transduction, where mechanical signals from the ECM can be converted into biochemical signals that regulate various cellular processes such as gene expression, proliferation, differentiation, and survival. Dysregulation of cell-matrix junctions has been implicated in a variety of diseases, including fibrosis, cancer, and neurodegenerative disorders.

In situ hybridization (ISH) is a molecular biology technique used to detect and localize specific nucleic acid sequences, such as DNA or RNA, within cells or tissues. This technique involves the use of a labeled probe that is complementary to the target nucleic acid sequence. The probe can be labeled with various types of markers, including radioisotopes, fluorescent dyes, or enzymes.

During the ISH procedure, the labeled probe is hybridized to the target nucleic acid sequence in situ, meaning that the hybridization occurs within the intact cells or tissues. After washing away unbound probe, the location of the labeled probe can be visualized using various methods depending on the type of label used.

In situ hybridization has a wide range of applications in both research and diagnostic settings, including the detection of gene expression patterns, identification of viral infections, and diagnosis of genetic disorders.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

The Fluorescent Antibody Technique (FAT) is a type of immunofluorescence assay used in laboratory medicine and pathology for the detection and localization of specific antigens or antibodies in tissues, cells, or microorganisms. In this technique, a fluorescein-labeled antibody is used to selectively bind to the target antigen or antibody, forming an immune complex. When excited by light of a specific wavelength, the fluorescein label emits light at a longer wavelength, typically visualized as green fluorescence under a fluorescence microscope.

The FAT is widely used in diagnostic microbiology for the identification and characterization of various bacteria, viruses, fungi, and parasites. It has also been applied in the diagnosis of autoimmune diseases and certain cancers by detecting specific antibodies or antigens in patient samples. The main advantage of FAT is its high sensitivity and specificity, allowing for accurate detection and differentiation of various pathogens and disease markers. However, it requires specialized equipment and trained personnel to perform and interpret the results.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.

A precipitin test is a type of immunodiagnostic test used to detect and measure the presence of specific antibodies or antigens in a patient's serum. The test is based on the principle of antigen-antibody interaction, where the addition of an antigen to a solution containing its corresponding antibody results in the formation of an insoluble immune complex known as a precipitin.

In this test, a small amount of the patient's serum is added to a solution containing a known antigen or antibody. If the patient has antibodies or antigens that correspond to the added reagent, they will bind and form a visible precipitate. The size and density of the precipitate can be used to quantify the amount of antibody or antigen present in the sample.

Precipitin tests are commonly used in the diagnosis of various infectious diseases, autoimmune disorders, and allergies. They can also be used in forensic science to identify biological samples. However, they have largely been replaced by more modern immunological techniques such as enzyme-linked immunosorbent assays (ELISAs) and radioimmunoassays (RIAs).

Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.

Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.

Cell movement, also known as cell motility, refers to the ability of cells to move independently and change their location within tissue or inside the body. This process is essential for various biological functions, including embryonic development, wound healing, immune responses, and cancer metastasis.

There are several types of cell movement, including:

1. **Crawling or mesenchymal migration:** Cells move by extending and retracting protrusions called pseudopodia or filopodia, which contain actin filaments. This type of movement is common in fibroblasts, immune cells, and cancer cells during tissue invasion and metastasis.
2. **Amoeboid migration:** Cells move by changing their shape and squeezing through tight spaces without forming protrusions. This type of movement is often observed in white blood cells (leukocytes) as they migrate through the body to fight infections.
3. **Pseudopodial extension:** Cells extend pseudopodia, which are temporary cytoplasmic projections containing actin filaments. These protrusions help the cell explore its environment and move forward.
4. **Bacterial flagellar motion:** Bacteria use a whip-like structure called a flagellum to propel themselves through their environment. The rotation of the flagellum is driven by a molecular motor in the bacterial cell membrane.
5. **Ciliary and ependymal movement:** Ciliated cells, such as those lining the respiratory tract and fallopian tubes, have hair-like structures called cilia that beat in coordinated waves to move fluids or mucus across the cell surface.

Cell movement is regulated by a complex interplay of signaling pathways, cytoskeletal rearrangements, and adhesion molecules, which enable cells to respond to environmental cues and navigate through tissues.

Immunoblotting, also known as western blotting, is a laboratory technique used in molecular biology and immunogenetics to detect and quantify specific proteins in a complex mixture. This technique combines the electrophoretic separation of proteins by gel electrophoresis with their detection using antibodies that recognize specific epitopes (protein fragments) on the target protein.

The process involves several steps: first, the protein sample is separated based on size through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Next, the separated proteins are transferred onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric field. The membrane is then blocked with a blocking agent to prevent non-specific binding of antibodies.

After blocking, the membrane is incubated with a primary antibody that specifically recognizes the target protein. Following this, the membrane is washed to remove unbound primary antibodies and then incubated with a secondary antibody conjugated to an enzyme such as horseradish peroxidase (HRP) or alkaline phosphatase (AP). The enzyme catalyzes a colorimetric or chemiluminescent reaction that allows for the detection of the target protein.

Immunoblotting is widely used in research and clinical settings to study protein expression, post-translational modifications, protein-protein interactions, and disease biomarkers. It provides high specificity and sensitivity, making it a valuable tool for identifying and quantifying proteins in various biological samples.

Integrins are a type of cell-adhesion molecule that play a crucial role in cell-cell and cell-extracellular matrix (ECM) interactions. They are heterodimeric transmembrane receptors composed of non-covalently associated α and β subunits, which form more than 24 distinct integrin heterodimers in humans.

Integrins bind to specific ligands, such as ECM proteins (e.g., collagen, fibronectin, laminin), cell surface molecules, and soluble factors, through their extracellular domains. The intracellular domains of integrins interact with the cytoskeleton and various signaling proteins, allowing them to transduce signals from the ECM into the cell (outside-in signaling) and vice versa (inside-out signaling).

These molecular interactions are essential for numerous biological processes, including cell adhesion, migration, proliferation, differentiation, survival, and angiogenesis. Dysregulation of integrin function has been implicated in various pathological conditions, such as cancer, fibrosis, inflammation, and autoimmune diseases.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Rac1 (Ras-related C3 botulinum toxin substrate 1) is a GTP-binding protein, which belongs to the Rho family of small GTPases. These proteins function as molecular switches that regulate various cellular processes such as actin cytoskeleton organization, gene expression, cell proliferation, and differentiation.

Rac1 cycles between an inactive GDP-bound state and an active GTP-bound state. When Rac1 is in its active form (GTP-bound), it interacts with various downstream effectors to modulate the actin cytoskeleton dynamics, cell adhesion, and motility. Activation of Rac1 has been implicated in several cellular responses, including cell migration, membrane ruffling, and filopodia formation.

Rac1 GTP-binding protein plays a crucial role in many physiological processes, such as embryonic development, angiogenesis, and wound healing. However, dysregulation of Rac1 activity has been associated with various pathological conditions, including cancer, inflammation, and neurological disorders.

The epidermis is the outermost layer of the skin, composed mainly of stratified squamous epithelium. It forms a protective barrier that prevents water loss and inhibits the entry of microorganisms. The epidermis contains no blood vessels, and its cells are nourished by diffusion from the underlying dermis. The bottom-most layer of the epidermis, called the stratum basale, is responsible for generating new skin cells that eventually move up to replace dead cells on the surface. This process of cell turnover takes about 28 days in adults.

The most superficial part of the epidermis consists of dead cells called squames, which are constantly shed and replaced. The exact rate at which this happens varies depending on location; for example, it's faster on the palms and soles than elsewhere. Melanocytes, the pigment-producing cells, are also located in the epidermis, specifically within the stratum basale layer.

In summary, the epidermis is a vital part of our integumentary system, providing not only physical protection but also playing a crucial role in immunity and sensory perception through touch receptors called Pacinian corpuscles.

Acantholysis is a medical term that refers to the separation of the cells in the upper layer of the skin (the epidermis), specifically between the pickle cell layer (stratum spinosum) and the granular cell layer (stratum granulosum). This separation results in the formation of distinct, round, or oval cells called acantholytic cells, which are typically seen in certain skin conditions.

Acantholysis is a characteristic feature of several skin disorders, including:

1. Pemphigus vulgaris: A rare autoimmune blistering disorder where the immune system produces antibodies against desmoglein-1 and -3 proteins, leading to acantholysis and formation of flaccid blisters.
2. Pemphigus foliaceus: Another autoimmune blistering disorder that specifically targets desmoglein-1 protein, causing superficial blisters and erosions on the skin.
3. Hailey-Hailey disease (familial benign chronic pemphigus): An autosomal dominant genetic disorder affecting ATP2C1 gene, leading to defective calcium transport and abnormal keratinocyte adhesion, resulting in acantholysis and recurrent skin eruptions.
4. Darier's disease (keratosis follicularis): An autosomal dominant genetic disorder affecting ATP2A2 gene, causing dysfunction of calcium transport and abnormal keratinocyte adhesion, resulting in acantholysis and characteristic papular or keratotic skin lesions.
5. Grover's disease (transient acantholytic dermatosis): An acquired skin disorder of unknown cause, characterized by the development of pruritic, red, and scaly papules and vesicles due to acantholysis.

The presence of acantholysis in these conditions can be confirmed through histopathological examination of skin biopsies.

Gastrulation is a fundamental process in embryonic development, characterized by the transformation of a initially flat layer of cells called the blastula into a three-layered structure known as the gastrula. This complex series of cellular movements and rearrangements establishes the foundation for the formation of the three primary germ layers: the ectoderm, mesoderm, and endoderm. These germ layers further differentiate to give rise to all the diverse cell types and tissues in the developing organism, including the nervous system, muscles, bones, and internal organs.

