alpha Catenin
Cytoskeletal Proteins
Cadherins
Catenins
L Cells (Cell Line)
beta Catenin
gamma Catenin
Desmoplakins
Adherens Junctions
alpha 1-Antitrypsin
Cell Adhesion Molecules
The alphaE-catenin gene (CTNNA1) acts as an invasion-suppressor gene in human colon cancer cells. (1/431)
The acquisition of invasiveness is a crucial step in the malignant progression of cancer. In cancers of the colon and of other organs the E-cadherin/catenin complex, which is implicated in homotypic cell-cell adhesion as well as in signal transduction, serves as a powerful inhibitor of invasion. We show here that one allele of the alphaE-catenin (CTNNA1) gene is mutated in the human colon cancer cell family HCT-8, which is identical to HCT-15, DLD-1 and HRT-18. Genetic instability, due to mutations in the HMSH6 (also called GTBP) mismatch repair gene, results in the spontaneous occurrence of invasive variants, all carrying either a mutation or exon skipping in the second alphaE-catenin allele. The alphaE-catenin gene is therefore, an invasion-suppressor gene in accordance with the two-hit model of Knudsen for tumour-suppressor genes. (+info)Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin. (2/431)
ZO-2, a member of the MAGUK family, was thought to be specific for tight junctions (TJs) in contrast to ZO-1, another MAGUK family member, which is localized at TJs and adherens junctions (AJs) in epithelial and nonepithelial cells, respectively. Mouse ZO-2 cDNA was isolated, and a specific polyclonal antibody was generated using corresponding synthetic peptides as antigens. Immunofluorescence microscopy with this polyclonal antibody revealed that, similarly to ZO-1, in addition to TJs in epithelial cells, ZO-2 was also concentrated at AJs in nonepithelial cells such as fibroblasts and cardiac muscle cells lacking TJs. When NH2-terminal dlg-like and COOH-terminal non-dlg-like domains of ZO-2 (N-ZO-2 and C-ZO-2, respectively) were separately introduced into cultured cells, N-ZO-2 was colocalized with endogenous ZO-1/ZO-2, i.e. at TJs in epithelial cells and at AJs in non-epithelial cells, whereas C-ZO-2 was distributed along actin filaments. Consistently, occludin as well as alpha catenin directly bound to N-ZO-2 as well as the NH2-terminal dlg-like portion of ZO-1 (N-ZO-1) in vitro. Furthermore, immunoprecipitation experiments revealed that the second PDZ domain of ZO-2 was directly associated with N-ZO-1. These findings indicated that ZO-2 forms a complex with ZO-1/occludin or ZO-1/alpha catenin to establish TJ or AJ domains, respectively. (+info)Cadherin-11 is expressed in invasive breast cancer cell lines. (3/431)
In several cancers, including breast cancer, loss of E-cadherin expression is correlated with a loss of the epithelial phenotype and with a gain of invasiveness. Cells that have lost E-cadherin expression are either poorly invasive with a rounded phenotype, or highly invasive, with a mesenchymal phenotype. Most cells lacking E-cadherin still retain weak calcium-dependent adhesion, indicating the presence of another cadherin family member. We have now examined the expression of the mesenchymal cadherin, cadherin-11, in breast cancer cell lines. Cadherin-11 mRNA and protein, as well as a variant form, are expressed in the most invasive cell lines but not in any of the noninvasive cell lines. Cadherin-11 is localized to a detergent-soluble pool and is associated with both alpha- and beta-catenin. Immunocytochemistry shows that cadherin-11 is localized to the cell membrane at sites of cell-cell contact as well as at lamellipodia-like projections, which do not interact with other cells. These results suggest that cadherin-11 expression may be well correlated with the invasive phenotype in cancer cells and may serve as a molecular marker for the more aggressive, invasive subset of tumors. Cadherin-11 may mediate the interaction between malignant tumor cells and other cell types that normally express cadherin-11, such as stromal cells or osteoblasts or perhaps even with the surrounding extracellular matrix, thus facilitating tumor cell invasion and metastasis. (+info)Functional domains of alpha-catenin required for the strong state of cadherin-based cell adhesion. (4/431)
