Catenins: A family of cytoskeletal proteins that play essential roles in CELL ADHESION at ADHERENS JUNCTIONS by linking CADHERINS to the ACTIN FILAMENTS of the CYTOSKELETON.alpha Catenin: A catenin that binds F-ACTIN and links the CYTOSKELETON with BETA CATENIN and GAMMA CATENIN.gamma Catenin: A multi-functional catenin that is highly homologous to BETA CATENIN. Gamma catenin binds CADHERINS and helps link their cytoplasmic tails to ACTIN in the CYTOSKELETON via ALPHA CATENIN. It is also found in DESMOSOMES where it mediates the link between DESMOSOMAL CADHERINS and DESMOPLAKIN.Desmoplakins: Desmoplakins are cytoskeletal linker proteins that anchor INTERMEDIATE FILAMENTS to the PLASMA MEMBRANE at DESMOSOMES.Cadherins: Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.beta Catenin: A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.Cytoskeletal Proteins: Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.Adherens Junctions: Anchoring points where the CYTOSKELETON of neighboring cells are connected to each other. They are composed of specialized areas of the plasma membrane where bundles of the ACTIN CYTOSKELETON attach to the membrane through the transmembrane linkers, CADHERINS, which in turn attach through their extracellular domains to cadherins in the neighboring cell membranes. In sheets of cells, they form into adhesion belts (zonula adherens) that go all the way around a cell.Trans-Activators: Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.Cell Adhesion Molecules: Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.Intercellular Junctions: Direct contact of a cell with a neighboring cell. Most such junctions are too small to be resolved by light microscopy, but they can be visualized by conventional or freeze-fracture electron microscopy, both of which show that the interacting CELL MEMBRANE and often the underlying CYTOPLASM and the intervening EXTRACELLULAR SPACE are highly specialized in these regions. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p792)Cell Adhesion: Adherence of cells to surfaces or to other cells.Armadillo Domain Proteins: A family of proteins that contain several 42-amino acid repeat domains and are homologous to the Drosophila armadillo protein. They bind to other proteins through their armadillo domains and play a variety of roles in the CELL including SIGNAL TRANSDUCTION, regulation of DESMOSOME assembly, and CELL ADHESION.Desmogleins: A group of desmosomal cadherins with cytoplasmic tails that resemble those of classical CADHERINS.PhosphoproteinsCell Aggregation: The phenomenon by which dissociated cells intermixed in vitro tend to group themselves with cells of their own type.Precipitin Tests: Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.L Cells (Cell Line): A cultured line of C3H mouse FIBROBLASTS that do not adhere to one another and do not express CADHERINS.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.Actins: Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.Xenopus Proteins: Proteins obtained from various species of Xenopus. Included here are proteins from the African clawed frog (XENOPUS LAEVIS). Many of these proteins have been the subject of scientific investigations in the area of MORPHOGENESIS and development.Epithelial Cells: Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Dogs: The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)Cell Line: Established cell cultures that have the potential to propagate indefinitely.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Cell Communication: Any of several ways in which living cells of an organism communicate with one another, whether by direct contact between cells or by means of chemical signals carried by neurotransmitter substances, hormones, and cyclic AMP.Fluorescent Antibody Technique: Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Tumor Cells, Cultured: Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Antigens, CD: Differentiation antigens residing on mammalian leukocytes. CD stands for cluster of differentiation, which refers to groups of monoclonal antibodies that show similar reactivity with certain subpopulations of antigens of a particular lineage or differentiation stage. The subpopulations of antigens are also known by the same CD designation.Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.

Misexpression of the catenin p120(ctn)1A perturbs Xenopus gastrulation but does not elicit Wnt-directed axis specification. (1/407)

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 catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor. (2/407)

p120(ctn) is an Armadillo repeat domain protein with structural similarity to the cell adhesion cofactors beta-catenin and plakoglobin. All three proteins interact directly with the cytoplasmic domain of the transmembrane cell adhesion molecule E-cadherin; beta-catenin and plakoglobin bind a carboxy-terminal region in a mutually exclusive manner, while p120 binds the juxtamembrane region. Unlike beta-catenin and plakoglobin, p120 does not interact with alpha-catenin, the tumor suppressor adenomatous polyposis coli (APC), or the transcription factor Lef-1, suggesting that it has unique binding partners and plays a distinct role in the cadherin-catenin complex. Using p120 as bait, we conducted a yeast two-hybrid screen and identified a novel transcription factor which we named Kaiso. Kaiso's deduced amino acid sequence revealed an amino-terminal BTB/POZ protein-protein interaction domain and three carboxy-terminal zinc fingers of the C2H2 DNA-binding type. Kaiso thus belongs to a rapidly growing family of POZ-ZF transcription factors that include the Drosophila developmental regulators Tramtrak and Bric a brac, and the human oncoproteins BCL-6 and PLZF, which are causally linked to non-Hodgkins' lymphoma and acute promyelocytic leukemia, respectively. Monoclonal antibodies to Kaiso were generated and used to immunolocalize the protein and confirm the specificity of the p120-Kaiso interaction in mammalian cells. Kaiso specifically coprecipitated with a variety of p120-specific monoclonal antibodies but not with antibodies to alpha- or beta-catenin, E-cadherin, or APC. Like other POZ-ZF proteins, Kaiso localized to the nucleus and was associated with specific nuclear dots. Yeast two-hybrid interaction assays mapped the binding domains to Arm repeats 1 to 7 of p120 and the carboxy-terminal 200 amino acids of Kaiso. In addition, Kaiso homodimerized via its POZ domain but it did not heterodimerize with BCL-6, which heterodimerizes with PLZF. The involvement of POZ-ZF proteins in development and cancer makes Kaiso an interesting candidate for a downstream effector of cadherin and/or p120 signaling.  (+info)

p120(ctn) acts as an inhibitory regulator of cadherin function in colon carcinoma cells. (3/407)

p120(ctn) binds to the cytoplasmic domain of cadherins but its role is poorly understood. Colo 205 cells grow as dispersed cells despite their normal expression of E-cadherin and catenins. However, in these cells we can induce typical E-cadherin-dependent aggregation by treatment with staurosporine or trypsin. These treatments concomitantly induce an electrophoretic mobility shift of p120(ctn) to a faster position. To investigate whether p120(ctn) plays a role in this cadherin reactivation process, we transfected Colo 205 cells with a series of p120(ctn) deletion constructs. Notably, expression of NH2-terminally deleted p120(ctn) induced aggregation. Similar effects were observed when these constructs were introduced into HT-29 cells. When a mutant N-cadherin lacking the p120(ctn)-binding site was introduced into Colo 205 cells, this molecule also induced cell aggregation, indicating that cadherins can function normally if they do not bind to p120(ctn). These findings suggest that in Colo 205 cells, a signaling mechanism exists to modify a biochemical state of p120(ctn) and the modified p120(ctn) blocks the cadherin system. The NH2 terminus-deleted p120(ctn) appears to compete with the endogenous p120(ctn) to abolish the adhesion-blocking action.  (+info)

Functional characterization of multiple transactivating elements in beta-catenin, some of which interact with the TATA-binding protein in vitro. (4/407)

beta-Catenin, a member of the family of Armadillo repeat proteins, plays a dual role in cadherin-mediated cell adhesion and in signaling by Wnt growth factors. Upon Wnt stimulation beta-catenin undergoes nuclear translocation and serves as transcriptional coactivator of T cell factor DNA-binding proteins. Previously the transactivation potential of different portions of beta-catenin has been demonstrated, but the precise location of transactivating elements has not been established. Also, the mechanism of transactivation by beta-catenin and the molecular basis for functional differences between beta-catenin and the closely related proteins Armadillo and Plakoglobin are poorly understood. Here we have used a yeast system for the detailed characterization of the transactivation properties of beta-catenin. We show that its transactivation domains possess a modular structure, consist of multiple subelements that cover broad regions at its N and C termini, and extend considerably into the Armadillo repeat region. Compared with beta-catenin the N termini of Plakoglobin and Armadillo have different transactivation capacities that may explain their distinct signaling properties. Furthermore, transactivating elements of beta-catenin interact specifically and directly with the TATA-binding protein in vitro providing further evidence that a major function of beta-catenin during Wnt signaling is to recruit the basal transcription machinery to promoter regions of Wnt target genes.  (+info)

Nuclear localization of the p120(ctn) Armadillo-like catenin is counteracted by a nuclear export signal and by E-cadherin expression. (5/407)

The Armadillo protein p120(ctn) associates with the cytoplasmic domain of cadherins and accumulates at cell-cell junctions. Particular Armadillo proteins such as beta-catenin and plakophilins show a partly nuclear location, suggesting gene-regulatory activities. For different human E-cadherin-negative carcinoma cancer cell lines we found expression of endogenous p120(ctn) in the nucleus. Expression of E-cadherin directed p120(ctn) out of the nucleus. Previously, we reported that the human p120(ctn) gene might encode up to 32 protein isoforms as products of alternative splicing. Overexpression of p120(ctn) isoforms B in various cell lines resulted in cytoplasmic immunopositivity but never in nuclear staining. In contrast, upon expression of p120(ctn) cDNAs lacking exon B, the isoforms were detectable within both nuclei and cytoplasm. A putative nuclear export signal (NES) with a characteristic leucine-rich motif is encoded by exon B. This sequence element was shown to be required for nuclear export and to function autonomously when fused to a carrier protein and microinjected into cell nuclei. Moreover, the NES function of endogenously or exogenously expressed p120(ctn) isoforms B was sensitive to the nuclear export inhibitor leptomycin B. Expression of exogenous E-cadherin down-regulated nuclear p120(ctn) whereas activation of protein kinase C increased the level of nuclear p120(ctn). These results reveal molecular mechanisms controlling the subcellular distribution of p120(ctn).  (+info)

p120(ctn) binds to the membrane-proximal region of the E-cadherin cytoplasmic domain and is involved in modulation of adhesion activity. (6/407)

Cadherins are transmembrane glycoproteins involved in Ca(2+)-dependent cell-cell adhesion. Previously, we showed that the conserved membrane-proximal region of the E-cadherin cytoplasmic domain negatively regulates adhesion activity. In this report, we provide several lines of evidence that p120(ctn) is involved in this negative regulation. p120(ctn) binds to the membrane-proximal region of the nonfunctional carboxyl-terminally deleted E-cadherin protein. An additional internal deletion in this region prevented the association with p120(ctn) and activated the protein, as seen in an aggregation assay. Furthermore, the nonfunctional E-cadherin can be activated through coexpression of p120(ctn) proteins with amino-terminal deletions, which eliminate several potential serine/threonine phosphorylation sites but do not affect the ability to bind to cadherins. Finally, we show that staurosporine, a kinase inhibitor, induces an increased electrophoretic mobility of p120(ctn) bound to E-cadherin polypeptides, activates the nonfunctional E-cadherin protein, and converts the wild-type E-cadherin and an E-cadherin-alpha-catenin chimeric protein from a cytochalasin D-sensitive to a cytochalasin D-insensitive state. Together, these results indicate that p120(ctn) is a modulator of E-cadherin-mediated cell adhesion.  (+info)

N-Cadherin expression in human prostate carcinoma cell lines. An epithelial-mesenchymal transformation mediating adhesion withStromal cells. (7/407)

In human prostate adenocarcinoma, an association between loss of E-cadherin, increased Gleason score, and extracapsular dissemination has been observed. Further characterization of the E-cadherin/catenin phenotype of human prostate carcinoma cell lines showed loss of E-cadherin and expression of N-cadherin in poorly differentiated prostate carcinoma cell lines (PC-3N derived from PC-3, PC-3, and JCA1). We showed that N-cadherin is concentrated at sites of cell-cell contact in PC-3N cellular extensions. N-cadherin was also expressed in prostate stromal fibroblasts both in vitro and in prostate tissue. Co-cultures of prostate stromal fibroblasts and PC-3N cells showed the immunolocalization of N-cadherin in intercellular contacts. In addition, the isoform expression of the cadherin binding protein p120(ctn) differed in relation to the expression of E- versus N-cadherin by the prostate carcinoma cell lines. The p100 isoform was more highly expressed in E-cadherin-positive carcinoma cell lines, whereas p120 was predominantly expressed only in N-cadherin-positive prostate carcinoma cell lines and prostate stromal fibroblasts. The N-cadherin-positive carcinoma cell line, PC-3N, displayed aggressive invasion into the surface of the diaphragm muscle after intraperitoneal injection of SCID mice. The gain of N-cadherin and loss of E-cadherin by invasive prostate carcinoma cell lines suggests a progression from an epithelial to a mesenchymal phenotype, which may allow for their interaction with surrounding stromal fibroblasts and facilitate metastasis.  (+info)

Epithelial mesenchymal transition by c-Fos estrogen receptor activation involves nuclear translocation of beta-catenin and upregulation of beta-catenin/lymphoid enhancer binding factor-1 transcriptional activity. (8/407)

Mouse mammary epithelial cells expressing a fusion protein of c-Fos and the estrogen receptor (FosER) formed highly polarized epithelial cell sheets in the absence of estradiol. Beta-catenin and p120(ctn) were exclusively located at the lateral plasma membrane in a tight complex with the adherens junction protein, E-cadherin. Upon activation of FosER by estradiol addition, cells lost epithelial polarity within two days, giving rise to a uniform distribution of junctional proteins along the entire plasma membrane. Most of the beta-catenin and p120(ctn) remained in a complex with E-cadherin at the membrane, but a minor fraction of uncomplexed cytoplasmic beta-catenin increased significantly. The epithelial-mesenchymal cell conversion induced by prolonged estradiol treatment was accompanied by a complete loss of E-cadherin expression, a 70% reduction in beta-catenin protein level, and a change in the expression pattern of p120(ctn) isoforms. In these mesenchymal cells, beta-catenin and p120(ctn) were localized in the cytoplasm and in defined intranuclear structures. Furthermore, beta-catenin colocalized with transcription factor LEF-1 in the nucleus, and coprecipitated with LEF-1-related proteins from cell extracts. Accordingly, beta-catenin- dependent reporter activity was upregulated in mesenchymal cells and could be reduced by transient expression of exogenous E-cadherin. Thus, epithelial mesenchymal conversion in FosER cells may involve beta-catenin signaling.  (+info)

*Catenin

α-catenin β-catenin δ-catenin γ-catenin All but α-catenin contain armadillo repeats. Several types of catenins work with N- ... The first two catenins that were identified became known as α-catenin and β-catenin. A-catenin can bind to β-catenin and can ... B-catenin binds the cytoplasmic domain of some cadherins. Additional catenins such as γ-catenin and δ-catenin have been ... Most studies investigating catenin actions focus on α-catenin and β-catenin. β-catenin is particularly interesting as it plays ...