The precise mechanisms of gastrulation vary among different animal groups; however, common features include:

1. Formation of a blastopore: A small indentation or opening that forms on the surface of the blastula, which eventually develops into the primitive gut or anus in the gastrula.
2. Invagination: The process by which cells at the blastopore fold inward and migrate towards the interior of the embryo, forming the endodermal layer.
3. Epiboly: A coordinated movement of cells that spreads over and encloses the yolk within the embryo, contributing to the formation of the ectodermal layer.
4. Delamination: The separation and migration of cells from the epiblast (the outer layer of the blastula) to form the mesodermal layer in between the ectoderm and endoderm.

Gastrulation is a critical period in embryonic development, as errors during this process can lead to severe congenital abnormalities or even embryonic lethality. A thorough understanding of gastrulation has important implications for regenerative medicine, stem cell research, and the study of evolutionary developmental biology (Evo-Devo).

Cytoplasm is the material within a eukaryotic cell (a cell with a true nucleus) that lies between the nuclear membrane and the cell membrane. It is composed of an aqueous solution called cytosol, in which various organelles such as mitochondria, ribosomes, endoplasmic reticulum, Golgi apparatus, lysosomes, and vacuoles are suspended. Cytoplasm also contains a variety of dissolved nutrients, metabolites, ions, and enzymes that are involved in various cellular processes such as metabolism, signaling, and transport. It is where most of the cell's metabolic activities take place, and it plays a crucial role in maintaining the structure and function of the cell.

Amino acid repetitive sequences refer to patterns of amino acids that are repeated in a polypeptide chain. These repetitions can vary in length and can be composed of a single type of amino acid or a combination of different types. In some cases, expansions of these repetitive sequences can lead to the production of abnormal proteins that are associated with certain genetic disorders. The expansion of trinucleotide repeats that code for particular amino acids is one example of this phenomenon. These expansions can result in protein misfolding and aggregation, leading to neurodegenerative diseases such as Huntington's disease and spinocerebellar ataxias.

Immunoelectron microscopy (IEM) is a specialized type of electron microscopy that combines the principles of immunochemistry and electron microscopy to detect and localize specific antigens within cells or tissues at the ultrastructural level. This technique allows for the visualization and identification of specific proteins, viruses, or other antigenic structures with a high degree of resolution and specificity.

In IEM, samples are first fixed, embedded, and sectioned to prepare them for electron microscopy. The sections are then treated with specific antibodies that have been labeled with electron-dense markers, such as gold particles or ferritin. These labeled antibodies bind to the target antigens in the sample, allowing for their visualization under an electron microscope.

There are several different methods of IEM, including pre-embedding and post-embedding techniques. Pre-embedding involves labeling the antigens before embedding the sample in resin, while post-embedding involves labeling the antigens after embedding. Post-embedding techniques are generally more commonly used because they allow for better preservation of ultrastructure and higher resolution.

IEM is a valuable tool in many areas of research, including virology, bacteriology, immunology, and cell biology. It can be used to study the structure and function of viruses, bacteria, and other microorganisms, as well as the distribution and localization of specific proteins and antigens within cells and tissues.

Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.

Cell differentiation is the process by which a less specialized cell, or stem cell, becomes a more specialized cell type with specific functions and structures. This process involves changes in gene expression, which are regulated by various intracellular signaling pathways and transcription factors. Differentiation results in the development of distinct cell types that make up tissues and organs in multicellular organisms. It is a crucial aspect of embryonic development, tissue repair, and maintenance of homeostasis in the body.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Cellular mechanotransduction is the process by which cells convert mechanical stimuli into biochemical signals, resulting in changes in cell behavior and function. This complex process involves various molecular components, including transmembrane receptors, ion channels, cytoskeletal proteins, and signaling molecules. Mechanical forces such as tension, compression, or fluid flow can activate these components, leading to alterations in gene expression, protein synthesis, and cell shape or movement. Cellular mechanotransduction plays a crucial role in various physiological processes, including tissue development, homeostasis, and repair, as well as in pathological conditions such as fibrosis and cancer progression.

Synaptophysin is a protein found in the presynaptic vesicles of neurons, which are involved in the release of neurotransmitters during synaptic transmission. It is often used as a marker for neuronal differentiation and is widely expressed in neuroendocrine cells and tumors. Synaptophysin plays a role in the regulation of neurotransmitter release and has been implicated in various neurological disorders, including Alzheimer's disease and synaptic dysfunction-related conditions.

Biological models, also known as physiological models or organismal models, are simplified representations of biological systems, processes, or mechanisms that are used to understand and explain the underlying principles and relationships. These models can be theoretical (conceptual or mathematical) or physical (such as anatomical models, cell cultures, or animal models). They are widely used in biomedical research to study various phenomena, including disease pathophysiology, drug action, and therapeutic interventions.

Examples of biological models include:

1. Mathematical models: These use mathematical equations and formulas to describe complex biological systems or processes, such as population dynamics, metabolic pathways, or gene regulation networks. They can help predict the behavior of these systems under different conditions and test hypotheses about their underlying mechanisms.
2. Cell cultures: These are collections of cells grown in a controlled environment, typically in a laboratory dish or flask. They can be used to study cellular processes, such as signal transduction, gene expression, or metabolism, and to test the effects of drugs or other treatments on these processes.
3. Animal models: These are living organisms, usually vertebrates like mice, rats, or non-human primates, that are used to study various aspects of human biology and disease. They can provide valuable insights into the pathophysiology of diseases, the mechanisms of drug action, and the safety and efficacy of new therapies.
4. Anatomical models: These are physical representations of biological structures or systems, such as plastic models of organs or tissues, that can be used for educational purposes or to plan surgical procedures. They can also serve as a basis for developing more sophisticated models, such as computer simulations or 3D-printed replicas.

Overall, biological models play a crucial role in advancing our understanding of biology and medicine, helping to identify new targets for therapeutic intervention, develop novel drugs and treatments, and improve human health.

Dimerization is a process in which two molecules, usually proteins or similar structures, bind together to form a larger complex. This can occur through various mechanisms, such as the formation of disulfide bonds, hydrogen bonding, or other non-covalent interactions. Dimerization can play important roles in cell signaling, enzyme function, and the regulation of gene expression.

In the context of medical research and therapy, dimerization is often studied in relation to specific proteins that are involved in diseases such as cancer. For example, some drugs have been developed to target and inhibit the dimerization of certain proteins, with the goal of disrupting their function and slowing or stopping the progression of the disease.

Rho GTP-binding proteins are a subfamily of the Ras superfamily of small GTPases, which function as molecular switches in various cellular signaling pathways. These proteins play crucial roles in regulating diverse cellular processes such as actin cytoskeleton dynamics, gene expression, cell cycle progression, and cell migration.

Rho GTP-binding proteins cycle between an active GTP-bound state and an inactive GDP-bound state. In the active state, they interact with various downstream effectors to regulate their respective cellular functions. Guanine nucleotide exchange factors (GEFs) activate Rho GTP-binding proteins by promoting the exchange of GDP for GTP, while GTPase-activating proteins (GAPs) inactivate them by enhancing their intrinsic GTP hydrolysis activity.

There are several members of the Rho GTP-binding protein family, including RhoA, RhoB, RhoC, Rac1, Rac2, Rac3, Cdc42, and Rnd proteins, each with distinct functions and downstream effectors. Dysregulation of Rho GTP-binding proteins has been implicated in various human diseases, including cancer, cardiovascular disease, neurological disorders, and inflammatory diseases.

Calcium is an essential mineral that is vital for various physiological processes in the human body. The medical definition of calcium is as follows:

Calcium (Ca2+) is a crucial cation and the most abundant mineral in the human body, with approximately 99% of it found in bones and teeth. It plays a vital role in maintaining structural integrity, nerve impulse transmission, muscle contraction, hormonal secretion, blood coagulation, and enzyme activation.

Calcium homeostasis is tightly regulated through the interplay of several hormones, including parathyroid hormone (PTH), calcitonin, and vitamin D. Dietary calcium intake, absorption, and excretion are also critical factors in maintaining optimal calcium levels in the body.

Hypocalcemia refers to low serum calcium levels, while hypercalcemia indicates high serum calcium levels. Both conditions can have detrimental effects on various organ systems and require medical intervention to correct.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

"Xenopus laevis" is not a medical term itself, but it refers to a specific species of African clawed frog that is often used in scientific research, including biomedical and developmental studies. Therefore, its relevance to medicine comes from its role as a model organism in laboratories.

In a broader sense, Xenopus laevis has contributed significantly to various medical discoveries, such as the understanding of embryonic development, cell cycle regulation, and genetic research. For instance, the Nobel Prize in Physiology or Medicine was awarded in 1963 to John R. B. Gurdon and Sir Michael J. Bishop for their discoveries concerning the genetic mechanisms of organism development using Xenopus laevis as a model system.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

'Tumor cells, cultured' refers to the process of removing cancerous cells from a tumor and growing them in controlled laboratory conditions. This is typically done by isolating the tumor cells from a patient's tissue sample, then placing them in a nutrient-rich environment that promotes their growth and multiplication.

The resulting cultured tumor cells can be used for various research purposes, including the study of cancer biology, drug development, and toxicity testing. They provide a valuable tool for researchers to better understand the behavior and characteristics of cancer cells outside of the human body, which can lead to the development of more effective cancer treatments.

It is important to note that cultured tumor cells may not always behave exactly the same way as they do in the human body, so findings from cell culture studies must be validated through further research, such as animal models or clinical trials.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

A nonmammalian embryo refers to the developing organism in animals other than mammals, from the fertilized egg (zygote) stage until hatching or birth. In nonmammalian species, the developmental stages and terminology differ from those used in mammals. The term "embryo" is generally applied to the developing organism up until a specific stage of development that is characterized by the formation of major organs and structures. After this point, the developing organism is referred to as a "larva," "juvenile," or other species-specific terminology.

