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Human Transglutaminase 2 Protein expressed in - ABIN1047979
Faye, Inforzato, Bignon, Hartmann, Muller, Ballut, Olsen, Day, Ricard-Blum: Transglutaminase-2: a new endostatin partner in the extracellular matrix of endothelial cells. in The Biochemical journal 2010
High TGM2 expression is associated with recurrence in Glioma.
Exosomes from cells lacking TG2 present less protein content. Proteasome inhibition leads to the selective recruitment of TG2 in the exosomes. TG2 is an important player in the biogenesis of exosomes controlling the selectivity of their cargo under stressful cellular conditions.
High transglutaminase 2 expression is associated with colorectal cancer.
GTP binding (show RND2 Proteins), but not transamidase activity, is required for TG2-dependent cancer stem cell invasion, migration and tumour formation. However, transamidase site-specific inhibitors reduce cancer stem cell survival.
these findings ascribe a novel function for ALDH1A3 (show ALDH1A3 Proteins) in an aggressive glioma stem cells phenotype via the up-regulation of tissue transglutaminase
Data show that carboxyl-terminus of Hsp70-interacting protein (CHIP) promotes polyubiquitination of transglutaminase 2 (TG2) and its subsequent proteasomal degradation.
No clear evidence for an association of tTGA or EMA (show ETFA Proteins) seropositivity with incident coronary heart disease outcomes, suggesting that tTG autoimmunity is unlikely to be the biological link between coeliac disease and CHD (show CHDH Proteins).
the TG2 enzymatic activity was negligibly affected by bexarotene treatment. It is important to control TG2 overexpression since its upregulation is correlated with tumor transformation and drug resistance. Bexarotene also showed in vivo tumoricidal effects in a GBM xenograft mouse model. Therefore, we suggest bexarotene as a more beneficial differentiation agent than ATRA for GBM.
Thus it can be concluded that human transglutaminases differ in harboring damaging variants and TGM2 is under purifying selection suggesting that it may have so far not revealed physiological functions.
mechanical load-induced TGM2 expression and enzyme activity is involved in the progression of the calcification of ligamentum flavum.
TG2 contributes to 5-hydroxytryptamine-induced distal pulmonary artery smooth muscle cell proliferation via promotion of AKT (show AKT1 Proteins) signaling, likely via its serotonylation.
An important role for TG2, mediated by intracellular calcium fluxes and HIF1A (show HIF1A Proteins), in hypoxia-induced pulmonary artery smooth muscle cells proliferation.
externalized GTP (show AK3 Proteins)-bound TG2 serves as a molecular switch for differentiation of chondrocytes to a hypertrophic, calcifying phenotype in a manner that does not require either TG2 transamidation activity or fibronectin (show FN1 Proteins) binding
Two enhancers of Tgm2, which seem to act as integrators of the TGF-beta (show TGFB1 Proteins), retinoid and adenylate cyclase signaling pathways in dying thymocytes have been identified.
TG2 transamidating activity is induced upon proteasome inhibition. Proteasome inhibition leads to the selective recruitment of TG2 in the exosomes. Exosomes from cells lacking TG2 present less protein content. TG2 interacts with ESCRT proteins upon stressful stimulus. TG2 is an important player in the biogenesis of exosomes controlling the selectivity of their cargo under stressful cellular conditions.
data suggest that the anti-angiogenic mechanism of the celiac disease-specific autoantibodies involves extracellular TG2 and inhibited endothelial cell mobility
Kidney fibrosis in aging may represent a natural outcome of upregulated endostatin (show COL18A1 Proteins) (EST (show MAP3K8 Proteins)) and transglutaminase 2 (TG2), but more likely it appears to be a result of cumulative stresses occurring on the background of synergistically acting geronic (aging) proteins, EST (show MAP3K8 Proteins) and TG2.
findings support the potential pathophysiological relevance of TRX (show TXN Proteins) in celiac disease and establish the Cys (show DNAJC5 Proteins)(370)-Cys (show DNAJC5 Proteins)(371) disulfide bond of TG2 as one of clearest examples of an allosteric disulfide bond in mammals.
TG2 controls the formation of VEGF165-heparan sulfate proteoglycan complexes
TG2 is a novel inhibitor of adipogenesis.
LPS (show TLR4 Proteins)-induced TG2 was involved in the mechanism of pinocytosis and phagocytosis in microglia.
Inhibition of tissue transglutaminase resulted in a reduced rate of compaction compared to controls during early remodeling (up to 2 days). In contrast, inhibition of lysyl oxidase (show LOX Proteins) did not alter the early compaction.
TG2-deficient mice exhibited hyper inflammatory responses after being challenged with monosodium urate crystals.
Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene.
C polypeptide, protein-glutamine-gamma-glutamyltransferase
, TGase C
, TGase H
, protein-glutamine gamma-glutamyltransferase 2
, tissue transglutaminase
, transglutaminase C
, transglutaminase H
, transglutaminase 2
, tissue-type transglutaminase
, transglutaminase 2 (C polypeptide, protein-glutamine-gamma-glutamyltransferase)
, C polypeptide
, TG C