*Beta-catenin

This is possible because α-catenin and cadherins bind at distinct sites to β-catenin. The β-catenin - α-catenin complex can ... Catenin beta-1, also known as β-catenin, is a protein that in humans is encoded by the CTNNB1 gene. β-catenin is a dual ... On the other hand, BCL9 and BCL9L must compete with α-catenin to access β-catenin molecules. The cellular level of beta-catenin ... It is a member of the catenin protein family and homologous to γ-catenin, also known as plakoglobin. Beta-catenin is widely ...

*Delta catenin

Like beta-catenin and gamma-catenin, delta-catenins seem to interact with presenilins. These catenin-presenilin interaction ... Delta-1-catenin and Delta-2-catenin are members of a subfamily of proteins with ten Armadillo-repeats. Delta-2-catenin is ... While beta-catenin acts as a transcription reglatory protein in the Wnt/TCF pathway, delta-catenin 1 has been implicated as a ... catenin by DHHC5 mediates activity-induced synapse plasticity". Nature Neuroscience. doi:10.1038/nn.3657. Catenin. ...

*Alpha catenin

... alpha-2-catenin (also called alpha-N-catenin) alpha-3-catenin (also called alpha-T-catenin) Catenin alpha Catenin at the US ... There are three human alpha-catenin genes: alpha-1-catenin (also called alpha-E-catenin) ... beta-catenin and alpha-catenin has not been isolated. It has been suggested that alpha-catenin does not bind with high affinity ... It has been observed that when alpha-catenin is not in a molecular complex with beta-catenin, it dimerizes and functions to ...

*Catenin alpha-1

... αE-catenin has no homology to established actin-binding proteins. The N-terminus of αE-catenin binds β-catenin or γ-catenin/ ... αE-catenin, also known as Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene. αE-catenin is highly ... αE-catenin has been shown to interact with: APC, Beta-catenin, CDH1, CDH2, CDH3 Plakoglobin, and VE-cadherin. Alpha catenin ... Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ...

*Dishevelled binding antagonist of beta catenin 2

... is a protein that in humans is encoded by the DACT2 gene. GRCh38: Ensembl ... Dishevelled binding antagonist of beta catenin 2". Retrieved 2017-09-10. Koga Y, Yao T, Hirahashi M, Kumashiro Y, Ohji Y, ... "DACT2 is a functional tumor suppressor through inhibiting Wnt/β-catenin pathway and associated with poor survival in colon ... "Flat adenoma-carcinoma sequence with high-malignancy potential as demonstrated by CD10 and beta-catenin expression: a different ...

*Cadherin-catenin complex in learning and memory

... α-catenins, β-catenins, and p120ctn family catenins. β-catenins and p120ctns bind cadherin's intracellular domain at the distal ... will associate with the cadherin-catenin complex via β-catenins. In homodimeric form, α-catenins do not bind β- catenins, but ... β-catenin localizes reserve pool vesicles (RPVs) at presynaptic sites. The deletion of β-catenin in vivo results in a decrease ... Catenins also bind many scaffolding proteins, receptors, kinases and phosphatases. For example, the cadherin-α-catenin complex ...

*Endometrial cancer

CTNNB1 (beta-catenin; a transcription gene) mutations are found in 14-44% of endometrial cancers and may indicate a good ... Beta-catenin mutations are commonly found in endometrial cancers with squamous cells. FGFR2 mutations are found in ... The CTNNB1 (beta-catenin) gene is most commonly mutated in the squamous subtype of endometrioid adenocarcinoma. Serous ...

*CTNNBIP1

"Axin-independent phosphorylation of APC controls beta-catenin signaling via cytoplasmic retention of beta-catenin". Biochem. ... Beta-catenin-interacting protein 1 is a protein that is encoded in humans by the CTNNBIP1 gene. The protein encoded by this ... Reichel O, Mayr D, Durst F, Berghaus A (2008). "E-cadherin but not beta-catenin expression is decreased in laryngeal biopsies ... Kohler EM, Chandra SH, Behrens J, Schneikert J (2009). "Beta-catenin degradation mediated by the CID domain of APC provides a ...

*Mouse model of colorectal and intestinal cancer

APC was found to associate with catenins. Today we know that the beta-catenin protein (part of the Wnt signaling pathway) is ... A mouse model with deregulation of beta-catenin levels was created. The conditional stabilizing mutation in the beta-catenin ... there was substantial nuclear localization of beta-catenin as well as increased cytoplasmic beta-catenin. However, in mice fed ... Furthermore, when evaluated for ERCC1, beclin-1, and beta-catenin in the stem cell region of crypts, the colonic tissues of ...

*Vinculin family

Catenins are proteins that associate with the cytoplasmic domain of a variety of cadherins. The association of catenins to ... Three different types of catenins seem to exist: alpha, beta, and gamma. Alpha-catenins are proteins of about 100 kDa which are ... In terms of their structure the most significant differences are the absence, in alpha-catenin, of the repeated domain and of ... Vinculin InterPro: IPR000633 Alpha-catenin InterPro: IPR001033 CTNNA1; CTNNA2; CTNNA3; CTNNAL1; VCL; Otto JJ (1990). "Vinculin ...

*TBX2

Wnt/beta-catenin Pathway. The role of Tbx2 in Wnt signaling has yet to be confirmed; however, up-regulation of Tbx2 in the beta ... catenin signaling pathway leads to loss of the adhesion molecule E-cadherin. This returns cells to a mesenchymal state, and ...

*FZD6

beta-catenin signaling cascade". The Journal of Biological Chemistry. 279 (15): 14879-88. doi:10.1074/jbc.M306421200. PMID ... "Wnt-4 activates the canonical beta-catenin-mediated Wnt pathway and binds Frizzled-6 CRD: functional implications of Wnt/beta- ... catenin activity in kidney epithelial cells". Experimental Cell Research. 298 (2): 369-87. doi:10.1016/j.yexcr.2004.04.036. ...

*PTPRM

... such as p120-catenin, beta-catenin and alpha-catenin. Catenins, in turn, bind to the actin cytoskeleton. Binding of these ... Although p120 catenin is a potential substrate of PTPmu, others have suggested that the interaction between PTPmu and catenins ... In addition to catenins and cadherins, PTPmu dephosphorylates PIPKIγ90 and nectin-3 (PVRL3) to stabilize E-cadherin-based ... IQGAP1 is a scaffold for Rho family of GTPases, E-cadherin, beta-catenin and other proteins. IQGAP1 binding to Rho GTPases is ...

*CELSR2

The flamingo subfamily consists of nonclassic-type cadherins; a subpopulation that does not interact with catenins. The ...

*Adenomatous polyposis coli

The researchers hypothesized that APC's many β-catenin binding site increase the protein's efficiency at destroying β-catenin, ... interacts with beta-catenin, GSK-3beta and APC and reduces the beta-catenin level". Genes to Cells. 3 (6): 395-403. doi:10.1046 ... GSK-3β is able to phosphorylate β-catenin a second time. This targets β-catenin for ubiquitination and degradation by cellular ... "Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin ...

*Bert Vogelstein

They also showed how APC functions - through binding to beta-catenin and stimulating its degradation. Vogelstein and Kinzler ... Su LK, Vogelstein B, Kinzler KW (December 1993). "Association of the APC tumor suppressor protein with catenins". Science. 262 ...

*Plakoglobin

"Identification of the domain of alpha-catenin involved in its association with beta-catenin and plakoglobin (gamma-catenin)". ... Plakoglobin is a member of the catenin protein family and homologous to β-catenin. Plakoglobin is a cytoplasmic component of ... Hearts also exhibited increases in β-catenin signaling. Further investigations on the role of β-catenin and plakoglobin in the ... "A mutation in alpha-catenin disrupts adhesion in clone A cells without perturbing its actin and beta-catenin binding activity ...

*WNT5A

Clevers H, Nusse R (June 2012). "Wnt/β-catenin signaling and disease". Cell. 149 (6): 1192-205. doi:10.1016/j.cell.2012.05.012 ... Elevated levels of beta-catenin in both primary and metastases of malignant melanoma have been correlated to improved survival ... Dihlmann, Susanne; von Knebel Doeberitz, Magnus (2005-02-10). "Wnt/β-catenin-pathway as a molecular target for future anti- ... Anagnostou SH, Shepherd PR (December 2008). "Glucose induces an autocrine activation of the Wnt/beta-catenin pathway in ...

*CTNND1

Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ... Delta catenin Catenin CTNND2 GRCh38: Ensembl release 89: ENSG00000198561 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... Catenin delta-1 is a protein that in humans is encoded by the CTNND1 gene. This gene encodes a member of the Armadillo protein ... "Entrez Gene: CTNND1 catenin (cadherin-associated protein), delta 1". Hazan RB, Norton L (April 1998). "The epidermal growth ...

*CDH1 (gene)

Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ... Beta-catenin can also bind to alpha-catenin. Alpha-catenin participates in regulation of actin-containing cytoskeletal ... Loss of E-cadherin expression results in releasing β-catenin into the cytoplasm. Liberated β-catenin molecules may migrate into ... "A truncated beta-catenin disrupts the interaction between E-cadherin and alpha-catenin: a cause of loss of intercellular ...

*PITX2

"Identification of a Wnt/Dvl/beta-Catenin --> Pitx2 pathway mediating cell-type-specific proliferation during development". Cell ...

*CTNNBL1

Beta-catenin-like protein 1 is a protein that in humans is encoded by the CTNNBL1 gene. The protein encoded by this gene ... "Entrez Gene: CTNNBL1 catenin, beta like 1". Human CTNNBL1 genome location and CTNNBL1 gene details page in the UCSC Genome ... In addition, the encoded protein contains Armadillo/beta-catenin-like repeats, which have been implicated in protein-protein ...

*Androgen receptor

Yang F, Li X, Sharma M, Sasaki CY, Longo DL, Lim B, Sun Z (March 2002). "Linking beta-catenin to androgen-signaling pathway". ... Masiello D, Chen SY, Xu Y, Verhoeven MC, Choi E, Hollenberg AN, Balk SP (October 2004). "Recruitment of beta-catenin by wild- ... Amir AL, Barua M, McKnight NC, Cheng S, Yuan X, Balk SP (August 2003). "A direct beta-catenin-independent interaction between ... Beta-catenin, BRCA1, C-jun, Calmodulin 1, Caveolin 1, CDK9, COX5B, CREB-binding protein, Cyclin D1, Cyclin-dependent kinase 7, ...