The study of nonmammalian embryos has played an important role in our understanding of developmental biology and evolutionary developmental biology (evo-devo). By comparing the developmental processes across different animal groups, researchers can gain insights into the evolutionary origins and diversification of body plans and structures. Additionally, nonmammalian embryos are often used as model systems for studying basic biological processes, such as cell division, gene regulation, and pattern formation.

CDC42 is a small GTP-binding protein that belongs to the Rho family of GTPases. It acts as a molecular switch, cycling between an inactive GDP-bound state and an active GTP-bound state, and plays a critical role in regulating various cellular processes, including actin cytoskeleton organization, cell polarity, and membrane trafficking.

When CDC42 is activated by Guanine nucleotide exchange factors (GEFs), it interacts with downstream effectors to modulate the assembly of actin filaments and the formation of membrane protrusions, such as lamellipodia and filopodia. These cellular structures are essential for cell migration, adhesion, and morphogenesis.

CDC42 also plays a role in intracellular signaling pathways that regulate gene expression, cell cycle progression, and apoptosis. Dysregulation of CDC42 has been implicated in various human diseases, including cancer, neurodegenerative disorders, and immune disorders.

In summary, CDC42 is a crucial GTP-binding protein involved in regulating multiple cellular processes, and its dysfunction can contribute to the development of several pathological conditions.

CHO cells, or Chinese Hamster Ovary cells, are a type of immortalized cell line that are commonly used in scientific research and biotechnology. They were originally derived from the ovaries of a female Chinese hamster (Cricetulus griseus) in the 1950s.

CHO cells have several characteristics that make them useful for laboratory experiments. They can grow and divide indefinitely under appropriate conditions, which allows researchers to culture large quantities of them for study. Additionally, CHO cells are capable of expressing high levels of recombinant proteins, making them a popular choice for the production of therapeutic drugs, vaccines, and other biologics.

In particular, CHO cells have become a workhorse in the field of biotherapeutics, with many approved monoclonal antibody-based therapies being produced using these cells. The ability to genetically modify CHO cells through various methods has further expanded their utility in research and industrial applications.

It is important to note that while CHO cells are widely used in scientific research, they may not always accurately represent human cell behavior or respond to drugs and other compounds in the same way as human cells do. Therefore, results obtained using CHO cells should be validated in more relevant systems when possible.

Intermediate filaments (IFs) are a type of cytoskeletal filament found in the cytoplasm of eukaryotic cells, including animal cells. They are called "intermediate" because they are smaller in diameter than microfilaments and larger than microtubules, two other types of cytoskeletal structures.

Intermediate filaments are composed of fibrous proteins that form long, unbranched, and flexible filaments. These filaments provide structural support to the cell and help maintain its shape. They also play a role in cell-to-cell adhesion, intracellular transport, and protection against mechanical stress.

Intermediate filaments are classified into six types based on their protein composition: Type I (acidic keratins), Type II (neutral/basic keratins), Type III (vimentin, desmin, peripherin), Type IV (neurofilaments), Type V (lamins), and Type VI (nestin). Each type of intermediate filament has a specific function and is expressed in different cell types. For example, Type I and II keratins are found in epithelial cells, while vimentin is expressed in mesenchymal cells.

Overall, intermediate filaments play an essential role in maintaining the structural integrity of cells and tissues, and their dysfunction has been implicated in various human diseases, including cancer, neurodegenerative disorders, and genetic disorders.

Gene expression is the process by which the information encoded in a gene is used to synthesize a functional gene product, such as a protein or RNA molecule. This process involves several steps: transcription, RNA processing, and translation. During transcription, the genetic information in DNA is copied into a complementary RNA molecule, known as messenger RNA (mRNA). The mRNA then undergoes RNA processing, which includes adding a cap and tail to the mRNA and splicing out non-coding regions called introns. The resulting mature mRNA is then translated into a protein on ribosomes in the cytoplasm through the process of translation.

The regulation of gene expression is a complex and highly controlled process that allows cells to respond to changes in their environment, such as growth factors, hormones, and stress signals. This regulation can occur at various stages of gene expression, including transcriptional activation or repression, RNA processing, mRNA stability, and translation. Dysregulation of gene expression has been implicated in many diseases, including cancer, genetic disorders, and neurological conditions.