The interaction of cadherin-catenin complex with the actin-based cytoskeleton through alpha-catenin is indispensable for cadherin-based cell adhesion activity. We reported previously that E-cadherin-alpha-catenin fusion molecules showed cell adhesion and cytoskeleton binding activities when expressed in nonepithelial L cells. Here, we constructed deletion mutants of E-cadherin-alpha-catenin fusion molecules lacking various domains of alpha-catenin and introduced them into L cells. Detailed analysis identified three distinct functional domains of alpha-catenin: a vinculin/alpha-actinin-binding domain, a ZO-1-binding domain, and an adhesion-modulation domain. Furthermore, cell dissociation assay revealed that the fusion molecules containing the ZO-1-binding domain in addition to the adhesion-modulation domain conferred the strong state of cell adhesion activity on transfectants, although those lacking the ZO-1-binding domain conferred only the weak state. The disorganization of actin-based cytoskeleton by cytochalasin D treatment shifted the cadherin-based cell adhesion from the strong to the weak state. In the epithelial cells, where alpha-catenin was not precisely colocalized with ZO-1, the ZO-1-binding domain did not completely support the strong state of cell adhesion activity. Our studies showed that the interaction of alpha-catenin with the actin-based cytoskeleton through the ZO-1-binding domain is required for the strong state of E-cadherin-based cell adhesion activity. (+info)Different behavior of l-afadin and neurabin-II during the formation and destruction of cell-cell adherens junction. (5/431)
We have recently isolated two novel actin filament-binding proteins, l-afadin and neurabin-II and shown that they are localized at cell-cell adherens junction (AJ) in epithelial cells. We found here that l-afadin, neurabin-II, ZO-1, and E-cadherin showed similar and different behavior during the formation and destruction of cell-cell AJ in MDCK cells. In MDCK cells, the accumulation of both l-afadin and E-cadherin, but not that of ZO-1, changed in parallel depending on Rac small G protein activity. Dissociation of MDCK cells by culturing the cells at 2 microM Ca2+ caused rapid endocytosis of E-cadherin, but not that of l-afadin or ZO-1. Addition of phorbol 12-myristate 13-acetate to these dissociated cells formed a tight junction-like structure where ZO-1 and l-afadin, but not neurabin-II or E-cadherin, accumulated. We furthermore found that, in non-epithelial EL cells, which expressed E-cadherin and attached to each other, l-afadin, neurabin-II, ZO-1 and E-cadherin were all localized at AJ. In cadherin-deficient L cells, I-afadin was mainly localized at cell-cell contact sites, but ZO-1 was mainly localized at the tip area of cell processes. Neurabin-II did not accumulate at the plasma membrane area. Neither l-afadin nor neurabin-II significantly interacted with alpha-, beta-catenin, E-cadherin, ZO-1 or occludin. (+info)Cell-extracellular matrix interactions and EGF are important regulators of the basal mammary epithelial cell phenotype. (6/431)
The mammary epithelium is composed of a luminal epithelium and a basal layer containing myoepithelial cells and undifferentiated precursors. Basal cells express specific protein markers, such as keratin 14 (K14) and P-cadherin. To study the factors that regulate the basal mammary epithelial cell phenotype, we have established two clonal derivatives of the mouse HC11 cell line, BC20 and BC44, expressing high levels of K14 and P-cadherin. Unlike the parental HC11 cells, these basal cells did not produce beta-casein in response to lactogenic hormone treatment; however their phenotype appeared to be plastic. Cultured in EGF-free medium, they exhibited enhanced cell-extracellular matrix adhesions and deficient cell-cell junctions, whereas long-term treatment with EGF induced a decrease of focal contact number and establishment of cell-cell junctions, resulting in downregulation of K14 and P-cadherin expression at the protein and mRNA levels. To determine whether cell-extracellular matrix interactions mediated by integrins have a role in the regulation of the expression of K14 and P-cadherin, the amounts of transcripts for the two proteins were analysed in the basal cells, which were plated on the function-blocking antibodies against beta1 and alpha6 integrin chains, on fibronectin and on laminin 5. The amount of P-cadherin transcript was 2- to 4-fold higher in cells plated on the function-blocking anti-integrin antibodies and on the extracellular matrix proteins, as compared to cells plated on poly-L-lysine, whereas the K14 transcript levels were not significantly modified in response to adhesion. The data demonstrate that integrin-mediated cell interaction with extracellular matrix is directly implicated in the control of P-cadherin expression, and that EGF and cell-extracellular matrix adhesion events are important regulators of the basal mammary epithelial cell phenotype. (+info)Rearrangement of adherens junctions by transforming growth factor-beta1: role of contraction. (7/431)