*HDAC7

One study showed that HDAC7 suppresses proliferation and β-catenin activity in chondrocytes. This was shown by knocking out ... Overall, this study demonstrated that HDAC7 once again interacts with β-catenin to keep endothelial cells in a low ... Another study supported the conclusion that HDAC7 and β-catenin associate together by demonstrating that HDAC7 controls ... They found that overexpression of HDAC7 prevented nuclear translocation of β-catenin which then coincided with downregulation ...
Ctnnd1 - Ctnnd1 (Myc-DDK-tagged) - Mouse catenin (cadherin associated protein), delta 1 (Ctnnd1), transcript variant 2 available for purchase from OriGene - Your Gene Company.
Background: Approximately one third of the hereditary diffuse gastric cancer (HDGC) families carry germline mutations in the E-cadherin gene (CDH1). Risk prediction in members of families with this rare but deadly cancer could be improved by the identification of additional HDGC genes in non-CDH1 families.. Methods: Affected individuals from 22 CDH1 mutation-negative families were screened for germline mutations in four catenin genes: CTNNA1, CTNNB1, JUP, and CTNND1. Catenins interact closely with E-cadherin molecules in cells, and are therefore logical candidate genes for mutation screening in HDGC families.. Results: No nonsynonymous variants were seen in CTNNA1, CTNNB1, or CTNND1; only JUP contained nonsynonymous variants, of which only two rare variants were predicted to be deleterious.. Conclusion: Catenin genes are not commonly mutated in non-CDH1 HDGC families.. Impact: Germline mutations in CTNNA1, CTNNB1, JUP, or CTNND1 are unlikely to play a major role in HDGC. Cancer Epidemiol ...
BACKGROUND: Approximately one third of the hereditary diffuse gastric cancer (HDGC) families carry germline mutations in the E-cadherin gene (CDH1). Risk prediction in members of families with this rare but deadly cancer could be improved by the identification of additional HDGC genes in non-CDH1 families.METHODS: Affected individuals from 22 CDH1 mutation-negative families were screened for germline mutations in four catenin genes: CTNNA1, CTNNB1, JUP, and CTNND1. Catenins interact closely with E-cadherin molecules in cells, and are therefore logical candidate genes for mutation screening in HDGC families.RESULTS: No nonsynonymous variants were seen in CTNNA1, CTNNB1, or CTNND1; only JUP contained nonsynonymous variants, of which only two rare variants were predicted to be deleterious.CONCLUSION: Catenin genes are not commonly mutated in non-CDH1 HDGC families.Impact: Germline mutations in CTNNA1, CTNNB1, JUP, or CTNND1 are unlikely to play a major role in HDGC. Cancer Epidemiol Biomarkers Prev; 1-3.
Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells. The first two catenins that were identified became known as α-catenin and β-catenin. A-catenin can bind to β-catenin and can also bind actin. B-catenin binds the cytoplasmic domain of some cadherins. Additional catenins such as γ-catenin and δ-catenin have been identified. The name "catenin" was originally selected (catena means chain in Latin) because it was suspected that catenins might link cadherins to the cytoskeleton. α-catenin β-catenin δ-catenin γ-catenin All but α-catenin contain armadillo repeats. Several types of catenins work with N-cadherins to play an important role in learning and memory (For full article, see Cadherin-catenin complex in learning and memory). Cell-cell adhesion complexes are required for simple epithelia in higher organisms to maintain structure, function and polarity. These complexes, which help regulate cell growth in addition to creating and ...
Buy our Recombinant Human delta 1 Catenin protein. Ab114472 is a protein fragment produced in Wheat germ and has been validated in WB, ELISA, SDS-PAGE. Abcam…
Wnt pathway deregulation is a common characteristic of many cancers. But only Colorectal Cancer predominantly harbours mutations in APC, whereas other cancer types (hepatocellular carcinoma, solid pseudopapillary tumours of pancreas) have activating mutations in β-catenin (CTNNB1). We have compared the dynamics and the potency of β-catenin mutations in vivo. Within the murine small intestine (SI), an activating mutation of β-catenin took much longer to achieve a Wnt deregulation and acquire a crypt-progenitor-cell (CPC) phenotype than Apc or Gsk3 loss. Within the colon, a single activating mutation of β-catenin was unable to drive Wnt deregulation or induce the CPC phenotype. This ability of β-catenin mutation to differentially transform the SI versus the colon correlated with significantly higher expression of the β-catenin binding partner E-cadherin. This increased expression is associated with a higher number of E-cadherin:β-catenin complexes at the membrane. Reduction of E-cadherin ...
In metazoan adherens junctions, β-catenin links the cytoplasmic tail of classical cadherins to the F-actin-binding protein α-catenin. Phosphorylation of a Ser/Thr-rich region in the cadherin tail dramatically enhances affinity for β-catenin and promotes cell-cell adhesion in cell culture systems, but its importance has not been demonstrated in vivo. In this paper, we identify a critical phosphorylated serine in the C. elegans cadherin HMR-1 required for strong binding to the β-catenin homolog HMP-2. Ablation of this phosphoserine interaction produces developmental defects that resemble full loss-of-function (Hammerhead and Humpback) phenotypes. Most metazoans possess a single gene for β-catenin, which is also a transcriptional coactivator in Wnt signaling. Nematodes and planaria, however, have a set of paralogous β-catenins; for example, C. elegans HMP-2 functions only in cell-cell adhesion, whereas SYS-1 mediates transcriptional activation through interactions with POP-1/Tcf. Finally, our ...
When we examined solid pseudopapillary tumours of the pancreas, a tumour characterised by β‐catenin mutations within exon 3, these tumours showed a strong reduction in E‐cadherin:β‐catenin complexes. Moreover in HCC, a tumour type which has approximately 20% β‐catenin exon 3 mutations, there was a good correlation between reduction in E‐cadherin and activation of Wnt signalling targets. Thus, it may be that in these cancers, E‐cadherin limits the precise levels of Wnt signalling driven by β‐catenin mutation. Thus, downregulation of E‐cadherin in these tumours may drive tumour progression. It should also be noted that opposing patterns of Wnt signalling and E‐cadherin have been shown in murine liver, with β‐catenin higher in zone 3 of the liver and E‐cadherin in zone 1. Therefore, one might predict that β‐catenin mutations would yield a greater phenotype in hepatocytes from zone 3 of the liver versus zone 1 (Benhamouche et al, 2006). Hence, one could speculate ...
Objective: The aim of this study is to verify if oxidative stress is related to changes in content and pattern of β-catenin protein expression in an experimental model of diversion colitis. Methods: Sixty Wistar rats were submitted to intestinal bypass. The animals were divided into three groups according to the sacrifice to take place in six, 12 and 18 weeks. For each group, five animals only underwent laparotomy (control). The presence of colitis was diagnosed by histological study, and its severity, by inflammation grading scale. Cellular oxidative stress was measured by comet assay. Tissue expression of β-catenin protein was analyzed by the immunohistochemistry and quantification of its tissue content by computerized morphometry. Statistical analysis was performed with the Students t-test, median, Mann-Whitney, ANOVA and Kruskal-Wallis, adopting a significance level of 5% (p ,0.05). Results: Colon segments without fecal stream developed colitis, which worsened with time of exclusion. ...
The KOMP Repository Collection is located at the MMRRC at the University of California, Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...
TGF-β1 has been previously reported to promote tyrosine phosphorylation of β-catenin (Tian and Phillips, 2002), although the specific site of phosphorylation and its functional significance in TGF-β1 signaling has been unknown. Our finding of integrin-dependent tyrosine phosphorylation of Y654-β-catenin is important because phosphorylation of β-catenin at Y654 is known to promote both dissociation of β-catenin from E-cadherin and stabilization of β-catenin from ubiquitination and degradation (Brembeck et al., 2006). Therefore, independently of Wnt signaling, our findings indicate that TGF-β1 can promote a pathway of cross talk with β-catenin by generating stable pY654-β-catenin-Smad complexes. The data indicate that only a fraction of the β-catenin is phosphorylated, and presumably, this reflects, at least in part, the pool internalized with E-cadherin and TGF-βR1 after TGF-β1 stimulation. However, internalization alone does not appear to be sufficient, as α3-null cells, even ...
Aberrant regulation of the Wnt/β-catenin pathway plays important roles in colorectal carcinogenesis, with over 90% of cases of sporadic colon cancer featuring β-catenin accumulation. While ubiquitination-mediated degradation is widely accepted as a major route for β-catenin protein turnover, little is known about the regulation of β-catenin in transcriptional level. …Elf3, a member of the E-twenty-six family of transcription factors, drives β-catenin transactivation and associates with poor survival of colorectal cancer (CRC) patients. … first found recurrent amplification and upregulation of Elf3 in CRC tissues, and further Gene Set Enrichment Analysis identified significant association between Elf3 expression and activity of WNT/β-catenin pathway. Chromatin immunoprecipitation and electrophoretic mobility shift assay consistently revealed that Elf3 binds to and transactivates β-catenin promoter. Ectopic expression of Elf3 induces accumulation of β-catenin in both nucleus and ...
Regulating the cytosolic concentration of the protein β-catenin is an important cell proliferation control mechanism. The cytoplasmic concentration of β-catenin remains low through an interaction with a protein complex consisting of adenomatous polyposis coli (APC), Axin, protein phosphatase 2A, and glycogen synthase kinase 3β (GSK3β). Upon phosphorylation by GSK3β, β-catenin associates with a ubiquitin ligase (E3) complex, resulting in its ubiquitination and proteolysis. Activation of Wnt signaling inactivates GSK3, allowing β-catenin to accumulate in the cytoplasm and eventually to translocate to the nucleus so as to affect gene expression. Two groups report that a phosphorylation-independent mechanism can lead to the destruction of β-catenin. Matsuzawa and Reed show that a mammalian protein called Siah-1 lies at the hub of another pathway that destroys β-catenin in response to DNA damaging agents and the activation of the tumor suppressor protein p53. Siah-1 is known to interact with ...
Clone REA548 recognizes the S879-phosphorylated form of p120 catenin, a prototypic member of the subfamily of armadillo-domain (ARM) proteins. p120 ARM domain displays 22% homology to other ARM-domain proteins such as β-catenin and plakoglobin, which are basically cadherin binding proteins, suggesting the involvement of p120 in binding to cadherin. p120 associates with most classical (type I) and non-classical (type II) cadherins via ARM repeats 1-7 and is localised at the cell junctions, where it constitutes the cadherin complex. Functions of p120 include regulation of stability of cadherins and modulation of activity of rho GTPases in the cytoplasm. Furthermore, lack of p120 catenin in mouse leads to tumor development, suggesting its further role as tumor supressor. Phosphorylation of p120 catenin at multiple sites regulates its various functions and can be phosphorylated by Src and various receptor tyrosine kinases. Additional information: Clone REA548 displays negligible binding to Fc receptors. -
Clone REA548 recognizes the S879-phosphorylated form of p120 catenin, a prototypic member of the subfamily of armadillo-domain (ARM) proteins. p120 ARM domain displays 22% homology to other ARM-domain proteins such as β-catenin and plakoglobin, which are basically cadherin binding proteins, suggesting the involvement of p120 in binding to cadherin. p120 associates with most classical (type I) and non-classical (type II) cadherins via ARM repeats 1-7 and is localised at the cell junctions, where it constitutes the cadherin complex. Functions of p120 include regulation of stability of cadherins and modulation of activity of rho GTPases in the cytoplasm. Furthermore, lack of p120 catenin in mouse leads to tumor development, suggesting its further role as tumor supressor. Phosphorylation of p120 catenin at multiple sites regulates its various functions and can be phosphorylated by Src and various receptor tyrosine kinases. Additional information: Clone REA548 displays negligible binding to Fc receptors. -
A151 Vitamin D is implicated as a protective factor in human colon carcinogenesis. Anti-tumor activity of vitamin D on colonocytes is thought to be mediated by 1,25 (OH)2D3, the active hormonal metabolite of vitamin D. We examined the role of 1,25 (OH)2D3on a putative VDR/β-catenin interaction. We first sought to confirm that VDR associates physically with β-catenin regulating critical Wnt signaling events in colon tumorigenesis. Second, we assessed the role of the intact and mutant adenomatous polyposis coli (APC) gene, commonly dysregulated in human colon cancers, as a modulator of the VDR/β-catenin interaction. Glutathione-S-transferase (GST) pulldown assays and an in-vitro transcription/translation system to produce β-catenin protein support an interaction between β-catenin and VDR that appears independent of 1,25 (OH)2D3. Further evaluation of this interaction within the cell using a mammalian two hybrid system in transfected HT29-APC, a cell line which allows inducible wildtype APC ...
The present study identified five new β-catenin target genes in thalamic neurons, in addition to previously described Cacna1g[16]. Three of them, Kcna6, Calb2, and Gabra3, were validated by ChIP in vivo and a loss-of-function experiment in cultured neurons, confirming that they might be directly regulated by β-catenin. Two other genes, Cacna2d2 and Kcnh8, also displayed β-catenin-dependence in the latter experiment, although the binding of β-catenin to their regulatory elements was not found. Based on these data, we propose that β-catenin is a regulator of the electrophysiological properties of thalamic neurons in the adult brain.. Numerous genes that we selected in silico as potentially regulated by β-catenin belong to expected functional categories: transcription regulation, cell proliferation, morphogenesis, motility, adhesion, differentiation, and programmed cell death. Similar clusters were observed by others in the genes bound by TCF7L2 in a human colorectal cancer cell line [40]. ...
Our study unveils a TREM2/β-catenin pathway that regulates bone mass by regulating the rate of OC generation. Mechanistically, TREM2 and β-catenin augment the M-CSF-induced proliferation of OcP, retarding their differentiation into mature OC. Ablation of either TREM2 or β-catenin inhibits the proliferation of OcP, accelerating their differentiation into bone-resorbing OC, which ultimately cause osteoporosis. The possibility that TREM2 and β-catenin act along the same pathway is supported not only by the similar osteoporotic phenotypes of TREM2−/− and βcatΔ/Δ mice, but also by genetic evidence that simultaneous heterozygosity for TREM2- and β-catenin-null alleles results in osteoporosis, whereas no phenotype is observed in mice heterozygous for either of these alleles.. TREM2 may enhance M-CSF-induced activation of β-catenin by facilitating the recruitment of DAP12 to the receptor for M-CSF. In turn, DAP12 may activate Syk and Pyk2, which promote phosphorylation and nuclear ...
Shop Juxtamembrane domain-associated catenin ELISA Kit, Recombinant Protein and Juxtamembrane domain-associated catenin Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
gamma-catenin Antibody (F-2) is a monoclonal anti-γ-catenin antibody that detects m, r, and h γ-catenin by WB, IP, IF and ELISA.
β-Catenin is essential for embryonic development and required for cell renewal/regeneration in adult life. Cellular β-catenin exists in three different pools: membranous, cytoplasmic and nuclear. In...