... cadherin 7, type 2 CDH8 - cadherin 8, type 2 CDH9 - cadherin 9, type 2 (T1-cadherin) CDH10 - cadherin 10, type 2 (T2-cadherin) ... CDH2 - N-cadherin (neural): N-cadherins are found in neurons CDH12 - cadherin 12, type 2 (N-cadherin 2) CDH3 - P-cadherin ( ... Proteopedia Cadherin - view cadherin structure in interactive 3D Cadherin domain in PROSITE The cadherin family The Cadherin ... T-cadherin - H-cadherin (heart) CDH15 - M-cadherin (myotubule) CDH16 - KSP-cadherin CDH17 - LI cadherin (liver-intestine) CDH18 ...
... , also known as cadherin 13, H-cadherin (heart), and CDH13, is a unique member of the cadherin superfamily of ... 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 ... Transfection of T-cadherin negative neuroblastoma TGW and NH-12 cells with T-cadherin results in their loss of mitogenic ...
... or Epithelial cadherin (E-cadherin), (not to be confused with the APC/C activator protein CDH1) is a protein that in ... E-cadherin can sequester β-catenin on the cell membrane by the cytoplasmic tail of E-cadherin. Loss of E-cadherin expression ... Cadherin-1 is a classical member of the cadherin superfamily. The encoded protein is a calcium-dependent cell-cell adhesion ... E-cadherin (epithelial) is the most well-studied member of the cadherin family and is an essential transmembrane protein within ...
... , a classical cadherin from the cadherin superfamily, is composed of five extracellular cadherin repeats, a ... Cadherin-2 also known as Neural cadherin (N-cadherin), is a protein that in humans is encoded by the CDH2 gene. CDH2 has also ... Cadherin-2, as well as other cadherins, interact with Cadherin-2 on an adjacent cell in an anti-parallel conformation, thus ... Cadherin-2, originally named Neural cadherin for its role in neural tissue, plays a role in neurons and later was found to also ...
... is a classical cadherin from the cadherin superfamily and the gene is located in a six-cadherin cluster in a region ... Cadherin-5, or VE-cadherin (vascular endothelial cadherin), also known as CD144 (Cluster of Differentiation 144), is a type of ... "Functional properties of human vascular endothelial cadherin (7B4/cadherin-5), an endothelium-specific cadherin". Arterioscler ... VE-cadherin is indispensable for proper vascular development - there have been two transgenic mouse models of VE-cadherin ...
In molecular biology, the cadherin cytoplasmic region is a conserved region found at the C-terminus of cadherin proteins. A key ... Nagafuchi A, Takeichi M (December 1988). "Cell binding function of E-cadherin is regulated by the cytoplasmic domain". EMBO J. ... of the cadherin. This region induces clustering and also binds to the protein catenin (p120ctn). The cytoplasmic region is ... "The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction ...
... is a protein that in humans is encoded by the FAT3 gene. GRCh38: Ensembl release 89: ENSG00000165323 - ... "Entrez Gene: FAT atypical cadherin 3". Berndt JD, Aoyagi A, Yang P, Anastas JN, Tang L, Moon RT (September 2011). "Mindbomb 1, ... Mitsui K, Nakajima D, Ohara O, Nakayama M (February 2002). "Mammalian fat3: a large protein that contains multiple cadherin and ...
... (CDHR3), also known as CDH28 or its abbreviation CDHR3, is a protein that in humans is encoded ... "Entrez Gene: Cadherin related family member 3". Retrieved 2017-09-05. "Tissue expression of CDHR3 - Summary - The Human Protein ... April 2015). "Cadherin-related family member 3, a childhood asthma susceptibility gene product, mediates rhinovirus C binding ... Bochkov YA, Watters K, Ashraf S, Griggs TF, Devries MK, Jackson DJ, Palmenberg AC, Gern JE (April 2015). "Cadherin-related ...
Dimerized cadherins readily bind to their presynaptic cadherin partners. Inhibition of N-cadherin binding via blocking ... N-cadherins are transmembrane proteins expressed in the majority of CNS synapses. N-cadherins are most commonly expressed on ... At basal levels of synaptic activity, N-cadherins are largely monomers and are thus weakly adhesive to cadherins located in the ... P120 ctn proteins are thought to either inhibit endocytosis of neural cadherins, or act at the cell surface to control cadherin ...
2000). "Clustered cadherin genes: a sequence-ready contig for the desmosomal cadherin locus on human chromosome 18". Genomics. ... Garrod DR, Merritt AJ, Nie Z (2003). "Desmosomal cadherins". Curr. Opin. Cell Biol. 14 (5): 537-45. doi:10.1016/S0955-0674(02) ... Jun 1993). "Nomenclature of the desmosomal cadherins". J Cell Biol. 121 (3): 481-3. doi:10.1083/jcb.121.3.481. PMC 2119574. ... 2000). "Genomic organization and amplification of the human desmosomal cadherin genes DSC1 and DSC3, encoding desmocollin types ...
... is required for its high affinity binding to the cytoplasmic domains of E-cadherin and desmosomal cadherin Dsg2, and the tumor ... is required for its high affinity binding to the cytoplasmic domains of E-cadherin and desmosomal cadherin Dsg2, and the tumor ... Bannon LJ, Cabrera BL, Stack MS, Green KJ (Nov 2001). "Isoform-specific differences in the size of desmosomal cadherin/catenin ... Bannon LJ, Cabrera BL, Stack MS, Green KJ (Nov 2001). "Isoform-specific differences in the size of desmosomal cadherin/catenin ...
They are involved in regulating the adhesive activity of cadherin. The three types of plakophilin proteins found in humans are ... The Molecular Biology of Cadherins. Academic Press. 116: 387-407. doi:10.1016/b978-0-12-394311-8.00017-0. PMC 3752792. PMID ...
Desmosomal cadherins, including the desmocollin family members and desmogleins, are found at desmosome cell-cell junctions and ... Cadherin-like junctional molecules generated by alternative splicing". The Journal of Biological Chemistry. 266 (16): 10438-45 ... Desmocollin-2 is a cadherin-type protein that functions to link adjacent cells together in specialized regions known as ... Desmocollin-2 is a calcium-dependent glycoprotein that is a member of the desmocollin subfamily of the cadherin superfamily. ...
Rolf Kemler's anti serum was what helped him finally identify cadherin. E-cadherin was the first of the cadherin family to be ... After his discovery of cadherins, he continued to research cadherins and their properties. Along with cadherins, he also ... An assay showed the hemaglutinin interaction is specific to e-cadherin. Outside of cadherin, Takeichi studied other molecules ... They found the hemagglutinin directly interacted with the e-cadherin in the epithelial cells to disturbed cell to cell adhesion ...
Desmocollin-3 is a calcium-dependent glycoprotein that is a member of the desmocollin subfamily of the cadherin superfamily. ... Jun 1993). "Nomenclature of the desmosomal cadherins" (PDF). J Cell Biol. 121 (3): 481-3. doi:10.1083/jcb.121.3.481. PMC ... 2001). "Down-regulation of the desmosomal cadherin desmocollin 3 in human breast cancer". Int. J. Oncol. 19 (1): 169-74. doi: ... 2000). "Genomic organization and amplification of the human desmosomal cadherin genes DSC1 and DSC3, encoding desmocollin types ...
Müller, U (October 2008). "Cadherins and mechanotransduction by hair cells". Current Opinion in Cell Biology. 20 (5): 557-566. ...
Cadherins are calcium-dependent adhesion molecules. Cadherins are extremely important in the process of morphogenesis - fetal ... Cadherin molecules form the actual anchor by attaching to the cytoplasmic plaque, extending through the membrane and binding ... Together with an alpha-beta catenin complex, the cadherin can bind to the microfilaments of the cytoskeleton of the cell. This ... Similarly to desmosomes and hemidesmosomes, their transmembrane anchors are composed of cadherins in those that anchor to other ...
Amagai M (1999). "Autoimmunity against desmosomal cadherins in pemphigus". J. Dermatol. Sci. 20 (2): 92-102. doi:10.1016/S0923- ...
Cadherin-17 is a protein that in humans is encoded by the CDH17 gene. This gene is a member of the cadherin superfamily, genes ... 2004). "Ksp-cadherin is a functional cell-cell adhesion molecule related to LI-cadherin". Exp. Cell Res. 294 (2): 345-55. doi: ... "Entrez Gene: CDH17 cadherin 17, LI cadherin (liver-intestine)". Gessner R, Tauber R (2001). "Intestinal cell adhesion molecules ... The encoded protein is cadherin-like, consisting of an extracellular region, containing 7 cadherin domains, and a transmembrane ...
The encoded protein has a signal peptide, 27 cadherin repeat domains and a unique cytoplasmic region. This particular cadherin ... Protein dachsous homolog 1, also known as protocadherin-16 (PCDH16) or cadherin-19 (CDH19) or cadherin-25 (CDH25) or fibroblast ... cadherin-1 (FIB1), is a protein that in humans is encoded by the DCHS1 gene. This gene is a member of the cadherin superfamily ... 2001). "Identification of three novel non-classical cadherin genes through comprehensive analysis of large cDNAs". Brain Res. ...
... forms distinct complexes with cadherins and desmosomal cadherins. Plakoglobin is a major cytoplasmic component of ... is required for its high affinity binding to the cytoplasmic domains of E-cadherin and desmosomal cadherin Dsg2, and the tumor ... interacts with E-cadherin and N-cadherin". The Journal of Cell Biology. 118 (3): 671-9. doi:10.1083/jcb.118.3.671. PMC 2289540 ... interacts with E-cadherin and N-cadherin". The Journal of Cell Biology. 118 (3): 671-9. doi:10.1083/jcb.118.3.671. PMC 2289540 ...
P-cadherins), neural (N-cadherins), retinal (R-cadherins), brain (B-cadherins and T-cadherins), and muscle (M-cadherins). Many ... The cadherins are homophilic Ca2+ -dependent glycoproteins. The classic cadherins (E-, N- and P-) are concentrated at the ... Cadherins are notable in embryonic development. For example, cadherins are crucial in gastrulation for the formation of the ... The diverse family of cadherins include epithelial (E-cadherins), placental ( ...
These neural cadherin-like cell adhesion proteins most likely play a critical role in the establishment and function of ... Wu Q, Maniatis T (Jul 1999). "A striking organization of a large family of human neural cadherin-like cell adhesion genes". ... Each variable region exon encodes the extracellular region, which includes 6 cadherin ectodomains and a transmembrane region. ... Matsuyoshi N, Imamura S (1997). "Multiple cadherins are expressed in human fibroblasts". Biochem. Biophys. Res. Commun. 235 (2 ...
Larue, L.; Antos, C.; Butz, S.; Huber, O.; Delmas, V.; Dominis, M.; Kemler, R. (1996). "A role for cadherins in tissue ... Burdsal, C. A.; Damsky, C. H.; Pedersen, R. A. (1993). "The role of E-cadherin and integrins in mesoderm differentiation and ... EBs are formed by the homophilic binding of the Ca2+ dependent adhesion molecule E-cadherin, which is highly expressed on ...
The human FAT1 cadherin gene was cloned in 1995 from a human T-leukemia (T-ALL) cell line and consists of 27 exons located on ... FAT1 cadherin is multiply phosphorylated on its ectodomain but phosphorylation is not catalysed by FJX1. The ectodomain of FAT1 ... The FAT1 cadherin has been ascribed both as putative tumour suppressor or oncogene in different contexts. Loss of ... December 2015). "FAT1 cadherin acts upstream of Hippo signalling through TAZ to regulate neuronal differentiation". Cellular ...