The signal transduction pathways that lead to disruption of pulmonary endothelial monolayer integrity by transforming growth factor-beta1 (TGF-beta1) have not been elucidated. The purpose of this investigation was to determine whether disassembly of the adherens junction is temporally associated with the TGF-beta1-induced decrease in pulmonary endothelial monolayer integrity. Measurement of albumin clearance and electrical resistance showed that monolayer integrity started to decrease between 1 and 2 h post-TGF-beta1 treatment and continued to slowly decrease over the next 6 h. Immunofluorescence microscopy of monolayers between 2 and 3 h post-TGF-beta1 showed that beta-catenin, plakoglobin, alpha-catenin, and cadherin-5 were colocalized both at the cell periphery and in newly formed bands that are perpendicular to the cell-cell border. At 4 h post-TGF-beta1, cells began separating; however, beta- and alpha-catenin, plakoglobin, and cadherin-5 could still be found at the cell periphery at areas of cell separation and in strands between separated cells. By 8 h, these junctional proteins were no longer present at the cell periphery at areas of cell separation. The myosin light chain kinase inhibitor KT-5926 prevented the TGF-beta1-induced change in integrity but did not inhibit the formation of actin stress fibers or the formation of bands containing adherens junction proteins that were perpendicular to the cell-cell junction. Overall, these results suggest that adherens junction disassembly occurs after cell separation during TGF-beta1-induced decreases in pulmonary endothelial monolayer integrity and that the loss of integrity may be due to the activation of a myosin light chain kinase-dependent signaling cascade. (+info)E-cadherin and alpha-, beta- and gamma-catenin expression in prostate cancers: correlation with tumour invasion. (8/431)
The E-cadherin-catenin complex plays an important role in establishing and maintaining intercellular connections and morphogenesis and reduced expression of its constituent molecules is associated with invasion and metastasis. In the present study, we examined E-cadherin and alpha-, beta- and gamma-catenin levels in tumour tissues obtained by radical prostatectomy in order to investigate the relationship with histopathological tumour invasion. Immunohistochemical findings for 45 prostate cancer specimens demonstrated aberrant expression of each molecule to be associated with dedifferentiation and, in addition, alteration of staining patterns for the three types of catenin was significantly correlated with capsular but not lymphatic or vascular invasion. The data thus suggest that three types of catenin may be useful predictive markers for biological aggressiveness of prostate cancer. (+info)Alpha-catenin is a protein that plays a role in cell adhesion and the formation of tight junctions in cells. It is a component of the cadherin-catenin complex, which is responsible for mediating cell-cell adhesion. Alpha-catenin helps to link cadherins to the actin cytoskeleton, allowing cells to adhere to one another and maintain tissue integrity. In addition to its role in cell adhesion, alpha-catenin has been implicated in a number of other cellular processes, including cell signaling and the regulation of gene expression. Mutations in the alpha-catenin gene have been associated with various human diseases, including cancer.
Cytoskeletal proteins are a diverse group of proteins that make up the internal framework of cells. They provide structural support and help maintain the shape of cells. The cytoskeleton is composed of three main types of proteins: microfilaments, intermediate filaments, and microtubules. Microfilaments are the thinnest of the three types of cytoskeletal proteins and are composed of actin filaments. They are involved in cell movement, cell division, and muscle contraction. Intermediate filaments are thicker than microfilaments and are composed of various proteins, including keratins, vimentin, and desmin. They provide mechanical strength to cells and help maintain cell shape. Microtubules are the thickest of the three types of cytoskeletal proteins and are composed of tubulin subunits. They play a crucial role in cell division, intracellular transport, and the maintenance of cell shape. Cytoskeletal proteins are essential for many cellular processes and are involved in a wide range of diseases, including cancer, neurodegenerative disorders, and muscle diseases.