Mutations in the Wnt/-catenin pathway occur in most colorectal cancers (CRCs), and these mutations lead to increased nuclear accumulation of the -catenin transcriptional co-activator. element within the first intron of the gene to drive expression in CRC cells. As such, reducing -catenin expression in CRC cells using shRNAs leads to decreased mRNA and protein levels. …Read More. ...
Absence of β-catenin does not affect spontaneous or glucocorticoid-induced death of thymocytes. (a) Percentage of surviving thymocytes gated on CD45.1+ (WT don
Normal development of β-catenin−/− hematopoietic lineages in a competitive situation. Mixed BM chimeric mice were analyzed 4-6 mo after reconstitution wi
A bunch of us were trying to watch Duck Soup last night as a guy provided unsolicited Marxist subtextual analysis. It was quite illuminating. For example, I had never realized that Edgar Kennedy, selling his lemonade, represented Capital while Harpo, the peanut vendor (or El Manicero, badly whistled), was Labor. Their struggle was represented brilliantly by…
The canonical WNT-β-catenin pathway is essential for self-renewal, growth and survival of AML stem/blast progenitor cells (BPCs). Deregulated WNT signaling inhibits degradation of β-catenin, causing increased nuclear translocation and co-factor activity of β-catenin with the transcriptional regulator TCF4/LEF1 in AML BPCs. Here, we determined the pre-clinical anti-AML activity of the ...
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The catenins are polypeptides that bind to the conserved cytoplasmic tail of cadherins and are required for cadherin function. α-Catenin is related to vinculin and seems to be required for the interaction of cadherins with the actin cytoskeleton. β-Catenin is homologous to armadillo, a segment polarity gene in Drosophila that participates in developmental signaling. Recent findings indicate that β-catenin also participates in developmental signaling and embryonic patterning in Xenopus laevis. At least a portion of the electrophoretic band migrating at the position of γ-catenin consists of plakoglobin, a desmosomal and zonula adherens protein that has high sequence similarity to β-catenin and armadillo. The catenins may be involved in the regulation of cadherin function during tissue morphogenesis and tumorigenesis. ...
TY - JOUR. T1 - Expression of cadherins and catenins in paired tumor and non-neoplastic primary prostate cultures and corresponding prostatectomy specimens. AU - Wang, J.. AU - Krill, D.. AU - Torbenson, Michael. AU - Wang, Q.. AU - Bisceglia, M.. AU - Stoner, J.. AU - Thomas, A.. AU - DeFlavia, P.. AU - Dhir, R.. AU - Becich, M. J.. PY - 2000/1/1. Y1 - 2000/1/1. N2 - Cadherins are a family of transmembrane proteins that play a crucial role in cell differentiation, cell migration, and intercellular adhesion. Cadherins are associated with catenins through their highly conserved cytoplasmic domain. Down-regulation of E-cadherin protein has been shown in various human cancers. This study examined the expression of cadherins and associated catenins at the mRNA level. Paired tumor and non-neoplastic primary prostate cultures were obtained from surgical specimens. Quantitative multiplex fluorescence reverse transcriptase-polymerase chain reaction (QMF RT-PCR) and quantitative analysis were performed ...
Cadherins represent a distinct family of single transmembrane domain glycoproteins that mediate calcium-dependent cell-cell adhesion via homophilic interactions of their NH2-terminal ectodomains (Shapiro et al., 1995; Gumbiner, 2000). The intracellular domain of E-cadherin associates with a protein family collectively termed catenins (Ozawa et al., 1989; Nathke et al., 1994). β-catenin and γ-catenin (plakoglobin) interact directly with E-cadherins COOH-terminal domain in a mutually exclusive way, and both proteins associate with α-catenin, which links the cadherin complexes to the actin cytoskeleton and mediates stable cell adhesion. p120ctn is another catenin family member (Anastasiadis and Reynolds, 2000), which binds to the cytoplasmic juxtamembrane portion of E-cadherin and influences E-cadherin clustering and adhesive strength (Ozawa and Kemler, 1998; Yap et al., 1998; Aono et al., 1999; Ohkubo and Ozawa, 1999; Thoreson et al., 2000).. In addition to its adhesive functions, β-catenin ...
The sys-1 gene encodes a highly divergent β-catenin (6, 8). Several lines of evidence support the idea that SYS-1 is a functional β-catenin. First, transgenic SYS-1 can rescue a null mutant of bar-1, which encodes a typical β-catenin. Second, SYS-1 binds the β-catenin binding domain of POP-1/TCF. Third, SYS-1 acts as a transcriptional coactivator for POP-1 in a TOPFLASH reporter. Fourth, ceh-22 expression in distal SGP daughters depends on POP-1 binding sites in the ceh-22b promoter and also on SYS-1 and POP-1. Therefore, SYS-1 acts in many ways like a typical β-catenin.. Both SYS-1/β-catenin and POP-1/TCF control the SGP asymmetric cell division (7, 9). In pop-1 mutants, as in sys-1 mutants, the SGP daughters both adopt a proximal fate (Fig. 1B). Importantly, POP-1 is asymmetrically distributed to SGP daughters (10), a phenomenon that has been seen in many asymmetric cell divisions and has been dubbed "POP-1 asymmetry" (11). Although counterintuitive, nuclear POP-1 is reduced in distal ...
The advanced phases of chronic myeloid leukemia (CML) are known to be more resistant to therapy. This resistance has been associated with the overexpression of ABCB1, which gives rise to the multidrug resistance (MDR) phenomenon. MDR is characterized by resistance to nonrelated drugs, and P-glycoprotein (encoded by ABCB1) has been implicated as the major cause of its emergence. Wnt signaling has been demonstrated to be important in several aspects of CML. Recently, Wnt signaling was linked to ABCB1 regulation through its canonical pathway, which is mediated by β-catenin, in other types of cancer. In this study, we investigated the involvement of the Wnt/β-catenin pathway in the regulation of ABCB1 transcription in CML, as the basal promoter of ABCB1 has several β-catenin binding sites. β-catenin is the mediator of canonical Wnt signaling, which is important for CML progression. In this work we used the K562 cell line and its derived MDR-resistant cell line Lucena (K562/VCR) as CML study models. Real
Nasopharyngeal carcinoma has a high incidence in southern China. The Wnt/β-catenin signaling pathway plays a major role in cancer development and progression. Our current study aims to determine the clinical significance of the Wnt/β-catenin pathway components such as β-catenin, cyclooxygenase 2, cyclin D1, c-Myc, and E-cadherin in 148 nasopharyngeal carcinomas by immunohistochemistry. We found that nasopharyngeal carcinoma stage T3+T4 had significantly higher expression of β-catenin, cyclooxygenase 2, cyclin D1, and c-Myc and lower expression of E-cadherin than nasopharyngeal carcinoma stage T1+T2 (P | .001, P | .05, respectively).There was significantly higher expression of β-catenin (P = .001) and cyclooxygenase 2 (P = .003) and lower expression of E-cadherin (P = .001) in nasopharyngeal carcinoma with lymph node metastasis than in nasopharyngeal carcinoma without lymph node metastasis. The expression of β-catenin in nasopharyngeal carcinoma was positively correlated with cyclooxygenase 2 (r =
Pancreatic β-cells are highly responsive to changes in glucose, but the mechanisms involved are only partially understood. There is increasing evidence that the β-catenin signalling pathway plays an important role in regulating β-cell function, but the mechanisms regulating β-catenin signalling in these cells is not well understood. In the present study we show that β-catenin levels and downstream signalling are regulated by changes in glucose levels in INS-1E and β-TC6-F7 β-cell models. We found a glucose-dependent increase in levels of β-catenin in the cytoplasm and nucleus of INS-1E cells. Expression of cyclin D1 also increased with glucose and required the presence of β-catenin. This was associated with an increase in phosphorylation of β-catenin on Ser552, which is known to stabilize the molecule and increase its transcriptional activity. In a search for possible signalling intermediates we found forskolin and cell-permeable cAMP analogues recapitulated the glucose effects, ...
Synapses are fundamental building blocks of neural circuits. Synapse formation requires complex regulation involving cell adhesion molecules, secreted molecules, transcription factors and so forth. For cell adhesion molecules, ...
In cells not exposed to the signal, β-catenin levels are kept low through interactions with the protein kinase zw3/GSK-3, CK1a, APC and Axin (Behrens, 1998 Itoh 1998., Hamada, 1999.) β-catenin is degraded, after phosphorylation by GSK-3 and CK1 alpha (Yanagawa 2002, Liu 2002, Amit 2002), through the ubiquitin pathway (Aberle 1997.), involving interactions with Slimb/bTrCP (Jiang 1998, Marikawa 1998,; reviewed in Maniatis 1999). In a current model, Wnt signaling initially leads to a complex between Dsh, GBP/Frat1, Axin and Zw3/GSK, which may be the regulatory step in the inactivation of Zw3/GSK (Salic, 2000; Farr 2000). The DIX domain in Axin is similar to the NH2 terminus in Dsh, and promotes interactions between Dsh and Axin (Hsu 1999, Smalley, 1999). As a consequence, GSK does not phosphorylate β-catenin anymore, releasing it from the Axin complex and accumulation (Salic, 2000).The stabilized β-catenin then enters the nucleus to interact with TCF. β-catenin can convert TCF into a ...
The most cogent studies supporting the S45 primer model used exogenously overexpressed β-catenin mutants and did not examine cells of intestinal epithelial origin, the major cell type in which disruption of this pathway results in neoplasia. We reasoned that naturally occurring mutations of the β-catenin gene in colorectal cancers could provide a unique opportunity to address this model in cells of colorectal epithelial origin under near physiological conditions (i.e., without overexpression of exogenous proteins). It was reported previously that the colorectal cancer cell line LS 174T harbors a mutation of β-catenin at codon 45 (S45F). We confirmed the presence of the S45F mutation in LS 174T and further determined that these cells lacked a WT 3 allele (Fig. 1A) ⇓ . Accordingly, the S45 primer model would suggest that phosphorylation of β-catenin at S33, S37, or T41 should be absent or greatly diminished in these cells. Indeed, previous studies using overexpressed mutant S45F β-catenin ...
Aberrant activation of the Wnt-β-catenin pathway has been found in a wide range of cancers, especially in cancers derived from intestine, skin, mammary gland and haematopoietic cells. Moreover, the Wnt-β-catenin pathway may preferentially influence stem/progenitor cell expansion in these cancers (Wend et al., 2010). Although many downstream target genes for both normal development and tumorigenesis have been identified in different cellular contexts, the genes that mediate the Wnt-β-catenin pathway activity in maintaining the stem cell properties are still not very clear. c-Myc, a reprogramming factor and a well-known Wnt target, was recently demonstrated to be an important stem cell regulator in normal and cancerous cells (Kim et al., 2010; Smith et al., 2011). However, no study has established a convincing relationship between the Wnt-β-catenin pathway and c-Myc in stem cells. In contrast, recent studies on both iPS and ESCs suggest that the role of the Wnt-β-catenin pathway in ...
Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the
beta Catenin (phospho Thr41/Ser45) antibody (catenin (cadherin-associated protein), beta 1, 88kDa) for WB. Anti-beta Catenin (phospho Thr41/Ser45) pAb (GTX50180) is tested in Human samples. 100% Ab-Assurance.
beta Catenin antibody [1F3] (catenin (cadherin-associated protein), beta 1, 88kDa) for IHC-P, WB. Anti-beta Catenin mAb (GTX84650) is tested in Human, Monkey samples. 100% Ab-Assurance.
Cadherins are a family of transmembrane proteins formed from multiple repeats of cadherin-specific motif (a recurrent molecular sequence) and also share a large extracellular domain. Cadherins are classified into two groups: Classical Cadherins and Protocadherins. The main difference between the two groups of cadherins is the classical cadherins contain five cadherin repeats with the third (EC3) and the fifth (EC5) repeat having very specific features. The protocadherins do not share the same features of the EC3 and EC5 units; are longer than five repeats long; and the sequences are very similar to each other. As a result of these differences, the classical cadherins are very specific and do not adhere to a large number of different ECM proteins, whereas protocadherins are much more flexible in their attachments. Classical cadherins are known to only be found in vertebrates so far, while protocadherins are found in planaria, hydra, Drosophila, and various mammals. Cadherins rely heavily on ...
β-Catenin expression was observed in the membrane and/or cytoplasm without any significant nuclear expression. HER-2/neu and EGFR were observed on the membrane in 21% and 6% of tumors, respectively, and Met stained in a membrane/cytoplasm distribution in 28% of cases. Cyclin D1 was expressed in the nucleus and MMP7 was expressed in the cytoplasm in 26% and 75% of tumors, respectively. Nuclear expression of p53 was noted in 31% of tumors. When each marker was analyzed separately, only p53 and Met demonstrated a significant correlation with survival. However, patients who had tumors that coexpressed high levels of β-catenin and p53 had markedly worse overall survival (P = 0.0026). In multivariate analysis, only tumor size, Met, and the coexpression of β-catenin and p53 retained statistical significance. ...
THE EXISTENCE OF CTNND1 IN THIS RENDITION OF GENES IS NOTABLE, THAT IS THAT SOMEWHERE ALONG THE LINE IMMUNOTHERAPY OR ANTI-ROS-1 MAY HAVE A ROLE IN ANAPLASTIC CANCERS WHICH OVER EXPRESS THE ROS-1 MUTATION! IN ITS METASTATIC PHASE THAT IS. "activation of β-catenin could represent another mechanism leading to the ATC (THYROID) phenotype. Indeed in one study, such mutations were found in 61% of the lesions but not in the precursor lesions" (HEBRANT ET AL ...
The Wnt/β-catenin pathway regulates the cell growth and survival following radiation in various types of cancer cells. Our previous report show that activation of the Wnt/β-catenin signaling pathway is a key radioprotective mechanism in irradiated head and neck cancer (HNC) cells. However, the molecular mechanisms by which β-catenin regulates radiation sensitivity are not clear. Here we attempted to elucidate the mechanism of cell death following radiation by studying how β-catenin silencing controls the radiation sensitivity of radioresistant HNC cells.. Of nine cell lines examined, the most radioresistant cell line (AMC-HN-9) were selected for this experiments. β-catenin silencing using small interfering RNA(siRNA) down-regulated β-catenin expression up to 72 h, which was confirmed by western blot analysis. The sensitivity to radiation was anlayzed by clonogenic analysis and MTT assay. As a result, β-catenin silencing remarkably decreased the survival of irradiated AMC-HN-9 cells and ...
Background: β‐Catenin is an important signaling molecule in the Wnt pathway that plays a key role in tumorgenesis. In the absence of Wnt signaling, the cytoplasmic level of β‐catenin is kept low due to rapid proteasomal‐mediated degradation of GSK3β phosphorylated β‐catenin. Activation of Wnt signaling leads to the inactivation of GSK3β, resulting in stabilization and accumulation of β‐catenin in the cytoplasm. Consequently, β‐catenin translocates into the nucleus, where it binds with members of the T‐cell factor (Tcf)/lymphocyte enhancer‐binding factor family of transcription factors and activates the expression of many target genes important for cancer development. Most colon cancers have activating mutations in the APC tumor suppressor or in β‐catenin itself. Furthermore, activating β‐catenin mutations have been found in a variety of other tumors such as melanomas, hepatocellular carcinomas, skin, breast, and prostate cancer, whereas β‐catenin is not activated ...