Cadherin 10 is a protein that in humans is encoded by the CDH10 gene. An association with autism has been suggested. Cadherin ... "Entrez Gene: cadherin 10". Suzuki S, Sano K, Tanihara H (April 1991). "Diversity of the cadherin family: evidence for eight new ... Ali J, Liao F, Martens E, Muller WA (1997). "Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial cell- ... Kools P, Vanhalst K, Van den Eynde E, van Roy F (1999). "The human cadherin-10 gene: complete coding sequence, predominant ...
Cadherin 9 is a protein that in humans is encoded by the CDH9 gene. An association with autism has been suggested. Cadherin ... "Entrez Gene: cadherin 9". Suzuki S, Sano K, Tanihara H (April 1991). "Diversity of the cadherin family: evidence for eight new ... Ali J, Liao F, Martens E, Muller WA (June 1997). "Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial ... Thedieck C, Kalbacher H, Kuczyk M, Müller GA, Müller CA, Klein G (2007). Zoccali C (ed.). "Cadherin-9 is a novel cell surface ...
Dusek, Rachel L; Godsel, Lisa M.; l, Kathleen J. (January 2007). "Discriminating roles of desmosomal cadherins:Beyond ...
Cadherin-1), CDH2 N-cadherin (Cadherin-2), CDH4 R-cadherin (cadherin-4), CDH5 VE-cadherin (cadherin 5, CDH5), CTNND1 ( ... Cadherins regulate cell-cell adhesion during development of the body and in adult tissue. Disruption of cadherin proteins, by ... Cadherins stabilize adherens junctions through the interaction of the cadherin cytoplasmic domains with catenin proteins, such ... PTPmu likely regulates cadherin-dependent adhesion by interacting with both cadherins and catenins via PTPmu's cytoplasmic ...
The flamingo cadherins are located at the plasma membrane and have nine cadherin domains, seven epidermal growth factor-like ... Cadherin EGF LAG seven-pass G-type receptor 2 is a protein that in humans is encoded by the CELSR2 gene. The protein encoded by ... "Entrez Gene: CELSR2 cadherin, EGF LAG seven-pass G-type receptor 2 (flamingo homolog, Drosophila)". Nagase T, Seki N, Ishikawa ... Wu Q, Maniatis T (1999). "A striking organization of a large family of human neural cadherin-like cell adhesion genes". Cell. ...
... cadherin 7, type 2 CDH8 - cadherin 8, type 2 CDH9 - cadherin 9, type 2 (T1-cadherin) CDH10 - cadherin 10, type 2 (T2-cadherin) ... CDH2 - N-cadherin (neural): N-cadherins are found in neurons CDH12 - cadherin 12, type 2 (N-cadherin 2) CDH3 - P-cadherin ( ... Proteopedia Cadherin - view cadherin structure in interactive 3D Cadherin domain in PROSITE The cadherin family The Cadherin ... T-cadherin - H-cadherin (heart) CDH15 - M-cadherin (myotubule) CDH16 - KSP-cadherin CDH17 - LI cadherin (liver-intestine) CDH18 ...
003179 STOCK |i|Cdh2|sup|tm1Hyn|/sup||/i|/J These |i| Cdh2|/i| knock-out mice exhibit embryonic lethality and malformation of structures resulting from neurulation and somitogenesis.
Protein target information for Cadherin-1 (zebrafish). Find diseases associated with this biological target and compounds ...
E-cadherin (uvomorulin), N-cadherin (neural cadherin), R-cadherin, cadherin 5, L-CAM, and EP-cadherin. N-cadherin mRNA is found ... E-cadherin (uvomorulin), N-cadherin (neural cadherin), R-cadherin, cadherin 5, L-CAM, and EP-cadherin. N-cadherin mRNA is found ... However, N-cadherin also interacts with a PTP1B-like phosphatase that dephosphorylates β-catenin and promotes N-cadherin/actin ... However, N-cadherin also interacts with a PTP1B-like phosphatase that dephosphorylates β-catenin and promotes N-cadherin/actin ...
More like The Lifestory Of A Cadherin Assignment. Essay On A History Of The Beatles. 2530 words - 11 pages ... Probably the ... The Lifestory Of A Cadherin. 1234 words - 5 pages Anchoring junctions occur in two functionally different forms:Adherens ... Anti-cadherin antibodies that block theformation of adherens junctions, for example, also block the formation of tightjunctions ... Affected individuals make antibodiesagainst one of their own desmosomal cadherin proteins. These antibodies bindto and disrupt ...
In this regard E-Cadherin (E-cad) is a 120 kDa polypeptide present in all epithelial tissues and it is the prime mediator of ... In this regard E-Cadherin (E-cad) is a 120 kDa polypeptide present in all epithelial tissues and it is the prime mediator of ... Differential expression of e-cadherin in normal, metaplastic and dysplastic esophageal mucosa - a putative biomarker Int J ...
This gene is a classical cadherin from the cadherin superfamily. The encoded protein is a calcium dependent cell-cell adhesion ... Recombinant protein of human cadherin 1, type 1, E-cadherin (epithelial) (CDH1), 20 µg ... Transient overexpression lysate of cadherin 1, type 1, E-cadherin (epithelial) (CDH1) ... glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. ...
A complementary cadherin code is required in phrenic motor neurons and respiratory interneurons to generate robust breathing ... Here, we show that coordinated activity of a type I cadherin (N-cadherin) and type II cadherins (Cadherin-6, -9, and -10) is ... It has recently been demonstrated that type I cadherins, such as N-cadherin, can mask the contributions of type II cadherins in ... and the type II cadherins Cdh6, 9, 10, 11, and 22 (Vagnozzi et al., 2020). While the type I cadherin N-cadherin and the type II ...
Crystal structure of mouse N-cadherin EC1-2 with AA insertion between residues 2 and 3 ... Type I cadherin cell-adhesion proteins are similar in sequence and structure and yet are different enough to mediate highly ... Structural and energetic determinants of adhesive binding specificity in type I cadherins.. Vendome, J., Felsovalyi, K., Song, ... electron paramagnetic resonance spectroscopy to identify the molecular determinants of type I cadherin dimerization affinities ...
The loss of E-cadherin (E-cad), an epithelial cell adhesion molecule, has been implicated in the epithelial-mesenchymal ... Serine synthesis pathway upregulated by E-cadherin is essential for the proliferation and metastasis of breast cancers bioRxiv ... The loss of E-cadherin (E-cad), an epithelial cell adhesion molecule, has been implicated in the epithelial-mesenchymal ...
E-cadherin plays an essential role in collective directional migration of large epithelial sheets.. Return to Grants ... Furthermore, E-cadherin blocking antibodies abolished migration of cell sheets. Traction force analysis revealed an important ... Our study thus identifies a novel mechanism--E-cadherin dependence and coordinated traction forces of leading cells in ...
N-cadherin) is a 130 kD, single pass transmembrane protein. ... Cadherin-2, Neural cadherin Isotype Mouse IgG1, κ Ave. Rating ... CD325 (N-cadherin) is a 130 kD, single pass transmembrane protein. Its extracellular region consists of five EC domains and has ... N-cadherin is expressed by stem cells, myeloblasts, endothelial cells, and fibroblasts, and also is expressed in neural and ... Recombinant human N-cadherin extracellular domain Formulation Phosphate-buffered solution, pH 7.2, containing 0.09% sodium ...
View Mouse P-Cadherin Alexa Fluor® 488-conjugated Antibody (FAB761G-100UG) datasheet. ... CAD3; cadherin 3, P-cadherin (placental); cadherin 3, type 1, P-cadherin (placental); Cadherin-3; CDH3; CDHP; CDHPcalcium- ... Background: P-Cadherin. Placental Cadherin (P-Cadherin or PCAD) is a member of the cadherin family of cell adhesion molecules, ... P-Cadherin is a classical cadherin molecule. Classical cadherins consist of a large extracellular domain which contains DXD and ...
Integrating barcoded neuroanatomy with spatial transcriptional profiling reveals cadherin correlates of projections shared ... Integrating barcoded neuroanatomy with spatial transcriptional profiling reveals cadherin correlates of projections shared ... Integrating barcoded neuroanatomy with spatial transcriptional profiling reveals cadherin correlates of projections shared ... Integrating barcoded neuroanatomy with spatial transcriptional profiling reveals cadherin correlates of projections shared ...
Using N-cadherin as a model for classical cadherins, the binding affinity of full length N-cadherin (N-cad EC1-5) expressed on ... Cadherin, binding affinity. Abstract. Cadherins are transmembrane glycoproteins that are involved in maintaining integrity of ... In my thesis, I have focused on studying the binding affinity of a class of cadherin superfamily called N-cadherins. Prior ... The first chapter of my thesis, I talked about the structural differences of most studied cadherins E and N-cadherins and ...
Cadherin-like receptor binding facilitates proteolytic cleavage of helix alpha-1 in domain I and oligomer pre-pore formation of ... TY - JOUR T1 - Cadherin-like receptor binding facilitates proteolytic cleavage of helix alpha-1 in domain I and oligomer pre- ... Cadherin-like receptor binding facilitates proteolytic cleavage of helix alpha-1 in domain I and oligomer pre-pore formation of ... "Cadherin-like Receptor Binding Facilitates Proteolytic Cleavage of Helix Alpha-1 in Domain I and Oligomer Pre-pore Formation of ...
E-cadherin, and vimentin in esophageal squamous cell carcinoma ... The expression of SOX2, vimentin, and E-cadherin were ... Prognostic significance of sex determining region Y-box 2, E-cadherin, and vimentin in esophageal squamous cell carcinoma. ... Prognostic significance of sex determining region Y-box 2, E-cadherin, and vimentin in esophageal squamous cell carcinoma ...
Loss of E-cadherin function or expression has been implicated in cancer progression and metastasis. E-cadherin downregulation ... Alternative Names CAM 120/80, Epithelial cadherin, E-cadherin, Uvomorulin, CD antigen CD324 [Cleaved into: E-Cad/CTF1; E-Cad/ ... Anti-E-Cadherin Antibody (34060) quantity. Add to cart. SKU: 34060 Categories: Antibody Products, Cancer Research Antibodies, ... Background E-cadherin is a calcium-dependent intercellular adhesion molecule encoded by the CDH1 gene and present on epithelial ...
Desmosomal cadherins utilize distinct kinesins for assembly into desmosomes Desmosomal cadherins utilize distinct kinesins for ... Desmosomal cadherins utilize distinct kinesins for assembly into desmosomes Oxana E. Nekrasova, Oxana E. Nekrasova ... Desmosomal cadherins utilize distinct kinesins for assembly into desmosomes. J Cell Biol 24 June 2013; 201 (7): 1085. doi: ...
Tags: art, brain, CA neurons, CA1, CA2, CA3, cadherin, cadherin-10, cerebral cortex, dentate gyrus, hippocampus, mouse ... 1] A catenin-dependent balance between N-cadherin and E-cadherin controls neuroectodermal cell fate choices. Rogers CD, ... cadherin. Students Contribute to Research Through Ovarian Art Posted on February 21st, 2019. by Dr. Francis Collins ... Tags: BioArt, cadherin, development, developmental biology, Drosophila melanogaster, embryology, embryos, fruit fly, microscopy ...