Cadherins are a family of transmembrane proteins that play a crucial role in cell-cell adhesion in the human body. They are responsible for the formation and maintenance of tissues and organs by linking neighboring cells together. There are over 20 different types of cadherins, each with its own unique function and distribution in the body. Cadherins are involved in a wide range of biological processes, including embryonic development, tissue repair, and cancer progression. In the medical field, cadherins are often studied as potential targets for therapeutic interventions. For example, some researchers are exploring the use of cadherin inhibitors to treat cancer by disrupting the adhesion between cancer cells and normal cells, which can help prevent the spread of the disease. Additionally, cadherins are being studied as potential biomarkers for various diseases, including cancer, cardiovascular disease, and neurological disorders.
Catenins are a family of proteins that play a crucial role in cell adhesion and signaling. They are composed of several subunits, including alpha, beta, gamma, delta, and epsilon catenins, which interact with each other to form a complex that links the cytoskeleton to the extracellular matrix. In the medical field, catenins are often studied in the context of cancer. Abnormalities in the expression or function of catenins have been linked to the development and progression of various types of cancer, including breast, colon, and prostate cancer. For example, mutations in the beta-catenin gene have been found in many cases of colorectal cancer, leading to increased cell proliferation and tumor growth. Catenins are also important for maintaining tissue integrity and regulating cell differentiation and migration. In addition, they play a role in the Wnt signaling pathway, which is involved in many developmental processes and has been implicated in various diseases, including cancer and neurodegenerative disorders.
Beta-catenin is a protein that plays a crucial role in the regulation of cell adhesion and signaling pathways in the body. In the medical field, beta-catenin is often studied in the context of cancer, as mutations in the beta-catenin gene (CTNNB1) can lead to the development of various types of cancer, including colorectal cancer, endometrial cancer, and ovarian cancer. In normal cells, beta-catenin is a component of the cadherin adhesion complex, which helps cells stick together and maintain tissue integrity. However, in cancer cells, mutations in the beta-catenin gene can lead to the accumulation of beta-catenin in the cytoplasm and nucleus, where it can activate downstream signaling pathways that promote cell proliferation and survival. Beta-catenin is also involved in the regulation of other cellular processes, such as cell migration, differentiation, and apoptosis. As such, it is a potential target for the development of new cancer therapies.
Gamma catenin, also known as gamma-catenin or plakoglobin, is a protein that plays a role in cell adhesion and signaling pathways in the mammalian body. It is a member of the catenin family of proteins, which are involved in the formation and maintenance of cell-cell adhesion complexes called adherens junctions. Gamma catenin is a multifunctional protein that interacts with other proteins, including alpha-catenin, beta-catenin, and cadherins, to form a complex that links the cadherin-catenin complex to the actin cytoskeleton. This complex is essential for the stability and function of adherens junctions, which are important for maintaining tissue integrity and regulating cell-cell communication. In addition to its role in cell adhesion, gamma catenin has also been implicated in a variety of cellular processes, including cell proliferation, differentiation, and migration. It has been implicated in the development and progression of several diseases, including cancer, and is a target for therapeutic intervention in some cases.
Desmoplakins are a group of proteins that are found in the desmosomes of epithelial cells. Desmosomes are specialized cell junctions that provide mechanical strength and stability to tissues, particularly in the skin and other epithelial tissues. Desmoplakins are important components of the desmosomal complex, which also includes cadherins, plakoglobins, and plakophilins. They are large, heavily glycosylated proteins that are synthesized in the endoplasmic reticulum and transported to the Golgi apparatus, where they are modified and packaged for transport to the cell membrane. Desmoplakins play a critical role in maintaining the structural integrity of epithelial tissues and are involved in a number of cellular processes, including cell adhesion, migration, and signaling. Mutations in desmoplakin genes have been associated with a number of human diseases, including epidermolysis bullosa simplex, a genetic disorder characterized by fragile skin that is prone to blistering.
Alpha 1-Antitrypsin (AAT) is a protein produced by the liver that plays a crucial role in protecting the lungs from damage caused by enzymes called proteases. Proteases are enzymes that break down proteins, and in the lungs, they can cause inflammation and damage to the airways and lung tissue. AAT acts as a protease inhibitor, binding to and neutralizing proteases that would otherwise cause damage to the lungs. It is particularly important in protecting the lungs from damage caused by cigarette smoke, air pollution, and other irritants. Deficiency in AAT can lead to a condition called alpha 1-antitrypsin deficiency, which is a genetic disorder that can cause lung disease, liver disease, and other health problems. People with alpha 1-antitrypsin deficiency produce low levels of AAT or produce AAT that is not functional, leading to an increased risk of lung damage and other health problems.