FHF3 span between extending and Be anxious image resolution (Fig. 3C). Measurements at 10s periods offered identical outcomes STF-62247 (Fig. H4G). Pretreatment with GdCl3 to stretch-loading got no impact prior, and dominated out advantages from stretch-activated Ca2+ stations (not really demonstrated). Cadherin inactivation with obstructing DECMA-1 antibody ablated the response (Fig. 3D). This instant, reversible switching suggests that -catenin features like an flexible springtime in series with the cytoskeleton, which deforms with the extracellular substrate and matrix. Assessment of the nanoprobe and MTC measurements shows that the Be anxious/ECFP reduce during bead rotating (Fig. 2B) can be credited to constant, mechanised perturbation than biochemical adaptation rather. Shape 3 Exogneous mechanised extend induce instant, reversible -catenin conformation switching at intercellular junctions Biochemical indicators STF-62247 during the 3s span between base extend and image resolution could ...
human SVH protein: A specific splicing variant of SVH, a novel human armadillo repeat protein, is up-regulated in hepatocellular carcinomas; amino acid sequence in first source
Article printed from SurvivalBlog.com: https://survivalblog.com URL to article: https://survivalblog.com/planning-escape-part-5-jmd/ URLs in this post:. [1] edible plants reference card: https://www.amazon.com/Edible-Wild-Plants-Familiar-Naturalist/dp/1583551271/ref=pd_bxgy_14_2/130-0102650-6272954?_encoding=UTF8&pd_rd_i=1583551271&pd_rd_r=a03930dd-ba27-4722-b30e-f4ed355ef016&pd_rd_w=KsEuq&pd_rd_wg=s3Ite&pf_rd_p=09627863-9889-4290-b90a-5e9f86682449&pf_rd_r=T7HBDBCKDNB88FPD7HV0&psc=1&refRID=T7HBDBCKDNB88FPD7HV0. [2] foraging guide: https://www.amazon.com/Foraging-Wild-Edible-Foods-Sustainable/dp/1620052784/ref=pd_sbs_14_4/130-0102650-6272954?_encoding=UTF8&pd_rd_i=1620052784&pd_rd_r=177f1d16-ad1c-4a67-af34-d1e34c70425a&pd_rd_w=LGVNT&pd_rd_wg=WSsxC&pf_rd_p=52b7592c-2dc9-4ac6-84d4-4bda6360045e&pf_rd_r=5167XZ38YCQ0YAW2C8QM&psc=1&refRID=5167XZ38YCQ0YAW2C8QM. [3] trotline: ...
Polyclonal antibody for ALPHA 1 CATENIN/CTNNA1 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. ALPHA 1 CATENIN/CTNNA1 information: Molecular Weight: 100071 MW; Subcellular Localization: Isoform 1: Cytoplasm,
Rabbit Polyclonal Anti-gamma Catenin Antibody. Validated: WB, IHC, IHC-P, IP. Tested Reactivity: Human, Mouse, Rat, and more. 100% Guaranteed.
Rabbit polyclonal beta Catenin (phospho Y489) antibody validated for WB, ICC and tested in Human. Immunogen corresponding to synthetic peptide
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The canonical Wnt/β-catenin pathway is involved in the formation of craniofacial skeleton and oral tissues. Aberrant nuclear localization of β-catenin protein has been described in several human diseases including a subset of odontogenic tumors thereby suggesting an important role in tumor development. Fibro-osseous lesions of the craniofacial skeleton comprise several neoplastic, and reactive mesenchymal proliferations in which β-catenin status is unknown. To study this, we immunostained 171 fibro-osseous lesions for β-catenin protein and, for lesions with nuclear positivity, sequenced exon 3 of the CTNNB1 gene and exon 15 of the APC gene ...
Catenin Beta 1, CTNNB are cell adhesion molecules called (p120*␠-catenin) cadherins (the (CDH1) E-cadherin/catenin complex) include the beta-catenins a multifunctional molecule Locus: 3p22.1 [§§; ^]. Neurons also exhibited a higher CTNNB/TCF pathway association (concentration versus accumulation) with cadherins; CAS-chromosome segregation 1-like (yeast) binds with E-cadherin but not with beta-catenin. Which interacts with (Tcf-T-cell factor where a…
The cadherin-catenin complex is important for mediating homotypic, calcium-dependent cell-cell interactions in diverse tissue types. Although proteins of this complex have been identified, little is known about their interactions. Using a genetic assay in yeast and an in vitro protein-binding assay, we demonstrate that beta-catenin is the linker protein between E-cadherin and alpha-catenin and that E-cadherin does not bind directly to alpha-catenin. We show that a 25-amino acid sequence in the cytoplasmic domain of E-cadherin and the amino-terminal domain of alpha-catenin are independent binding sites for beta-catenin. In addition to beta-catenin and plakoglobin, another member of the armadillo family, p120 binds to E-cadherin. However, unlike beta-catenin, p120 does not bind alpha-catenin in vitro, although a complex of p120 and endogenous alpha-catenin could be immunoprecipitated from cell extracts. In vitro protein-binding assays using recombinant E-cadherin cytoplasmic domain and ...
Due to alterations of any components in this pathway, Wnt/β-catenin signaling pathway is aberrantly activated in various cancers. β-catenin can also be activated or stabilized by other factors to promote cancer development. For example, long noncoding RNA pancEts-1 accelerates neuroblastoma progression via hnRNPK-mediated stabilization of β-catenin [33]. Cytoplasmic hPCL3s, which is highly expressed in HCC samples, promotes HCC metastasis through activation of β-catenin/IL6 pathway [34]. After stabilizing or activating by Wnt signals or other factors, β-catenin enters the nucleus and elicits its transcriptional activity. The most initially identified targets for β-catenin are c-myc and cyclin D1, which act as oncogenic roles in cancer development. Additionally, Deptor, a suppressor of mTOR, has been demonstrated as a novel target of Wnt/β-catenin/c-Myc signaling pathway and contributes to the growth of colorectal cancer cell [35]. Here, we showed that the expression of β-catenin as well ...
β-catenin, the critical effector of the Wnt pathway, regulates a number of key processes during development including proliferation, differentiation and cell fate determination, as well as tissue homeostasis in adults. β-catenin is normally localized to the cell adhesion junctions in epithelial cells and its abnormal cytplasmic/nuclear stabilization drives uncontrolled transcription of target genes (including c-jun, cyclin D1, c-myc, survivin, and MMP-7) regulating cell proliferation, survival and cell adhesion.12 In view of its biological importance, it is not surprisingly that deregulation of β-catenin has been linked to the pathogenesis of a number of human cancers, particularly those with an epithelial cell origin.28 Illegitimate activation of β-catenin has also been reported in several types of hematopoietic cancers.19,29-31 Nevertheless, the functional status and biological role of β-catenin have never been investigated in ALK+ALCL. In this study, we found that β-catenin is ...
The natural agent rhein is an ananthraquinone derivative of rhubarb, which has anticancer effects. To determine the mechanisms underlying the anticancer effects of rhein, we detected the effect of rhein on several oncoproteins. Here, we show that rhein induces β-catenin degradation in both hepatoma cell HepG2 and cervical cancer cell Hela. Treatment of HepG2 and Hela cells with rhein shortens the half-life of β-catenin. The proteasome inhibitor MG132 blunts the downregulation of β-catenin by rhein. The induction of β-catenin degradation by rhein is dependent on GSK3 but independent of Akt. Treatment of HepG2 and Hela cells with GSK3 inhibitor or GSK3β knockdown abrogates the effect of rhein on β-catenin. GSK3β knockdown compromises the inhibition of HepG2 and Hela cell growth by rhein. Furthermore, rhein dose not downregulate β-catenin mutant that is deficient of phosphorylation at multiple residues including Ser33, Ser37, Thr41 and Ser45. Moreover, rhein induces cell cycle arrest at S ...
To better understand the development of HSCs, we have investigated the role of Wnt/β-catenin signaling in the mouse embryonic aorta in the AGM region at midgestation. The AGM region exhibits activated β-catenin (as well as β-catenin activity) in a small subpopulation of endothelial-like cells. We have demonstrated that embryonic endothelial cells lacking β-catenin activity (by pharmacological inhibition or genetic deletion) preclude their contribution to generate HSCs and contribute to the hematopoiesis of the adult organism.. Wnt canonical pathway is important in the maintenance of several types of stem cells such as intestinal, epidermal, or mammary (Reya and Clevers, 2005); however, some questions still remain about the role of β-catenin for the generation and maintenance of HSCs. It has been shown that activation of β-catenin in BM hematopoietic precursors increases the pool of cells with long-term repopulating capacity (Reya et al., 2003; Willert et al., 2003; Goessling et al., 2009) ...
Mutations of APC appear to initiate sporadic and inherited forms of human colorectal cancer. Although these mutations have been well characterized, little is known about the function of the APC gene product. Two cellular proteins that associate with APC were identified by nucleotide sequence analysis and peptide mapping as the E-cadherin-associated proteins alpha- and beta-catenin. A 27-residue fragment of APC containing a 15-amino acid repeat was sufficient for the interaction with the catenins. These results suggest an important link between tumor initiation and cell adhesion. ...
Cadherins mediate homophilic, Ca2+-dependent cellular adhesion at adherens junctions. Experiments in MDCK cells, which provide a model for cadherins at adherens junctions, demonstrated the formation of cadherin-NPRAP-ABP complexes dependent on the expression of NPRAP and the integrity of the NPRAP-ABP interaction, and the formation of NPRAP-ABP-GluR2 complexes dependent on expression of ABP. This suggests that the proposed cadherin-NPRAP-ABP-GluR2 complexes can indeed form in cells. Two dominant-negative mutants of NPRAP were assayed for their effects on GluR2. One mutant does not interact with ABP, GRIP, or PSD-95, and the second binds these scaffolding proteins but does not bind to cadherins. Both mutants reduced GluR2 surface levels. This suggests that cadherin-NPRAP-ABP-GluR2 complexes contribute to the surface stabilization of GluR2. In neurons, adherens junction structures containing cadherins are found at synapses (Takeichi and Abe, 2005). This suggests that the AMPARs that are anchored ...
Results Complete data were available on 19 patients comprising; two polyp cancers, six Dukes A, four Dukes B and seven Dukes C tumours. There were eight right-sided, seven left-sided and four rectal tumours. Higher levels of nuclear β-Catenin staining were noted in the 11 patients with node negative disease (mean H-score = 1.8; SD = 0.4) than in node positive disease (mean H-score = 1.3; SD = 0.2; p = 0.03, Mann-Whitney). Interestingly lower nuclear expression of β-Catenin was seen in the patient with a polyp cancer and node positive disease than in the polyp cancer without nodal disease (H-score 1.4 vs. 2.4). ...
Chandran K C ♦ December 11, 2015 ♦ Leave a comment Scientists and cancer researchers have lately identified a particular biological molecule in our body known as BETA CATENIN as an ideal molecular target for anti-cancer therapy. They have been trying to develop drugs that could inhibit the over-expressions and aberrations of BETA CATENIN, which is recognized to be playing a big role in the biochemical processes underlying various types of cancers. Their attempts have not been so far successful, since any chemical compound they develop to target BETA CATENIN will inevitably have serious harmful effects upon the organism, since it is an essential biological molecule having diverse roles normal vital processes, and its complete inhibition may lead to be very dangerous consequences.. BETA CATENIN is a protein found as part of molecular complexes in forming cadherin cell adhesion factors of animal cells. It belongs to a family of biological compounds known as catenins, consisting of alpha ...
1I7X: The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin.
The results of the current study showed the molecular and functional activation of β-catenin by hypoxia in HCC and showed its contribution to hypoxia-induced metastatic phenotypes. The induction of EMT was one of the proinvasive mechanisms augmented by β-catenin during hypoxia. The coexpression of β-catenin and HIF-1α (a marker of hypoxia) in HCC was found to be correlated with metastases and poor prognosis in two independent cohorts of patients. These results confirm the importance of β-catenin in HCC under hypoxic conditions.. Hypoxia plays a critical role in tumor progression (1). Consistent with our previous report (17), it not only facilitated in vitro cell invasion in HCC but also resulted in peritoneal seeding and pulmonary metastasis in an in vivo HAL model. However, the growth of HCC cells and xenografts were suppressed by hypoxia. Further analysis revealed that this could be attributed to the arrest of cell proliferation rather than the induction of apoptosis (Supplementary Fig. ...
Phospho-beta Catenin (Tyr489) Polyclonal Antibody from Invitrogen for Western Blot and Immunohistochemistry (Paraffin) applications. This antibody reacts with Human, Mouse, Non-human primate, Rat samples. Supplied as 100 µg purified antibody (1 mg/ml) in Dulbeccos PBS with 50% glycerol, 150mM NaCl and 0.02% sodium azide; pH 7.4.
View Notes - 2011_Questions_Week_14_Answers from BIO 349 at University of Texas. 1. What happens when you deplete beta catenin in planarians? -The organism is no longer able to form a posterior side
Antibody Sampler Kit for studying Catenin-alphaE/Catenin-beta/E-Cadherin/N-Cadherin/P-Cadherin/R-cadherin in the Adhesion research area.
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Z3330795 (talk) 16:14, 11 April 2013 (EST)FAK-Focal Adhesion Kinase Antibody --Z3376548 (talk) 16:15, 11 April 2013 (EST) Catenin beta Antibody (6F9) --Z3374087 (talk) 16:15, 11 April 2013 (EST)alpha-2-catenin --Z3331321 (talk) 16:16, 11 April 2013 (EST) Anti-α-E-Catenin Rabbit ...
ウサギ・ポリクローナル抗体 ab36905 交差種: Ms,Hu 適用: WB,IP,IHC-P,ICC/IF…H Cadherin抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody 製品。国内在庫と品質保証制度も充実。
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Androgen receptor (AR) is the major therapeutic target in aggressive prostate cancer. However, targeting AR alone can result in drug resistance and disease recurrence. Therefore, simultaneous targeting of multiple pathways could in principle be an effective approach to treating prostate cancer. Here we provide proof-of-concept that a small-molecule inhibitor of nuclear β-catenin activity (called C3) can inhibit both the AR and β-catenin-signaling pathways that are often misregulated in prostate cancer. Treatment with C3 ablated prostate cancer cell growth by disruption of both β-catenin/T-cell factor and β-catenin/AR protein interaction, reflecting the fact that T-cell factor and AR have overlapping binding sites on β-catenin. Given that AR interacts with, and is transcriptionally regulated by β-catenin, C3 treatment also resulted in decreased occupancy of β-catenin on the AR promoter and diminished AR and AR/β-catenin target gene expression. Interestingly, C3 treatment resulted in ...
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin, and gamma-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with alpha-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show ...
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin, and gamma-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with alpha-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show ...
The Wnt/β-catenin pathway has a key role in regulating cellular processes and its aberrant signaling can lead to cancer development. The role of β-catenin expression in pancreatic ductal adenocarcinoma is somewhat controversial. Transcription factor PROX1 is a target of Wnt/β-catenin signaling and it is involved in carcinogenesis through alterations in its expression. The actions can be either oncogenic or tumor suppressive depending on the tissue. The aim of this study was to investigate PROX1 and β-catenin expression in pancreatic ductal adenocarcinoma (PDAC). Expression of PROX1 and β-catenin were evaluated in 156 patients by immunohistochemistry of tissue microarrays. Associations between tumor marker expression and clinicopathological parameters were assessed by the Fischers exact-test or the linear-by-linear association test. The Kaplan-Meier method and log-rank test were used for survival analysis. Uni- and multivariate survival analyses were carried out by the Cox regression proportional