Understanding the spatial and functional relationship between cadherins and neuroligins at synapses Aiga, Mytyl Abstract. ... Cadherins and Neuroligins (NLs) are two of the most extensively studied cell adhesion molecules (CAMs) at synapses and have ... Furthermore, N-cadherin expression can partially rescue synapse loss that is due to knockdown of NL1 expression. Together this ... Cadherins and Neuroligins (NLs) are two of the most extensively studied cell adhesion molecules (CAMs) at synapses and have ...
VE-cadherin and N-cadherin. The importance of VE-cadherin in vascular development is well known; however, the f ... Endothelial cells express two classic cadherins, VE-cadherin and N-cadherin. The importance of VE-cadherin in vascular ... VE-cadherin is dependent on N-cadherin To confirm the efficiency of the Tie2-Cre-mediated deletion, we examined N-cadherin ... N-cadherin regulates VE-cadherin expression in human endothelial cells To further examine the function of N-cadherin in ...
Cancers publication investigating the role of E-cadherin in hereditary fuse gastric cancer utilising mouse model derived from ... Loss of E-Cadherin Leads to Druggable Vulnerabilities in Sphingolipid Metabolism and Vesicle Trafficking. Tom Brew, Nicola ... Loss of E-Cadherin Leads to Druggable Vulnerabilities in Sphingolipid Metabolism and Vesicle Trafficking ... Loss of E-Cadherin Leads to Druggable Vulnerabilities in Sphingolipid Metabolism and Vesicle Trafficking ...
Keywords: colon cancer, invasion, metastasis, E-cadherin, dehydropeptidase 1. Received: October 20, 2015 Accepted: January 19, ... DPEP1 inhibited the leukotriene D4 signaling pathway and increased the expression of E-cadherin. We also show that DPEP1 ... These results suggest that DPEP1 promotes cancer metastasis by regulating E-cadherin plasticity and that it might be a ... TGF-β treatment decreased E-cadherin expression and promoted cell invasion in DPEP1-expressing colon cancer cell lines, whereas ...
Cadherin-11 (cad-11) is a novel member of the cadherin family of cell adhesion molecules, having recently been identified by ... For comparison, we studied the expression of N-cadherin and found that the expressions of these two cadherins were differential ... or R-cadherin when they were mixed, indicating that this novel cadherin has a homophilic binding specificity, as found for ... Cadherin-11 expressed in association with mesenchymal morphogenesis in the head, somite, and limb bud of early mouse embryos.. ...
E-cadherins are found in epithelial tissue; N-cadherins are found in neurons; and P-cadherins are found in the placenta. T- ... E-cadherin (epithelial) is probably the best understood cadherin. It consists of 5 cadherin repeats (EC1 ~ EC5) in the ... Cadherins within one class will bind only to themselves. For example, an N-cadherin will bind only to another N-cadherin ... Loss of E-cadherin function or expression has been implicated in cancer progression and metastasis. E-cadherin downregulation ...
... Gomes, Alessandra F. et al. ... Toxoplasma gondii down modulates cadherin expression in skeletal muscle cells inhibiting myogenesis. BMC Microbiology, v.11, n. ...
Aims : Vascular endothelial (VE)-cadherin, also known as cadherin-5 and CD144, is an adhesion molecule uniquely expressed in ... Both VE-cadherin and PECAM-1 had significantly reduced expression in lobular compared with ductal carcinomas: there was no ... Q-PCR revealed elevated levels of VE-cadherin and PECAM-1 in tumour samples compared with background tissue and in patients ... We hypothesized that VE-cadherin may be a useful marker for assessing microvessels and angiogenesis in human breast cancer and ...
VE-cadherin) level and anti-A/B IgG titer in the prenatal diagnosis of ABO hemolytic disease. Methods We conducted a case- ... Objective To study the value of maternal vascular endothelial cadherin ( ... Objective To study the value of maternal vascular endothelial cadherin (VE-cadherin) level and anti-A/B IgG titer in the ... Vascular endothelial cadherin(VE-cadherin) is a membrane protein that is the major component of endothelial cell-to-cell ...
  • Cowin P. Unraveling the cytoplasmic interactions of the cadherin superfamily. (bdbiosciences.com)
  • This gene is a classical cadherin from the cadherin superfamily. (origene.com)
  • In my thesis, I have focused on studying the binding affinity of a class of cadherin superfamily called N-cadherins. (illinois.edu)
  • In this review, we will provide a brief overview of the cadherin superfamily, describe cadherin family members expressed in central neurons, cadherin-catenin complexes in central neurons and then focus on role of the cadherin-catenin complex in dendrite morphogenesis and synapse morphogenesis, function and plasticity. (nebraska.edu)
  • This gene encodes a classical cadherin of the cadherin superfamily. (ebiocell.com)
  • NCAD is a member of the Cadherin superfamily, and consists of five extracellular repeats, a transmembrane domain and a cytoplasmic domain. (neobiotechnologies.com)
  • The gene product is a member of the cadherin superfamily, a group of integral membrane proteins characterized by the presence of cadherin-type repeats. (nih.gov)
  • N Cadherin is a classical cadherin and member of the cadherin superfamily. (arigobio.cn)
  • One current model proposes that cells distinguish cadherin subtypes based on kinetic specificity rather than thermodynamic specificity, as different types of cadherin homotypic bonds have different lifetimes. (wikipedia.org)
  • These results demonstrate the importance of the flanking amino acids next to HAV sequence in cadherin specificity as well as the possible application of small peptide sequence HAVDI as a novel antagonist in processes involving N-cadherin mediated adhesion. (illinois.edu)
  • Specificity Human E-cadherin. (qedbio.com)
  • Transfection of L cells with cDNA led them to acquire a typical cadherin-dependent cell-cell adhesiveness, and the L cells expressing cad-11 did not coaggregate with L cells expressing E-, P-, N-, or R-cadherin when they were mixed, indicating that this novel cadherin has a homophilic binding specificity, as found for other cadherins. (duke.edu)
  • Because of this specificity, groups of cells that express the same type of cadherin molecule tend to cluster together during development , whereas cells expressing different types of cadherin molecules tend to separate. (wikidoc.org)
  • The intracellular portion of classical cadherins interacts with a complex of proteins that allows connection to the actin cytoskeleton. (wikipedia.org)
  • This association links the cadherin protein to the cytoskeleton. (rndsystems.com)
  • The adherens junction provides strong cell-cell adhesion mediated by the cadherin-catenin complex via its linkage to the actin cytoskeleton ( Wheelock and Johnson, 2003 ). (rupress.org)
  • In epithelial cells, E-cadherin-containing cell-to-cell junctions are often adjacent to actin-containing filaments of the cytoskeleton . (wikidoc.org)
  • The cytoplasmic region is highly conserved in sequence and has been shown experimentally to regulate the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton. (ecmbio.com)
  • Incubation of Cry1Ab protoxin with a single chain antibody that mimics the cadherin-like receptor and treatment with Manduca sexta midgut juice or trypsin, resulted in toxin preparations with high pore-forming activity in vitro. (unboundmedicine.com)
  • E-Cadherin Mouse Monoclonal Antibody detects endogenous levels of E-Cadherin protein. (ebiocell.com)
  • The antibody detects a band at ~ 130 kDa in western blots of Human endothelial cells and Mouse brain tissue, and does not cross-react with E Cadherin. (arigobio.cn)
  • The antibody detects endogenous N-cadherin protein. (arigobio.cn)
  • This antibody was affinity purified using E-cadherin (a.a. 774-786) peptide. (ecmbio.com)
  • In western blots, the antibody detects a 120 kDa band corresponding to E-cadherin in human A431 cells, and does not detect VE-cadherin or N-Cadherin. (ecmbio.com)
  • Western blot analysis of human heart tissue lysate using N-Cadherin Recombinant Rabbit Monoclonal Antibody (CDH2/6857R). (neobiotechnologies.com)
  • Formalin-fixed, paraffin-embedded human ovarian carcinoma stained with N-Cadherin Recombinant Rabbit Monoclonal Antibody (CDH2/6857R). (neobiotechnologies.com)
  • Mouse anti Human N-cadherin antibody, clone 13A9 studies have demonstrated that expression levels of E-Cadherin and N-Cadherin have a role to play in the invasive properties of breast cancer. (arigobio.cn)
  • 1999).Mouse anti Human N-cadherin antibody, clone 13A9 has been shown to be specific for N-cadherin, and does not recognize E-cadherin, M-cadherin or P-cadherin (Knudsen et al. (arigobio.cn)
  • The immunohistochemistry technique was performed by the estreptovidine biotine method using E-cadherin as the primary antibody. (bvsalud.org)
  • Recombinant Human N Cadherin-Protein is expressed from HEK293 with hFc tag at the C-Terminus.It contains Asp160-Ala724. (kactusbio.com)
  • Human N Cadherin on Tris-Bis PAGE under reduced condition. (kactusbio.com)
  • Recombinant MBP fusion protein containing the entire cytoplasmic domain of human N-cadherin. (arigobio.cn)
  • Homo sapiens cadherin 1 (CDH1), transcript variant 1, mRNA. (origene.com)
  • Background E-cadherin is a calcium-dependent intercellular adhesion molecule encoded by the CDH1 gene and present on epithelial cells. (qedbio.com)
  • Classical cadherins maintain the tone of tissues by forming a homodimer in cis while desmosomal cadherins are heterodimeric. (wikipedia.org)
  • Although classical cadherins take a role in cell layer formation and structure formation, desmosomal cadherins focus on resisting cell damage. (wikipedia.org)
  • Similar to classical cadherins, desmosomal cadherins have a single transmembrane domain, five EC repeats, and an intracellular domain. (wikipedia.org)
  • Classical cadherins consist of a large extracellular domain which contains DXD and DXNDN repeats responsible for mediating calcium-dependent adhesion, a single-pass transmembrane domain, and a short carboxy-terminal cytoplasmic domain responsible for interacting with the catenins. (rndsystems.com)
  • Using N-cadherin as a model for classical cadherins, the binding affinity of full length N-cadherin (N-cad EC1-5) expressed on a test cell surface (here, mesenchymal stem cell (MSCs) with the first two extracellular domains (N-cad EC1-2) and the binding pocket sequence HAVDI peptide and full length N-cadherin (N-cad EC 1-5) were measured by this assay. (illinois.edu)
  • In this review, we discuss the roles of the classical cadherins and catenins in various aspects of dendrite and synapse architecture and function and their relevance to human neurological disorders. (nebraska.edu)
  • The cadherin family is composed of more than 100 members and classified into several subfamilies, including classical cadherins and protocadherins. (nebraska.edu)