Cell adhesion molecules (CAMs) are proteins that mediate the attachment of cells to each other or to the extracellular matrix. They play a crucial role in various physiological processes, including tissue development, wound healing, immune response, and cancer progression. There are several types of CAMs, including cadherins, integrins, selectins, and immunoglobulin superfamily members. Each type of CAM has a unique structure and function, and they can interact with other molecules to form complex networks that regulate cell behavior. In the medical field, CAMs are often studied as potential targets for therapeutic interventions. For example, drugs that block specific CAMs have been developed to treat cancer, autoimmune diseases, and cardiovascular disorders. Additionally, CAMs are used as diagnostic markers to identify and monitor various diseases, including cancer, inflammation, and neurodegenerative disorders.
Catenin alpha-2
Catenin alpha-1
Catenin alpha-3
Catenin
Α-Catenin
Vinculin family
ZG16
CTNNAL1
CDH3 (gene)
P120 catenin
Masatoshi Takeichi
PTPRF
Cadherin-2
Protein dynamics
Cell adhesion
ALCAM
Epithelial polarity
Alpha-actinin-1
Cadherin
JUB (gene)
Plakoglobin
Catenin beta-1
Tight junction protein 1
PDLIM3
FYN
Cadherin-1
Cell junction
AKAP13
YES1
TCF7L2
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Signaling pathway3
- Hyperactivation of the Wnt/β-catenin signaling pathway due to mutations in its components initiates the majority of colorectal cancer (CRC) cases and promotes CRC development. (esmed.org)
- Wogonin induced G1 cell cycle arrest by regulating Wnt/β-catenin signaling pathway and inactivating CDK8 in human colorectal cancer carcinoma cells. (esmed.org)
- Weng X, Lin P, Liu F, et al: Achyranthes bidentata polysaccharides activate the Wnt/β-catenin signaling pathway to promote chondrocyte proliferation. (spandidos-publications.com)
Cadherin4
- 2006) Cdc42 regulates adherens junction stability and endothelial permeability by inducing alpha-catenin interaction with the vascular endothelial cadherin complex. (forth.gr)
- The head domain of vinculin associates to E-cadherin via α-, β - and γ -catenins. (wikidoc.org)
- It consists of 5 cadherin repeats (EC1 ~ EC5) in the extracellular domain, one transmembrane domain, and an intracellular domain that binds p120-catenin and beta-catenin . (wikidoc.org)
- The intracellular domain contains a highly- phosphorylated region vital to beta-catenin binding and therefore to E-cadherin function. (wikidoc.org)
Mediates1
- XTcf-3 transcription factor mediates β-catenin-induced axis formation in Xenopus embryos. (esmed.org)
Homology2
- Binding studies by surface plasmon resonance spectroscopy and peptide mapping combined with comparative homology modeling utilizing crystal structures led for the first time to a molecular model revealing the binding of both occludin and a-catenin to the same binding site in ZO-1. (fu-berlin.de)
- a-Catenin likewise consists of several four-helix bundles according to crystal structures and homology models. (fu-berlin.de)
Adherens5
- Die genauen Bereiche, Strukturen und molekularen Mechanismen der Wechselwirkung zwischen dem für die Zellverbindung wichtigen zona occludence Protein 1 (ZO-1) sowie dem tight junction Protein Occludin beziehungsweise dem adherens junction Protein a-Catenin sind unbekannt. (fu-berlin.de)
- Unsere Ergebnisse bestätigen das Konzept, dass ZO-1 nacheinander mit a-Catenin an den adherens junction und Occludin an den tight junction assoziiert. (fu-berlin.de)
- The exact sites, structures and molecular mechanisms of interaction between junction organizing zona occludence protein 1 (ZO-1) and the tight junction protein occludin or the adherens junction protein a-catenin are unknown. (fu-berlin.de)
- Our data support a concept that ZO-1 successively associates with a-catenin at the adherens junction and occludin at the tight junction. (fu-berlin.de)
- In conclusion, a common molecular mechanism of forming an intermolecular helical bundle between the hinge region/GUK domain of ZO-1 and a-catenin and occludin is identified as a general molecular principle organizing the association of ZO-1 at adherens and tight junctions. (fu-berlin.de)