Cell-cell adhesion plays a key role in development, tissue maintenance and cancer (Birchmeier, 1995; Gumbiner, 2005; Takeichi, 1995; Yap, 1998). In vertebrates, the classical cadherins (i.e. type I and type II cadherins) comprise a large family (26 members) of transmembrane glycoproteins found in essentially all adhesive tissues (Gallin, 1998; Hulpiau and van Roy, 2009). Epithelial cadherin (E-cadherin, or cadherin 1) is the main cadherin in epithelial tissues and plays an important role in morphogenesis and homeostasis in most glandular tissues, including the mammary gland. Although the importance of cadherins in mammary morphogenesis is widely accepted, the role of p120-catenin (also known as catenin delta 1) in this process remains to be investigated.. The extracellular domains of cadherins connect adjacent cells via homophilic interaction, while the cytoplasmic domains form a complex with a group of proteins known as catenins (Gumbiner, 2005; Takeichi, 1991). p120-catenin (hereafter p120) ...
Looking for online definition of Beta catenin in the Medical Dictionary? Beta catenin explanation free. What is Beta catenin? Meaning of Beta catenin medical term. What does Beta catenin mean?
Beginning at Leu 1029, the APC‐rA peptide adopts a conformation strikingly different from that of XTcf3 or E‐cadherin (Figure 3B). The C‐terminal half of the peptide, from Leu1029 to Glu1034, bulges out of the β‐catenin groove, away from the paths of XTcf3 and E‐cadherin (Figures 2B and 3B). This difference in conformation is probably due to the presence of a lysine residue at amino acid 1030 of APC‐rA. In XTcf3 and E‐cadherin this position is occupied by an acidic residue (Glu24 of XTcf3, Glu682 of E‐cadherin), which forms a salt bridge with β‐catenin Lys312 to form the second charged button of the extended region (Figure 3B). The lysine at this position in APC‐rA probably causes charge repulsion with β‐catenin Lys312, leading to a deviation from the conformations of the other two ligands. The conformation of the backbone at Lys1030 suggests that the side chain of this residue is in the vicinity of β‐catenin Glu462 and several other acidic residues. Although APC‐rA ...
A variety of signals governing early extension, guidance, and connectivity of olfactory receptor neuron (ORN) axons has been identified; however, little is known about axon-mesoderm and forebrain (FB)-mesoderm signals. Using Wnt-ßcatenin reporter mice, we identify a novel Wnt-responsive resident cell population, located in a Frizzled7 expression domain at the surface of the embryonic FB, along the trajectory of incoming ORN axons. Organotypic slice cultures that recapitulate olfactory-associated Wnt-ßcatenin activation show that the ßcatenin response depends on a placode-derived signal(s). Likewise, in Dlx5-/- embryos, in which the primary connections fail to form, Wnt-ßcatenin response on the surface of the FB is strongly reduced. The olfactory placode expresses a number of ßcatenin-activating Wnt genes, and the Frizzled7 receptor transduces the canonical Wnt signal; using Wnt expression plasmids we show that Wnt5a and Wnt7b are sufficient to rescue ßcatenin activation in the absence of ...
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The intercellular Adherens Junctions (AJs) are specialized sub-apical structures that function as principle mediators of cell-cell adhesion. Their disassembly correlates with a loss of cell-cell contact and an acquisition of migratory potential. The Adherens Junctions have a crucial role both as sensors of extracellular stimuli and in regulating the dynamics of epithelial cell sheets or with neighboring cells. Cadherins, the Type-I transmembrane proteins of the Adherens Junctions, are principally responsible for homotypic cell-cell adhesion. E-Cadherin, which is present primarily in epithelia, is the best-characterized Cadherin and represents the prototype of classical Cadherins. The extracellular domain of E-Cadherin binds to Ca2+ (Calcium) and forms complexes with the extracellular domains of E-Cadherin molecules on neighboring cells. The cytoplasmic domain of E-Cadherin associates with cytosolic proteins called Catenins (Alpha, Beta and p120), which in turn provide anchorage to the Actin ...
TY - JOUR. T1 - Osteopontin, E-cadherin, and β-catenin expression as prognostic biomarkers in patients with radically resected gastric cancer. AU - Di Bartolomeo, M.. AU - Pietrantonio, F.. AU - Pellegrinelli, A.. AU - Martinetti, A.. AU - Mariani, L.. AU - Daidone, M.G.. AU - Bajetta, Emillio. AU - Pelosi, G.. AU - de Braud, F.. AU - Floriani, I.. AU - Miceli, R.. N1 - Cited By :3 Export Date: 8 March 2017. PY - 2016. Y1 - 2016. U2 - 10.1007/s10120-015-0495-y. DO - 10.1007/s10120-015-0495-y. M3 - Article. VL - 19. SP - 412. EP - 420. JO - Gastric Cancer. JF - Gastric Cancer. SN - 1436-3291. IS - 2. ER - ...
Expression of both Otx2 and Mitf proteins is rapidly downregulated in Tyrp1-Cretg/0;β-cateninfloxdel/FL RPE; therefore, we asked whether β-catenin associates with their enhancers in vivo. We identified six putative TCF/LEF binding sites (Hallikas et al., 2006) in a 2248bp-fragment of the RPE-specific Mitf-D enhancer, positioned at -1393, -1389, -389, -364, -321 and -132 relative to the transcriptional start site. β-catenin binds at or near these sites, as determined by ChIP using native RPE lysate from E12.5 embryos (Fig. 4I). To examine whether β-catenin can transcriptionally activate Mitf, the Mitf-D enhancer was cloned into the pGL3B luciferase reporter. β-catenin produced an 8-fold increase in luciferase activity, and this activation was reduced by co-transfection with ΔTCF3 or by mutation of all potential TCF/LEF binding sites (Fig. 4I). Furthermore, one putative TCF/LEF binding site was identified in the T0 enhancer of Otx2 (Martinez-Morales et al., 2003), within in a region that is ...
Wnt-5a signaling may activate PKC and intracellular Ca2+ mobilization to trigger a series of downstream effects including activation of NF-AT and CaMKII (Kuhl et al., 2000a; Saneyoshi et al., 2002). During early Xenopus development, Wnt-5a activates calcineurin, which leads to NF-AT nuclear localization and increased β-catenin degradation (Saneyoshi et al., 2002). To address how Wnt-5a transduces its signal in mammalian cells, we checked whether Wnt-5a activates NF-AT transcriptional activity and whether such activation is required for Wnt-5a-induced β-catenin degradation. We found that NF-AT transcriptional activity was only weakly activated by Wnt-5a (∼50%), whereas it was strongly up-regulated by activated calcineurin (∼300%; Fig. 3 A). In addition, we found that although activated calcineurin was able to inhibit the TOPFLASH activity up-regulated by β-catenin S37A, Wnt-5a had an additive effect in its presence (Fig. 3 B). Moreover, specific inhibition of calcineurin by Cyclosporin A ...
Proto-oncogene tyrosine-protein kinase Yes is an enzyme that in humans is encoded by the YES1 gene. This gene is the cellular homolog of the Yamaguchi sarcoma virus oncogene. The encoded protein has tyrosine kinase activity and belongs to the src family of proteins. This gene lies in close proximity to thymidylate synthase gene on chromosome 18, and a corresponding pseudogene has been found on chromosome 22. YES1 has been shown to interact with Janus kinase 2, CTNND1, RPL10 and Occludin. GRCh38: Ensembl release 89: ENSG00000176105 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000014932 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Semba K, Yamanashi Y, Nishizawa M, Sukegawa J, Yoshida M, Sasaki M, Yamamoto T, Toyoshima K (Mar 1985). "Location of the c-yes gene on the human chromosome and its expression in various tissues". Science. 227 (4690): 1038-40. doi:10.1126/science.2983418. PMID 2983418. "Entrez Gene: YES1 v-yes-1 Yamaguchi sarcoma viral oncogene ...
Our results identified a novel pathway of YWHAZ-β-catenin axis in NSCLC cell malignancy. We showed that the metastatic activity of YWHAZ is mediated through the prevention of β-catenin ubiquitination. We showed that YWHAZ associates with phospho-β-catenin at Ser552 to retard β-catenin degradation. Subsequently, β-catenin accumulation in cancer cells contributes to its nuclear translocation and the activation of EMT-related genes (Fig. 6E). Conversely, disruption of the YWHAZ-β-catenin interaction enhances β-catenin ubiquitination and reduces cell invasiveness.. YWHAZ protein expression is well known to be associated with advanced disease grade and poor clinical outcome in Western NSCLC patients (18), but the molecular contribution of YWHAZ in lung cancer metastasis is still unknown. Particularly, it is unclear whether YWHAZ gene amplification is relevant to lung cancer progression. Here, we conducted array CGH and microarray to identify YWHAZ as an invasion-enhancer candidate. Actually, ...
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Hepatocellular carcinoma (HCC) is one of the most common primary hepatic malignancies and one of the fastest-growing causes of cancer-related mortality in the United States. The molecular basis of HCC carcinogenesis has not been clearly identified. Among the molecular signaling pathways implicated in the pathogenesis of HCC, the Wnt/β-catenin signaling pathway is one of the most frequently activated. A great effort is under way to clearly understand the role of this pathway in the pathogenesis of HCC and its role in the transition from chronic liver diseases, including viral hepatitis, to hepatocellular adenomas (HCAs) and HCCs and its targetability in novel therapies. In this article, we review the role of the β-catenin pathway in hepatocarcinogenesis and progression from chronic inflammation to HCC, the novel potential treatments targeting the pathway and its prognostic role in HCC patients, as well as the imaging features of HCC and their association with aberrant activation of the pathway ...
β-Catenin and Acetylcholine Receptor Clustering. Bin Zhang, Shiwen Luo, Xian-Ping Dong, Xian Zhang, Chunming Liu, Zhenge Luo, Wen-Cheng Xiong, and Lin Mei. (see pages 3968-3973). Its a story that has touched the careers of many neuroscientists: the clustering of acetylcholine receptors (AChRs) at the neuromuscular junction. This week, Zhang et al. add β-catenin to a list of molecular characters that already includes agrin, rapysn, and MuSK (muscle-specific tyrosine kinase). The authors found β-catenin in a two-hybrid screen using rapsyn as bait. They confirmed that the interaction was direct, and that β-catenin coprecipitated with AChR complexes in control myotubes, but not in myotubes derived from rapsyn−/− mice. In a nicely controlled set of experiments, suppression of β-catenin by a short hairpin RNA reduced agrin-induced clustering of AChRs in C2C12 myoblasts. Although β-catenin is multifunctional, its action here did not involve the Wnt signaling pathway. Rather, an interaction ...
Background Many cancerous cells accumulate β-catenin in the nucleus. We examined the role of epidermal growth factor receptor (EGFR) signaling in the accumulation of β-catenin in the nuclei of oral...
Development of the cerebellum proceeds under the precise spatio-temporal control of several key developmental signalling pathways, including the Wnt/β-catenin pathway. We recently reported the activity of Wnt/β-catenin signalling in the perinatal c
Classical cadherins mediate Ca2+-dependent intercellular adhesion and are essential for tissue morphogenesis and maintenance. They are key components of adherens junctions (AJs). In vitro studies in simple epithelial cells indicated an essential role for E-cadherin not only in the formation of AJs but also other intercellular contacts, such as desmosomes and tight junctions. In contrast, in vivo tissue specific knockout studies did not reveal a necessity of E-cadherin in the formation of intercellular junctions, raising the question if classical cadherins are necessary or if other classical cadherins can compensate for the loss of E-cadherin. Therefore, the aim of this thesis was to ask how E-cadherin regulates tight junctions and if E-cadherin has a specific function in the formation of tight junctions. In addition, the question was asked if classical cadherin function is necessary for the formation of other intercellular contacts, such as desmosomes. Using primary keratinocytes as a model for ...
E-cadherin-mediated cell-cell adhesion is critical for naive pluripotency of cultured mouse embryonic stem cells (mESCs). E-cadherin-depleted mESC fail to downregulate their pluripotency program and are unable to initiate lineage commitment. To further explore the roles of cell adhesion molecules during mESC differentiation, we focused on p120 catenin (p120ctn). Although one key function of p120ctn is to stabilize and regulate cadherin-mediated cell-cell adhesion, it has many additional functions, including regulation of transcription and Rho GTPase activity. Here, we investigated the role of mouse p120ctn in early embryogenesis, mESC pluripotency and early fate determination. In contrast to the E-cadherin-null phenotype, p120ctn-null mESCs remained pluripotent, but their in vitro differentiation was incomplete. In particular, they failed to form cystic embryoid bodies and showed defects in primitive endoderm formation. To pinpoint the underlying mechanism, we undertook a structure-function approach.
TY - JOUR. T1 - Ras farnesylation inhibitor FTI-277 restores the E-cadherin/catenin cell adhesion system in human cancer cells and reduces cancer metastasis. AU - Nam, Jeong Seok. AU - Ino, Yoshinori. AU - Sakamoto, Michiie. AU - Hirohashi, Setsuo. PY - 2002/9/1. Y1 - 2002/9/1. N2 - The E-cadherin/catenin cell adhesion system is often down-regulated in epithelial tumors. This is thought to play an important role in cancer invasion and metastasis, and restoration of this system may suppress metastatic spread of cancer. In this study, the effects of a Ras farnesylation inhibitor (FTI-277) on E-cadherin-mediated cell-cell adhesion and metastatic potential were examined. In cell aggregation assays, FTI-277 stimulated aggregation of colon, liver and breast cancer cells. In vitro cultures of cancer cells showed that FTI-277 induced strong cell-cell contact. Immunoblotting analysis showed that FTI-277 increased E-cadherin/catenin (α, β and γ) expression and strongly stabilized E-cadherin/catenin ...
The RNA-binding protein Sam68 regulates expression and transcription function of the androgen receptor splice variant AR-V7. Stockley J, Markert E, Zhou Y, Robson CN, Elliott DJ, Lindberg J, Leung HY*, Rajan P*. Sci Rep. 2015; 5:13426 PMID: 26310125 *Equal contributors. The RNA-binding protein hnRNPA2 regulates β-catenin protein expression and is over-expressed in prostate cancer. Stockley J, Villasevil MEM, Nixon C, Ahmad I, Leung HY*, Rajan P*. RNA Biol. 2014; 11(6) PMID: 24823909*Equal contributors. Next-generation Sequencing of Advanced Prostate Cancer Treated with Androgen-deprivation Therapy. Rajan P*, Sudbery IM*, M. Eugenia M. Villasevil MEM, Mui E, Fleming J, Davis M, Ahmad I, Edwards J, Sansom OJ, Sims D, Ponting CP, Heger A, McMenemin RM, Pedley ID, Leung HY. Eur Urol. 2014; 66(1):32-9 PMID: 24054872 *Equal contributors. The RNA-binding and adaptor protein Sam68 modulates signal-dependent splicing and transcriptional activity of the androgen receptor. Rajan P*, Gaughan L*, Dalgliesh ...
Costa, M., et al. (1998). A putative catenin-cadherin system mediates morphogenesis of the Caenorhabditis elegans embryo. J. Cell Biol. 141(1): 297-308 Coste, A. L., et al. (1998). Somatic mutations of the beta-catenin gene are frequent in mouse and human hepatocellular carcinomas. Proc. Natl. Acad. Sci. 95(15): 8847-8851 Cox, R. T., Kirkpatrick, C. and Peifer, M. (1996), Armadillo is required for adherens junction assembly, cell polarity and morphogenesis during Drosophila embryogenesis. J. Cell Biol. 134: 133-148 Cox, R. T., et al. (1999). Membrane-tethered Drosophila Armadillo cannot transduce Wingless signal on its own. Development 126: 1327-1335 Cox, R. T., et al. (2000). A screen for mutations that suppress the phenotype of Drosophila armadillo, the ß-catenin homolog. Genetics 155: 1725-1740 Daniels, D. L. and Weis, W. I. (2002). ICAT inhibits ß-Catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules. Molec. Cell 10: ...
Methods A controlled impact model of TBI was established using Feeneys free-drop method. Seventy-eight Sprague-Dawley rats were randomly divided into the following three groups: a normal group (n=18) that was left untreated; a model group (n=30) that received no treatment after TBI; and an acupuncture group (n=30) that received acupuncture (at LI4, GV20, GV26 and GV16) after TBI. Rats in each group were randomly and equally divided into 3-day, 7-day and 14-day subgroups according to the duration of therapy. Real-time fluorescence quantitative PCR (RT-qPCR) was used to measure mRNA expression of Wnt3a, β-catenin and Sox2. Western blots were performed to determine the expression levels of WNT3a, β-Catenin and SOX2. ...