  • Several of these cadherin family members have been implicated in various aspects of neuronal development and function.1-3 The classical cadherins are associated with a group of cytosolic proteins, collectively called the catenins. (nebraska.edu)
  • Anti-cadherin antibodies that block theformation of adherens junctions, for example, also block the formation of tightjunctions.Desmosomes Connect Intermediate Filaments from Cell toCellDesmosomes are buttonlike points of intercellular contact that rivet cellsTogether. (ostatic.com)
  • Furthermore, E-cadherin blocking antibodies abolished migration of cell sheets. (ca.gov)
  • Methods and results : Frozen sections from breast cancer primary tumours (tumour n = 114, background n = 30) were immunostained with VE-cadherin, factor VIII and PECAM-1 antibodies and microvessel number was assessed. (cardiff.ac.uk)
  • Each cadherin has a small C-terminal cytoplasmic component, a transmembrane component, and the remaining bulk of the protein is extra-cellular (outside the cell). (wikipedia.org)
  • Once the cell-cell adhesion between cadherins present in the cell membranes of two different cells has formed, adherens junctions can then be made when protein complexes, usually composed of α-, β-, and γ-catenins, bind to the cytoplasmic portion of the cadherin. (wikipedia.org)
  • Mechanisms such as mRNA expression, cytokine modulation, and protease-mediated turnover modulate N-cadherin protein levels during development. (bdbiosciences.com)
  • Thus, N-cadherin is an integral adhesion molecule whose function is regulated by protein-protein interactions and phosphorylation/dephosphorylation events. (bdbiosciences.com)
  • The encoded protein is a calcium dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. (origene.com)
  • CD325 (N-cadherin) is a 130 kD, single pass transmembrane protein. (biolegend.com)
  • Mouse P-Cadherin is an 822 amino acid (aa) protein with a 27 aa signal sequence and a 795 aa propeptide. (rndsystems.com)
  • Cadherin-11 (CDH11 or CAD11) is a type II classical cadherin which is an integral membrane protein that is responsible for mediating calcium dependent cell-cell adhesion. (elisakits.co.uk)
  • E Cadherin is an adhesion protein that is expressed in cells of epithelial lineage. (celltechgen.com)
  • Recognizes a protein of ~140kDa, identified as N-Cadherin (NCAD), also known as CD325. (neobiotechnologies.com)
  • Objective: To establish the correlation of the clinical staging of epidermoid intrabuccal carcinoma with the expression pattern of the E-cadherin protein. (bvsalud.org)
  • Moreover, pharmacological or genetic activation of inositol -requiring enzyme 1α, a central regulator of ER stress, downregulated T- cadherin at the mRNA and protein levels as well as attenuated EV production . (bvsalud.org)
  • In direct ELISAs and Western blots, no cross-reactivity with recombinant human (rh) N-Cadherin, recombinant mouse (rm) VE-Cadherin, rhCadherin-8, or rhCadherin-17 is observed. (rndsystems.com)
  • Immunogen Recombinant human E-cadherin. (qedbio.com)
  • The loss of E-cadherin (E-cad), an epithelial cell adhesion molecule, has been implicated in the epithelial-mesenchymal transition (EMT), promoting invasion and migration of cancer cells and, consequently, metastasis. (nih.gov)
  • Loss of E-cadherin function or expression has been implicated in cancer progression and metastasis. (qedbio.com)
  • These results suggest that DPEP1 promotes cancer metastasis by regulating E-cadherin plasticity and that it might be a potential therapeutic target for preventing the progression of colon cancer. (oncotarget.com)
  • Furthermore, CD325 is normally involved in inducing cell cycle arrest and its expression is frequently deregulated in cancer cells.Studies have linked N-cadherin to cancer metastasis by showing the aggressive tumor cells had preferentially turned on N-cadherin as opposed to E- or P-cadherin. (neobiotechnologies.com)
  • N-cadherin is directly involved in the differentiation of early hematopoietic progenitors, and is commonly expressed by cancer cells, playing a role in transendothelial migration and metastasis, through the up-regulation of the src kinase pathway, and subsequent failure of the intercellular connection between two adjacent endothelial cells. (arigobio.cn)
  • Decreased levels of E-cadherin and loss of E-cadherin-mediated adhesion, can result in the transition of a benign epithelial tumor to an invasive tumor, and increase invasiveness, whilst the expression of N-cadherin correlates with motility, invasiveness and tumor metastasis, irrespective of the presence of E-cadherin (Nieman et al. (arigobio.cn)
  • Cell-cell adhesion is mediated by extracellular cadherin domains, whereas the intracellular cytoplasmic tail associates with numerous adaptors and signaling proteins, collectively referred to as the cadherin adhesome. (wikipedia.org)
  • The mAb 8C11 recognizes the amino acids 92-593 of CD325, located between the extracellular cadherin structural domain (EC) 3 and 4. (biolegend.com)
  • In addition, several groups have observed heterotypic binding affinity (i.e., binding of different types of cadherin together) in various assays. (wikipedia.org)
  • In structure, they share cadherin repeats, which are the extracellular Ca2+-binding domains. (wikipedia.org)
  • Because cadherins are Ca2+ dependent, they have five tandem extracellular domain repeats that act as the binding site for Ca2+ ions. (wikipedia.org)
  • It consists of 5 cadherin repeats (EC1 ~ EC5) in the extracellular domain, one transmembrane domain, and an intracellular domain that binds p120-catenin and beta-catenin . (wikidoc.org)
  • In addition to containing 34 tandem cadherin-type repeats, the gene product has two epidermal growth factor (EGF)-like repeats and one laminin G domain. (nih.gov)
  • Here, we show that coordinated activity of a type I cadherin (N-cadherin) and type II cadherins (Cadherin-6, -9, and -10) is required in both MNs and Dbx1-derived neurons to generate robust respiratory motor output. (elifesciences.org)
  • The overarching hypothesis is that cadherin adhesion molecules specify the code that enables the premotor brainstem breathing circuits to innervate the phrenic motor neurons that control the primary breathing muscle, the diaphragm. (elifesciences.org)
  • Newborn mice in which phrenic motor neurons lacked a specific combination of cadherins experienced respiratory failure, showing that these proteins were needed for breathing circuits to develop normally. (elifesciences.org)
  • Electrical activity recorded from these cells showed that phrenic motor neurons lacking cadherins could not receive the signals required to activate the breathing muscles. (elifesciences.org)
  • It appears green because these neurons express cadherin-10. (nih.gov)
  • In the present study, we examine the spatial and functional relationship of cadherin and NL isoforms at glutamatergic and GABAergic synapses in cultured hippocampal neurons. (ubc.ca)
  • While the functional roles of the cadherin-catenin cell adhesion complex have been extensively investigated in epithelial cells, it is now clear that components of the complex are well expressed in central neurons at different stages during development. (nebraska.edu)
  • 4,5 Recent exciting studies have shed some light on the functional roles of cadherins and catenins in central neurons. (nebraska.edu)
  • While the roles of cadherins and catenins have been examined in several different types of neurons, the focus of this review is their role in mammalian central neurons, particularly those of the cortex and hippocampus. (nebraska.edu)
  • Specifically, we show that N-cadherin acts upstream of NL1 to promote synapse formation and that NL1 is a limiting factor in this pathway. (ubc.ca)
  • We also show that N-cadherin is important for endothelial cell proliferation and motility. (rupress.org)
  • Type I cadherin cell-adhesion proteins are similar in sequence and structure and yet are different enough to mediate highly specific cell-cell recognition phenomena. (rcsb.org)
  • Here we use a combination of X-ray crystallography, analytical ultracentrifugation, surface plasmon resonance and double electron-electron resonance (DEER) electron paramagnetic resonance spectroscopy to identify the molecular determinants of type I cadherin dimerization affinities. (rcsb.org)
  • There are multiple classes of cadherin molecules, each designated with a prefix for tissues with which it associates. (wikipedia.org)
  • Desmosomal cadherins maintain the function of desmosomes that is to overturn the mechanical stress of the tissues. (wikipedia.org)
  • In this regard E-Cadherin (E-cad) is a 120 kDa polypeptide present in all epithelial tissues and it is the prime mediator of cell-cell interactions. (nih.gov)
  • N-cadherin is involved in organogenesis and maintenance of organ architecture by contributing to the sorting of heterogeneous cell types and in the cell adhesion needed to form tissues. (biolegend.com)
  • N-cadherin is expressed by stem cells, myeloblasts, endothelial cells, and fibroblasts, and also is expressed in neural and muscle tissues and some types of carcinoma cells. (biolegend.com)
  • For comparison, we studied the expression of N-cadherin and found that the expressions of these two cadherins were differential, and complementary in some tissues. (duke.edu)
  • In adult tissues, E-cadherin is expressed in epithelial tissues, where it is constantly regenerated with a 5-hour half-life on the cell surface. (wikidoc.org)
  • The cadherins are glycosylated transmembrane proteins that form cell adhesion complexes in various tissues. (nebraska.edu)
  • In non-epithelial tissues, the role of cadherins in the development of cancer is still debated. (pasteur.fr)
  • In this study, we demonstrated that miR-200a and E-cadherin were significantly upregulated in EOC compared to benign epithelial ovarian cysts and normal ovarian tissues. (current-pharmaceutical-design.com)
  • Cadherins are a class of type-1 transmembrane proteins, and they depend on calcium (Ca2+) ions to function, hence their name. (wikipedia.org)
  • The adaptor proteins that associate with desmosomal cadherins are plakoglobin (related to β {\displaystyle \beta } -catenin), plakophilins (p120 catenin subfamily), and desmoplakins. (wikipedia.org)
  • Cadherins are synthesized as polypeptides and undergo many post-translational modifications to become the proteins which mediate cell-cell adhesion and recognition. (wikipedia.org)
  • Affected individuals make antibodiesagainst one of their own desmosomal cadherin proteins. (ostatic.com)
  • The transmembrane adhesion proteins in these cell-matrixjunctions are integrins a large family of proteins distinct from the cadherins.Focal adhesions enable cells to get a hold on the extracellular matrix through integrins that link intracellularly to actin filaments. (ostatic.com)