Mutations1
- Mutations in beta catenin gene (CTNNB1) leads accumulation of the beta catenin protein in cytoplasm and nucleus in different type of tumors eg. (newmarketscientific.com)
Protein1
- The present results suggested that IL‑1β could decrease Col II expression and increase MMP‑13 expression at both the mRNA and protein levels, and also activate the Wnt/β‑catenin and NF‑κB signaling pathways in SW1353 cells. (spandidos-publications.com)
Gene3
- CTNNA3 (alpha-catenin) gene variants are associated with diisocyanate asthma: a replication study in a Caucasian worker population. (cdc.gov)
- This gene may regulate the signaling activity of beta-catenin and is required to maintain transcription of genes that control intracellular calcium cycling including ryanodine receptor 2, ankyrin-B, triadin, and calcium channel, voltage-dependent, L type, alpha 1C. (nih.gov)
- Liacini A, Sylvester J, Li WQ, Huang W, Dehnade F, Ahmad M and Zafarullah M: Induction of matrix metalloproteinase-13 gene expression by TNF-alpha is mediated by MAP kinases, AP-1, and NF-kappaB transcription factors in articular chondrocytes. (spandidos-publications.com)
Interaction1
- Functional interaction of β-catenin with the transcription factor LEF-1. (esmed.org)
Actin1
- Alpha-catenin participates in regulation of actin -containing cytoskeletal filaments. (wikidoc.org)
Regulation2
Gamma1
- Beta-Catenin is a member of catenin family together with alpha and gamma catenin. (newmarketscientific.com)
Cadherins2
- Without association with the catenins, the cadherins are non-adhesive. (rndsystems.com)
- Classical cadherins consist of a large extracellular domain which contains DXD and DXNDN repeats responsible for mediating calcium-dependent adhesion, a single-pass transmembrane domain, and a short carboxy-terminal cytoplasmic domain responsible for interacting with the catenins. (rndsystems.com)
Regulates3
- Camargo's team now demonstrates that Yap1 regulates proliferation of epidermal stem cells, and that it's controlled by a second molecule known as alpha-catenin, a tiny sensor that imparts information on the surrounding cell density. (vectorblog.org)
- 16] Tetsu O, McCormick F. β-Catenin regulates expression of cyclin D1 in colon carcinoma cells. (esmed.org)
- A double-negative feedback loop between Wnt-β-catenin signaling and HNF4α regulates epithelial-mesenchymal transition in hepatocellular carcinoma. (esmed.org)
Genes1
- Unphosphorylated β-catenin accumulates in the nuclear and interacts with TCF/LEF factors to stimulate the transcription of the downstream target genes of Wnt/β-catenin signaling. (esmed.org)
Expression3
- Decreased Expression of Plakophilin-2 and αT-Catenin in Arrhythmogenic Right Ventricular Cardiomyopathy: Potential Markers for Diagnosis. (nih.gov)
- Knocking down FFAR2 by siRNA decreased the expression of cleaved caspase 3 and the expression of phospho-GSK3β (Ser9) and active β-catenin in Caco-2 cells, subsequently mitigated the anticancer effect of butyrate. (umass.edu)
- The present study evaluated cell viability, expression levels of collagen II (Col II) and matrix metalloproteinase‑13 (MMP‑13), and activity of the Wnt/β‑catenin and NF‑κB signaling pathways in treated SW1353 cells. (spandidos-publications.com)
Colon2
- But alpha-catenin is known to be inappropriately silenced in skin and other epithelial cancers, such as colon cancer, so the "stop growing" message never gets sent, or is never heeded. (vectorblog.org)
- Mesenteric fat, vessels and lymph nodes were resected en block with the ascending colon. (medscape.com)
Role1
- Beta catenin has a role in cellular proliferation, differentiation and development. (newmarketscientific.com)
Beta1
- Beta-catenin can also bind to alpha-catenin. (wikidoc.org)
Cells1
- When skin cells are densely packed, alpha-catenin inactivates Yap1, keeping it out of the cell nucleus and preventing it from triggering any more cell growth. (vectorblog.org)
Activity2
Study1