Catenin - WikipediaCatenin - Wikipedia

α-catenin β-catenin δ-catenin γ-catenin All but α-catenin contain armadillo repeats. Several types of catenins work with N- ... The first two catenins that were identified became known as α-catenin and β-catenin. A-catenin can bind to β-catenin and can ... B-catenin binds the cytoplasmic domain of some cadherins. Additional catenins such as γ-catenin and δ-catenin have been ... Most studies investigating catenin actions focus on α-catenin and β-catenin. β-catenin is particularly interesting as it plays ...
more infohttps://en.wikipedia.org/wiki/Catenin

CTNNA1 - Catenin alpha-1 - Homo sapiens (Human) - CTNNA1 gene & proteinCTNNA1 - Catenin alpha-1 - Homo sapiens (Human) - CTNNA1 gene & protein

Catenin alpha-1Imported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p>,a ... tr,E5RJP7,E5RJP7_HUMAN Catenin alpha-1 (Fragment) OS=Homo sapiens GN=CTNNA1 PE=1 SV=1 ...
more infohttp://www.uniprot.org/uniprot/E5RJP7

Catenin Family Genes Are Not Commonly Mutated in Hereditary Diffuse Gastric Cancer | Cancer Epidemiology, Biomarkers &...Catenin Family Genes Are Not Commonly Mutated in Hereditary Diffuse Gastric Cancer | Cancer Epidemiology, Biomarkers &...

Catenin Family Genes Are Not Commonly Mutated in Hereditary Diffuse Gastric Cancer. Johanna M. Schuetz, Stephen Leach, Pardeep ... Catenins interact closely with E-cadherin molecules in cells, and are therefore logical candidate genes for mutation screening ... Conclusion: Catenin genes are not commonly mutated in non-CDH1 HDGC families. ... Methods: Affected individuals from 22 CDH1 mutation-negative families were screened for germline mutations in four catenin ...
more infohttp://cebp.aacrjournals.org/content/early/2012/11/14/1055-9965.EPI-12-1110.long

Catenin Family Genes Are Not Commonly Mutated in Hereditary Diffuse Gastric Cancer. - Canadas Michael Smith Genome Sciences...Catenin Family Genes Are Not Commonly Mutated in Hereditary Diffuse Gastric Cancer. - Canada's Michael Smith Genome Sciences...

Catenins interact closely with E-cadherin molecules in cells, and are therefore logical candidate genes for mutation screening ... Catenin genes are not commonly mutated in non-CDH1 HDGC families.Impact: Germline mutations in CTNNA1, CTNNB1, JUP, or CTNND1 ... Affected individuals from 22 CDH1 mutation-negative families were screened for germline mutations in four catenin genes: CTNNA1 ... You are here: Home / Platforms / Scientific Publications / Catenin Family Genes Are Not Commonly Mutated in Hereditary Diffuse ...
more infohttp://www.bcgsc.ca/platform/publications/catenin-family-genes-are-not-commonly-mutated-in-hereditary-diffuse-gastric-cancer

CTNNB1 catenin (cadherin-associated protein), beta 1 and formation of branching point structures beta-catenin / LEF...CTNNB1 catenin (cadherin-associated protein), beta 1 and formation of branching point structures beta-catenin / LEF...

... catenin) cadherins (the (CDH1) E-cadherin/catenin complex) include the beta-catenins a multifunctional molecule Locus: 3p22.1 ... binds with E-cadherin but not with beta-catenin. Which interacts with (Tcf-T-cell factor where a… ... Catenin Beta 1, CTNNB are cell adhesion molecules called (p120*␠- ... Catenin Beta 1, CTNNB are cell adhesion molecules called (p120*␠-catenin) cadherins (the (CDH1) E-cadherin/catenin complex) ...
more infohttps://faroucheombre.wordpress.com/2012/03/25/ctnnb1-catenin-cadherin-associated-protein-beta-1-and-formation-of-branching-point-structures-beta-catenin-lef-demonstrating-nucleation-at-tbe1-site-tcf7l2/

Institute of Cancer Research Repository -  beta-Catenin pathway activation in breast cancer is associated with triple-negative...Institute of Cancer Research Repository - beta-Catenin pathway activation in breast cancer is associated with triple-negative...

... and to determine whether aberrant beta-catenin expression is driven by CTNNB1 (beta-catenin encoding gene) activating mutations ... ALPHA-CATENIN; GAMMA-CATENIN; CYCLIN D1; EXPRESSION; CARCINOMAS. ... beta-Catenin pathway activation in breast cancer is associated ... In conclusion, beta-catenin/Wnt pathway activation is preferentially found in triple-negative/basal-like breast carcinomas, is ... Aberrant beta-catenin expression as determined by assessment of its subcellular localization constitutes a surrogate marker of ...
more infohttp://publications.icr.ac.uk/10393/

Order US Biologicals Anti-Catenin, beta (Beta Catenin, Cadherin-associated Protein, Catenin beta 1, Catenin beta-1, CATNB,...Order US Biological's Anti-Catenin, beta (Beta Catenin, Cadherin-associated Protein, Catenin beta 1, Catenin beta-1, CATNB,...