  • To do so, the team focused on cadherins, a group of proteins which allow cells to attach to one another. (elifesciences.org)
  • Cadherins are calcium-dependent transmembrane proteins, which bind to one another in a homophilic manner. (rndsystems.com)
  • Biological Function Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). (qedbio.com)
  • She and her team study salamanders and chickens to determine how biological "glue" proteins, called cadherins, help to create neural crest cells, a critical cell type that arises very early in development [1]. (nih.gov)
  • The red lines are the actin filaments that give each endothelial cell its shape, while the purple are proteins called cadherins. (nih.gov)
  • Principal interactions of structural proteins at cadherin-based adherens junction. (wikidoc.org)
  • Cadherins are a class of type-1 transmembrane proteins . (wikidoc.org)
  • Cadherins are glycosylated transmembrane proteins that were initially identified as Ca 2+ -dependent cell adhesion molecules. (nebraska.edu)
  • This is an extremely thorough investigation of the role of cadherins in generating a functional motor circuit. (elifesciences.org)
  • Accompanying this review is a series of excellent reviews targeting the roles of cadherins and protocadherins in other aspects of neural development. (nebraska.edu)
  • Cadherins play a role in development, specifically in tissue formation. (rndsystems.com)
  • E-cadherin downregulation decreases the strength of cellular adhesion within a tissue, resulting in an increase in cellular motility. (qedbio.com)
  • There are multiple classes of cadherin molecule, each designated with a one-letter prefix (generally noting the type of tissue with which it is associated). (wikidoc.org)
  • Q-PCR revealed elevated levels of VE-cadherin and PECAM-1 in tumour samples compared with background tissue and in patients with a poor prognosis, as determined by the Nottingham Prognostic Index. (cardiff.ac.uk)
  • Human cadherin-11 ELISA kit is designed for determining in vitro quantitative amounts of cadherin-11 (CAD-11, CDH11) in human plasma, serum, other biological fluids and tissue homogenates. (elisakits.co.uk)
  • In the past several years, it has become clear that in addition to providing mechanical adhesion between cells, cadherins play integral roles in tissue morphogenesis and homeostasis. (nebraska.edu)
  • Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. (ecmbio.com)
  • E-cadherin expression was found to be absent in normal ovarian tissue and was frequently expressed in benign epithelial ovarian cysts, with absence or low levels observed in late-stage ovarian cancers. (current-pharmaceutical-design.com)
  • Repeated administration of tunicamycin to mice decreased circulating small EVs without decreasing tissue T- cadherin expression. (bvsalud.org)
  • Cadherins (named for "calcium-dependent adhesion") are cell adhesion molecules important in forming adherens junctions that let cells adhere to each other. (wikipedia.org)
  • Without association with the catenins, the cadherins are non-adhesive. (rndsystems.com)
  • The head domain of vinculin associates to E-cadherin via α-, β - and γ -catenins. (wikidoc.org)
  • The final section is dedicated to discussion of the emerging list of neural disorders linked to cadherins and catenins. (nebraska.edu)
  • Miyatani S, Shimamura K, Hatta M. Neural cadherin: role in selective cell-cell adhesion. (bdbiosciences.com)
  • The components that build an atypical cadherin are flamingo (seven pass transmembrane) and Dcad102F-like cadherins. (wikipedia.org)
  • There are two types of desmosomal cadherins: desmogleins and desmocollins. (wikipedia.org)
  • Prior studies have demonstrated that N-cadherins can promote neuronal growth and axonal regeneration in vitro. (illinois.edu)
  • Two dimensional affinity measurements reveal probability of stable bond formation during homophilic and/or heterophilic interactions between cadherins via extracellular domains. (illinois.edu)
  • Cadherins cluster to form foci of homophilic binding units. (ecmbio.com)
  • Among intercellular junctions, cadherin-based adherens junctions mediate strong physical interactions and transmit information from the cell microenvironment to the cytoplasm. (pasteur.fr)
  • Detects mouse P-Cadherin in direct ELISAs and Western blots. (rndsystems.com)
  • Western blot image of human A431 cells that were probed with rabbit polyclonal anti-E-Cadherin (a.a. 774-786) at 1:250 (lane 1), 1:1000 (lane 2), and 1:4000 (lane 3) or mouse monoclonal anti-E-cadherin (Cytoplasmic) at 1:250 (lane 4) and 1:1000 (lane 5). (ecmbio.com)
  • P-Cadherin is a classical cadherin molecule. (rndsystems.com)
  • For example, an N-cadherin will bind only to another N-cadherin molecule. (wikidoc.org)
  • Aims : Vascular endothelial (VE)-cadherin, also known as cadherin-5 and CD144, is an adhesion molecule uniquely expressed in endothelial cells. (cardiff.ac.uk)
  • We hypothesized that VE-cadherin may be a useful marker for assessing microvessels and angiogenesis in human breast cancer and sought to determine whether a correlation exists between levels of VE-cadherin, angiogenic markers factor VIII and platelet endothelial cell adhesion molecule (PECAM)-1 and patient outcome in breast cancer. (cardiff.ac.uk)
  • Endothelial cells express two classic cadherins, VE-cadherin and N-cadherin. (rupress.org)
  • however, the function of N-cadherin in endothelial cells remains poorly understood. (rupress.org)
  • Contrary to previous studies, we found that N-cadherin localizes to endothelial cell-cell junctions in addition to its well-known diffusive membrane expression. (rupress.org)
  • To investigate the role of N-cadherin in vascular development, N-cadherin was specifically deleted from endothelial cells in mice. (rupress.org)
  • Loss of N-cadherin in endothelial cells results in embryonic lethality at mid-gestation due to severe vascular defects. (rupress.org)
  • The down-regulation of both VE-cadherin and p120ctn was confirmed in cultured endothelial cells using small interfering RNA to knockdown N-cadherin. (rupress.org)
  • Objective To study the value of maternal vascular endothelial cadherin (VE-cadherin) level and anti-A/B IgG titer in the prenatal diagnosis of ABO hemolytic disease. (researchsquare.com)
  • Therefore, the author wondered whether the concentration of markers of vascular endothelial injury in maternal peripheral blood (such as VE-cadherin) would be affected through placenta during intrauterine onset. (researchsquare.com)
  • You need info about Pig Vascular Endothelial-Cadherin Complex (VE-cad) ELISA Kit or any other Gentaur produtct? (gentaurshop.com)
  • N-cadherin mRNA is found at elevated levels in brain and heart and at a much lower level in liver. (bdbiosciences.com)
  • Constitutive P-Cadherin expression is found in the epidermis, mesothelium, corneal epithelium, and uterine decidua. (rndsystems.com)
  • When compared with invasive ductal carcinoma, E-cadherin expression is markedly reduced or absent in the great majority of invasive lobular carcinomas when studied by immunohistochemistry. (qedbio.com)
  • In addition, functional compensation assays demonstrate that NL1 expression can fully rescue synapse loss that is due to knockdown of N-cadherin expression. (ubc.ca)
  • Furthermore, N-cadherin expression can partially rescue synapse loss that is due to knockdown of NL1 expression. (ubc.ca)
  • These findings provide a novel paradigm by which N-cadherin regulates angiogenesis, in part, by controlling VE-cadherin expression at the cell membrane. (rupress.org)
  • In this study, we genetically manipulate N-cadherin expression in vivo and in vitro to examine its function in ECs. (rupress.org)
  • DPEP1 inhibited the leukotriene D4 signaling pathway and increased the expression of E-cadherin. (oncotarget.com)
  • TGF-β treatment decreased E-cadherin expression and promoted cell invasion in DPEP1-expressing colon cancer cell lines, whereas it did not affect these parameters in DPEP1-depleted cell lines. (oncotarget.com)
  • Both VE-cadherin and PECAM-1 had significantly reduced expression in lobular compared with ductal carcinomas: there was no difference with factor VIII. (cardiff.ac.uk)
  • The expression of ERK-1/2, Slug and E-cadherin was measured by Western blot respectively. (biomedcentral.com)
  • The expression of cadherin-11 in osteoblastic cell lines and its ability to upregulate during differentiation has led to the indication of a specific function in bone maintenance and development. (elisakits.co.uk)
  • Re-expression of N-cadherin in glioma cells restores cell polarity and limits glioma cell migration, providing a potential therapeutic tool for diffuse glioma. (pasteur.fr)
  • The biphasic expression pattern suggested that miR-200a levels may serve as novel biomarkers for the early detection of EOC, and miR-200a and E-cadherin are candidate targets for the development of new treatment modalities against ovarian cancer. (current-pharmaceutical-design.com)
  • 2001). "Germline E-cadherin gene mutations: is prophylactic total gastrectomy indicated? (wikidoc.org)
  • In the following chapter, I describe the experimental approach for determining the binding affinities of N-cadherin fragments and compared the 2D binding affinity results with that of the full length wild type N-cadherin expressed on MSCs. (illinois.edu)
  • However, there is a lower binding affinity between E-cadherin and HAVDI than that between N-cadherin and HAVDI. (illinois.edu)
  • Cadherins are a family of Ca2+-dependent intercellular adhesion molecules that play a central role in controlling morphogenetic movements during development. (bdbiosciences.com)
  • The minimum detection sensitivity level of CDH-11 (cadherin-11, CAD11) using current CDH-11 ELISA kit was 0.094 ng/ml. (elisakits.co.uk)
  • Additional reported applications (for the relevant formats) include: immunofluorescence 1,3,6 , motility inhibition of N-cadherin-expressing cells 2 , and Western blot 2,4 . (biolegend.com)
  • and P-cadherins are found in the placenta. (wikidoc.org)
  • Type 2 cadherins in the human endometrium and placenta: their putative roles in human implantation and placentation. (elisakits.co.uk)
  • E-cadherin synthetic peptide corresponding to amino acids in the C-terminal region in human E-cadherin. (ecmbio.com)
  • The cadherin family is essential in maintaining cell-cell contact and regulating cytoskeletal complexes. (wikipedia.org)
  • Wahl, JK III et al.N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane. (neobiotechnologies.com)
  • Marquage par immunofluorescence d'astrocytes tumoraux ou astrocytomes (lignée cellulaire humaine U373), montrant en rouge, APC et en vert, la tubuline des microtubules. (pasteur.fr)
  • The use of e-cadherin immunofluorescence in pulmonary toxicologic pathology studies. (cdc.gov)
  • however, the interrelationship and functional contribution of the individual cadherins in cell adhesion and signaling is poorly understood. (rupress.org)