- Recently, a genome-wide association study (GWAS) conducted in Korean subjects identified four CTNNA3 (alpha-T catenin) single nucleotide polymorphisms (SNPs) (rs10762058, rs7088181, rs1786929, and rs4378283) associated with diisocyanate -induced occupational asthma (DA). (cdc.gov)
Found1
- We found that loss of Tumor necrosis factor alpha (TNF-α) decreased obesity associated intestinal tumorigenesis by decreasing the inflammation, and manipulating the β-catenin pathway and NF-kB signaling. (umass.edu)
Proteins5
- Its cytoplasmic domain associates with cytoplasmic proteins termed catenins. (medscape.com)
- Interactions between the E-cadherin and p120-catenin proteins, in particular, are thought to be important for normal development of the head and face (craniofacial development), including the eyelids and teeth. (nih.gov)
- Furthermore, WZ increased the number of Sertoli cells, restored the ultrastructure of the Sertoli cell TJ, and upregulated the expression of TJ-associated proteins (zonula occludens-1 and Claudin11), ectoplasm specialized-associated proteins (N-Cadherin, E-Cadherin and ß-Catenin), and gap junction-associated protein (connexin 43), but did not affect the expression of Occludin and cytoskeletal protein (Vimentin). (bvsalud.org)
- Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. (thermofisher.com)
- T-cell factor/lymphoid enhancer factor (TCF/LEF) proteins regulate transcription by recruiting beta-catenin and its associated co-regulators. (ca.gov)
Cytoplasm and nucleus1
- Mutations in beta catenin gene (CTNNB1) leads accumulation of the beta catenin protein in cytoplasm and nucleus in different type of tumors eg. (newmarketscientific.com)
Binds3
- A slightly larger fragment, comprising residues 57-264, binds to beta-catenin. (nih.gov)
- β-Catenin or γ-catenin binds directly, whereas α-catenin links the bound β-catenin or γ-catenin to the actin microfilament network of the cellular cytoskeleton. (medscape.com)
- A catenin that binds F-ACTIN and links the CYTOSKELETON with BETA CATENIN and GAMMA CATENIN . (bvsalud.org)
Cytoskeleton2
- In adherens junctions, alpha-catenin links the cadherin-beta-catenin complex to the actin-based cytoskeleton. (nih.gov)
- Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. (nih.gov)
Pathway3
- WNT/Beta-catenin pathway plays a key role in stem cell differentiation as well as other biological processes such as cell adhesion, proliferation or even invasion in tumor microenvironments. (oatext.com)
- The aim of the study was to explore the molecular mechanisms about Wnt/β-catenin signal pathway underlying the osteal side effects of APs. (biomedcentral.com)
- Wnt/β-catenin signaling pathway may be a target for avoiding the APs-induced osteal side effects. (biomedcentral.com)
Vinculin1
- αE-catenin is an autoinhibited molecule that coactivates vinculin. (nih.gov)
Antibody7
- Confocal immunofluorescent analysis of A-431 cells labeled with α-E-Catenin Antibody (green, left) compared to an isotype control (right). (cellsignal.jp)
- Western blot analysis of extracts from various cell lines, using α-E-Catenin Antibody. (cellsignal.jp)
- The following product was used in this experiment: CD49f (Integrin alpha 6) Monoclonal Antibody (eBioGoH3 (GoH3)), PE-Cyanine7, eBioscience™ from Thermo Fisher Scientific, catalog # 25-0495-82, RRID AB_10804881. (thermofisher.com)
- Description: The eBioGoH3 monoclonal antibody reacts with mouse and human CD49f, also known as integrin alpha 6, very late activation antigen 6 (VLA-6 alpha chain), and platelet gpIc. (thermofisher.com)
- The eBioGoH3 antibody is cross-reactive to integrin alpha 6 on human, mouse and bovine cells. (thermofisher.com)
- This antibody has also been reported to have functional activity in blocking the binding of integrin alpha 6 to laminin. (thermofisher.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Thyroid Hormone Receptor Alpha (THRa) in Tissue homogenates and other biological fluids. (tuberculosisdrugresearch.org)
Complexes2
- In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. (nih.gov)
- Therefore, we have identified a key interacting factor of TCF/beta-catenin complexes to regulate Wnt gene transcription. (ca.gov)
Adhesion5
- Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion. (nih.gov)