Beta Catenin, Cadherin-associated Protein, Catenin beta 1, Catenin beta-1, CATNB, CTNNB, CTNNB1) SKU: C2069-51C() ... Anti-Catenin, beta (Beta Catenin, Cadherin-associated Protein, Catenin beta 1, Catenin beta-1, CATNB, CTNNB, CTNNB1) SKU: C2069 ... Anti-Catenin, beta (Beta Catenin, Cadherin-associated Protein, Catenin beta 1, Catenin beta-1, CATNB, CTNNB, CTNNB1) ... Catenin beta is an adherens junction protein and has a role in the regulation of cell adhesion and in signal transduction ...
more infohttps://zageno.com/p/anti-catenin-beta-beta-catenin-cadherin-associated-protein-catenin-beta-1-catenin-beta-1-catnb-ctnnb-ctnnb1-sku-c2069-51c/2930012/3540615/13489339

CTNNA1 Gene - GeneCards | CTNA1 Protein | CTNA1 AntibodyCTNNA1 Gene - GeneCards | CTNA1 Protein | CTNA1 Antibody

Catenin Alpha 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene ... catenin adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-catenin/JUP; the complex is located to ... An α-E-catenin (CTNNA1) mutation in hereditary diffuse gastric cancer. (PMID: 23208944) Majewski IJ … Bernards R (The Journal ... Loss of alpha-catenin decreases the strength of single E-cadherin bonds between human cancer cells. (PMID: 19458087) Bajpai S ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=CTNNA1

Transient and Steady-State Effects of Shear Stress on Endothelial Cell Adherens Junctions | Circulation ResearchTransient and Steady-State Effects of Shear Stress on Endothelial Cell Adherens Junctions | Circulation Research

... staining for α-catenin (d) and β-catenin (e) became punctate and sparse, and in the case of β-catenin occurred only along cell ... β-catenin and plakoglobin (γ-catenin) are members of the armadillo family of proteins that link cadherins to α-catenin, a ... and goat polyclonal antibodies to human αE-catenin, β-catenin, and γ-catenin (Santa Cruz Biotechnology, Inc). Secondary ... Cells were double stained for α-catenin (a, d, g, and j), β-catenin (b, e, h, and k), or plakoglobin (c, f, i, and l) and F- ...
more infohttp://circres.ahajournals.org/content/85/6/504

Beta-Catenin | SpringerLinkBeta-Catenin | SpringerLink

Catenin beta; Catnb; Ctnnb; CTNNB1 Beta-catenin (β-catenin) (Armadillo in Drosophila) is a multifunctional protein involved in ... Catenin (cadherin-associated protein), beta 1 (88kD); Catenin beta; Catnb; Ctnnb; CTNNB1 ... Beta-catenin (β-catenin) (Armadillo in Drosophila) is a multifunctional protein involved in two essential cellular events: cell ... 2009). At cell-cell adhesion junctions, β-catenin interacts with type-I cadherins and α-catenin, which in turn associates with ...
more infohttps://link.springer.com/referenceworkentry/10.1007%2F978-3-319-67199-4_528

Beta-catenin (IPR013284) | InterPro | EMBL-EBIBeta-catenin (IPR013284) | InterPro | EMBL-EBI

Beta-catenin (IPR013284). Short name: Beta-catenin Family relationships *Beta-catenin (IPR013284) *Junction plakoglobin/protein ... Beta-catenin forms a cadherin/beta-catenin/alphaE-catenin complex that can tether the tripartite adhesion complex and regulate ... The beta-catenin structure has been determined [PMID: 9298899, PMID: 11136974]. Beta catenin family proteins contain several ... α-catenin, vinculin, and F-actin in strengthening E-cadherin cell-cell adhesions and mechanosensing.. Cell Adh Migr 7 345-50 ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR013284

Catenins
     Summary Report | CureHunterCatenins Summary Report | CureHunter

Catenins: A family of cytoskeletal proteins that play essential roles in CELL ADHESION at ADHERENS JUNCTIONS by linking ... Catenins. Subscribe to New Research on Catenins A family of cytoskeletal proteins that play essential roles in CELL ADHESION at ... 11/01/1995 - "This study examined the effects of n-6 PUFAs on the expression of catenins in a range of human cancer cells by ... 01/01/1998 - "We found that, although alteration is common in the catenins and E-cadherin, complete loss, as exemplified by E- ...
more infohttp://www.curehunter.com/public/keywordSummaryD051177-Catenins.do

Catenin beta-1 (Q02248) | InterPro | EMBL-EBICatenin beta-1 (Q02248) | InterPro | EMBL-EBI

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
more infohttp://www.ebi.ac.uk/interpro/protein/Q02248

Destroying β-Catenin | Science SignalingDestroying β-Catenin | Science Signaling

J. Liu, J. Stevens, C. A. Rote, H. J. Yost, Y. Hu, K. L. Neufeld, R. L. White, N. Matsunami, Siah-1 mediates a novel β-catenin ... SIP was found to bind to a protein called Ebi, which not only binds to β-catenin, but targets it to an E3 ubiquitinase complex ... Liu et al. report that Siah-1 also interacts with APC, which is required for Siah-1-dependent degradation of β-catenin. This ... Matsuzawa and Reed show that a mammalian protein called Siah-1 lies at the hub of another pathway that destroys β-catenin in ...
more infohttps://stke.sciencemag.org/content/2001/85/tw6

Inhibition of RhoA by p120 catenin.  - PubMed - NCBIInhibition of RhoA by p120 catenin. - PubMed - NCBI

Inhibition of RhoA by p120 catenin.. Anastasiadis PZ1, Moon SY, Thoreson MA, Mariner DJ, Crawford HC, Zheng Y, Reynolds AB. ... The catenin p120 has also been implicated in cadherin clustering through an unknown mechanism. Here we show that p120 ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/10980705?dopt=Abstract

The p120 Catenin Shuffle | Science SignalingThe p120 Catenin Shuffle | Science Signaling

It has not been clear how the cytoplasmic protein p120 catenin regulates cell motility. Overexpression of p120 catenin in ... Noren et al. now report that, when in the cytoplasm, p120 catenin binds to Vav2, an exchange factor that activates Cdc42 and ... Noren, N.K., Liu, B.P., Burridge, K., and Kreft, B. (2000) p120 catenin regulates the actin cytoskeleton via Rho family GTPases ... The authors suggest that the distribution of p120 catenin between the cadherin-bound state and the cytoplasmic pool is ...
more infohttps://stke.sciencemag.org/content/2000/45/tw4.abstract

beta Catenin Antibody
                
                
		        
	beta Catenin Antibody

beta Catenin Polyclonal Antibody from Invitrogen for Western Blot, Immunofluorescence, Immunocytochemistry, ... Protein Aliases: beta catenin; Beta-catenin; catenin; catenin (cadherin associated protein), beta 1, 88kDa; catenin (cadherin- ... Catenin beta-1; CATNB; CTNB1; CTNNB Gene Aliases: armadillo; B-catenin; beta-catenin; Bfc; Catnb; CHBCAT; CTNNB; CTNNB1; ctnnb1 ... Beta-catenin interacts with the cytoplasmic domain of E-cadherin and links E-cadherin to alpha-catenin, which in turn mediates ...
more infohttps://www.thermofisher.com/antibody/product/beta-Catenin-Antibody-Polyclonal/PA5-16762

Wnt/β-catenin signaling and disease.  - PubMed - NCBIWnt/β-catenin signaling and disease. - PubMed - NCBI

Wnt/β-catenin signaling and disease.. Clevers H1, Nusse R.. Author information. 1. Hubrecht Institute, KNAW and University ... In this Review, we provide an update of the core Wnt/β-catenin signaling pathway, discuss how its various components contribute ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/22682243?dopt=Abstract

Multiple oncogenic roles of nuclear β-catenin | SpringerLinkMultiple oncogenic roles of nuclear β-catenin | SpringerLink

Cellular β-catenin exists in three different pools: membranous, cytoplasmic and nuclear. In... ... "β-Catenin is essential for embryonic development and required for cell renewal/regeneration in adult life. ... p120 Catenin-associated Fer and Fyn tyrosine kinases regulate β-catenin Tyr-142 phosphorylation and beta-Catenin-alpha-Catenin ... Pokutta S and Weis WI 2000 Structure of the dimerization and beta-catenin-binding region of alpha-catenin. Mol. Cell 5 533-543 ...
more infohttps://link.springer.com/article/10.1007/s12038-017-9710-9

Beta-Catenin Antibody (Dako Omnis) | AgilentBeta-Catenin Antibody (Dako Omnis) | Agilent

Beta-catenin is also involved in the regulation of gene expression as a mediator of the Wnt signaling pathway. The expression ... Beta-catenin is an 88 kDa multifunctional protein playing an essential role in cell-cell adhesion by binding to the ... and intracellular localization of beta-catenin is altered in many types of cancers. ... Clone β-Catenin-1 Beta-catenin is an 88 kDa multifunctional protein playing an essential role in cell-cell adhesion by binding ...
more infohttps://www.agilent.com/en/product/immunohistochemistry/antibodies-controls/primary-antibodies/beta-catenin-

Catenin alpha Antibodies: Novus BiologicalsCatenin alpha Antibodies: Novus Biologicals

Browse our Catenin alpha Antibody catalog backed by our Guarantee+. ... Catenin alpha Antibodies. We offer Catenin alpha Antibodies for use in common research applications: Immunohistochemistry, ... Our Catenin alpha Antibodies can be used in a variety of model species: Human, Mouse, Xenopus. Use the list below to choose the ... Each Catenin alpha Antibody is fully covered by our Guarantee+, to give you complete peace of mind and the support when you ...
more infohttps://www.novusbio.com/primary-antibodies/catenin-alpha?facet_conjugate=PE

Catenin alpha Antibodies: Novus BiologicalsCatenin alpha Antibodies: Novus Biologicals

Browse our Catenin alpha Antibody catalog backed by our Guarantee+. ... Catenin alpha Antibodies. We offer Catenin alpha Antibodies for use in common research applications: Immunohistochemistry, ... Our Catenin alpha Antibodies can be used in a variety of model species: Human, Mouse, Xenopus. Use the list below to choose the ... Each Catenin alpha Antibody is fully covered by our Guarantee+, to give you complete peace of mind and the support when you ...
more infohttps://www.novusbio.com/primary-antibodies/catenin-alpha?facet_conjugate=Janelia%20Fluor%20549

β-Cateninβ-Catenin

CTNNB; catenin (cadherin-associated protein), beta 1 (88kD); catenin (cadherin-associated protein), beta 1, 88kDa; catenin beta ... Catenin (cadherin-associated protein), beta 1 (CTNNB1). Target Class. Pathway. Family. Wnt-Frizzled signalling. Official Symbol ... β-Catenin. Species. Human. Accession Number. NM_001904. Alias Names. ...
more infohttps://www.discoverx.com/target-data-sheets/pathways/%CE%B2-catenin

Evolution and diversity of cadherins and cateninsEvolution and diversity of cadherins and catenins

Its cytoplasmic tail interacts with the armadillo catenins, p120 and β-catenin. Further, α-catenin links the cadherin/armadillo ... Moreover, a large expansion of the cadherin and catenin families coincides with the emergence of vertebrates and reflects a ... Here, we revisit and review the functions, phylogenetic classifications and co-evolution of the cadherin and catenin protein ... catenin complex to the actin filament network. Even genomes of ancestral metazoan species such as cnidarians and placozoans ...
more infohttps://insights.ovid.com/pubmed?PMID=28268172

β-Catenin regulates excitatory postsynaptic strength at hippocampal synapses | PNASβ-Catenin regulates excitatory postsynaptic strength at hippocampal synapses | PNAS

A) Schematic diagram of β-catenin deletion mutants. (B) Interaction of β-catenin deletion mutants with N-cadherin or αN-catenin ... when WT or mutant β-catenin was coexpressed with αN-catenin in HEK293 cells, ΔN and L132A did not bind to αN-catenin, whereas ... 4 A). We first tested the binding of β-catenin mutants to N-cadherin by expressing the epitope-tagged WT or mutant β-catenin ... 4 B). We also tested the two N-terminal domain β-catenin mutants, ΔN and L132A, for their interaction with α-catenin. The ΔN ...
more infohttps://www.pnas.org/content/104/33/13479?ijkey=662ea73227b9ed09848f61e2df5f98c4f5b0622c&keytype2=tf_ipsecsha
  • Secondly, β-catenin participates in the Wnt signaling pathway as a downstream target. (wikipedia.org)
  • While the pathway is very detailed and not completely understood, in general, when Wnt is not present, GSK-3B (a member of the pathway) is able to phosphorylate β-catenin as a result of a complex formation that includes β-catenin, AXIN1, AXIN2, APC (a tumor suppressor gene product), CSNK1A1, and GSK3B. (wikipedia.org)
  • For instance, when an epithelial layer is complete and the adherens junctions indicate that the cell is surrounded, β-catenin may play a role in telling the cell to stop proliferating, as there is no room for more cells in the area. (wikipedia.org)
  • These gene products are important in determining cell fates during normal development and in maintaining homeostasis, or they can lead to de-regulated growth in disorders like cancer by responding to mutations in β-catenin, APC or Axin, each of which can lead to this de-regulated β-catenin level stabilization in cells. (wikipedia.org)
  • Following phosphorylation of the N-terminal Ser and Thr residues of β-catenin, BTRC promotes its ubiquitination, which causes it to be degraded by the TrCP/SKP complex. (wikipedia.org)
  • At this point, β-catenin becomes a coactivator for TCF and LEF to activate Wnt genes by displacing Groucho and HDAC transcription repressors. (wikipedia.org)
  • Mice engineered to specifically have vascular endothelium cells deficient in β-catenin showed disrupted adhesion between vascular endothelial cells. (wikipedia.org)
  • however, it is likely that α-catenin acts in concert with vinculin to bind to actin and help stabilize the junctions. (wikipedia.org)
  • While less attention is directed at α-catenin in studies involving cell adhesion, it is nonetheless an important player in cellular organization, function and growth. (wikipedia.org)
  • Eventually, some of this accumulated β-catenin will move into the nucleus with the help of Rac1. (wikipedia.org)
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