- To clarify the relation between altered expression of cell adhesion molecules and progression of T1 superficial bladder tumors, 101 cases (71 T1 tumors, 30 T2/T3 tumors) were examined immunohistochemically for E-cadherin and α-, β-, and γ-catenins. (medscape.com)
- The present study was undertaken to examine a large series of 101 urothelial carcinomas from stage T1 to T2/T3 for the expression of the adhesion molecules E-cadherin and α-, β-, and γ-catenin. (medscape.com)
- The expression of three adhesion molecules (alpha-catenin, integrin alpha3, and integrin beta6) and platelet-derived growth factor B (PDGF-B) was elevated following exposure of NHK-C cells to DHA. (nih.gov)
- The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. (nih.gov)
Integrin3
- Induction of alpha-catenin, integrin alpha3, integrin beta6, and PDGF-B by 2,8-dihydroxyadenine crystals in cultured kidney epithelial cells. (nih.gov)
- CD49f also associates with CD104, the integrin beta 4 chain, to form the alpha 6 beta 4 complex. (thermofisher.com)
- For example, alpha 6 may combine with beta 4 in the integrin referred to as TSP180, or with beta 1 in the integrin VLA-6. (thermofisher.com)
Gene transcription1
- These study reported that β-catenin accumulated in the cytoplasm and subsequently translocates into the nucleus [ 16 ], where it associated with the T cell factor/ lymphocyte growth factor (TCF/LEF) into the complex, thus regulated the apoptotic gene transcription [ 17 ]. (biomedcentral.com)
Tumors3
- 001). Univariate analysis, performed in cases of T1 tumors, revealed association of abnormal E-cadherin with β-catenin diminution. (medscape.com)
- Cox multivariate analysis revealed only γ-catenin as an independent predictor of progression-free survival in patients with stage T1 bladder urothelial tumors. (medscape.com)
- ATRX, DAXX or MEN1 mutant pancreatic neuroendocrine tumors are a distinct alpha-cell signature subgroup. (cancerindex.org)
Marker1
- Further apoptosis-related marker and β-catenin expression was analyzed by Western blot and Immunofluorescence analysis. (biomedcentral.com)
Beta6
- alpha-catenin is a homodimer in solution, but forms a 1:1 heterodimer with beta-catenin. (nih.gov)
- A chimera consisting of the alpha-catenin-binding region of beta-catenin linked to the amino terminus of alpha-catenin 57-264 behaves as a monomer in solution, as expected, since beta-catenin binding disrupts the alpha-catenin dimer. (nih.gov)
- The crystal structure of this chimera reveals the interaction between alpha- and beta-catenin, and provides a basis for understanding adherens junction assembly. (nih.gov)
- catenin beta 1 [Source:HGNC Symbol;Acc:HGN. (gsea-msigdb.org)
- Beta catenin has a role in cellular proliferation, differentiation and development. (newmarketscientific.com)
- We show that RNF14 positively regulates Wnt signalling in human cancer cells and in an in vivo zebrafish model by binding to target promoters with TCF and stabilizing beta-catenin recruitment. (ca.gov)
Asthma2
- CTNNA3 (alpha-catenin) gene variants are associated with diisocyanate asthma: a replication study in a Caucasian worker population. (cdc.gov)
- Recently, a genome-wide association study (GWAS) conducted in Korean subjects identified four CTNNA3 (alpha-T catenin) single nucleotide polymorphisms (SNPs) (rs10762058, rs7088181, rs1786929, and rs4378283) associated with diisocyanate -induced occupational asthma (DA). (cdc.gov)
Cell2
- Description: A competitive ELISA for quantitative measurement of Rat Thyroid hormone receptor Alpha (THRA) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (tuberculosisdrugresearch.org)
- Description: A sandwich ELISA kit for detection of Thyroid Hormone Receptor Alpha from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (tuberculosisdrugresearch.org)
Domain1
- The crystal structure of the alpha-catenin dimerization domain, residues 82-279, shows that alpha-catenin dimerizes through formation of a four-helix bundle in which two antiparallel helices are contributed by each protomer. (nih.gov)
Source1
- catenin alpha 1 [Source:HGNC Symbol;Acc:HG. (gsea-msigdb.org)