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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
PARP3 (show PARP3 Proteins) controls of TGFbeta (show TGFB1 Proteins)-induced epithelial mesenchymal transformation and acquisition of stem-like cell features by stimulation transglutaminase 2/SNAI1 (show SNAI1 Proteins) signaling.
Circulating tissue transglutaminase is associated with sFlt-1, soluble endoglin and VEGF in the maternal circulation of preeclampsia patients, suggesting that tTG may have a role in the pathogenesis of PE.
19% of pediatric celiac disease patients treated with a gluten-free diet had persistent enteropathy. At the time of the repeat biopsy, tTG was elevated in 43% of cases with persistent enteropathy and 32% of cases in which there was mucosal recovery. Overall the positive predictive value of the autoantibody tTG was 25% and the negative predictive value was 83% in patients on a gluten-free diet for a median of 2.4 years.
Computational analyses of the effect of novel amino acid clusters of human transglutaminase 2 on its structure and function have been presented.
The link is being discussed between P2X7R (show P2RX7 Proteins) signaling and TG2 export, a pathway that has been recently discovered and tied extracellular protein modifications into the danger signal-mediated innate immune response. (Review)
TG2-regulated signaling bestows on cancer cells the ability to proliferate, to resist cell death, to invade, to reprogram glucose metabolism and to metastasize, making it a therapeutic target. (Review)
TGM2 is involved in the resistance of cancer cells to the histone deacetylase (show HDAC1 Proteins) inhibitor vorinostat.
TGM2 is involved in amyloid-beta (1-42)-induced pro-inflammatory activation via AP1 (show FOSB Proteins)/JNK (show MAPK8 Proteins) signaling pathways in cultured monocytes.
The role of TG2 in certain pathological conditions, in which inflammation and monocytes and/or macrophages are prominently present, including atherosclerosis, sepsis, and multiple sclerosis, has been discussed. (Review)
The 45 kDa gelatin-binding domain of fibronectin (show FN1 Proteins) is responsible for the binding to TGM2.
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
tTG might be a key factor in pathogenesis of abnormal protein aggregation in Alzheimer's disease.
data suggest that TG2 has a tissue-specific role in GONAT function and browning, which becomes apparent under acute cold exposure.
Adenosine produced from adenine nucleotides through an interaction between apoptotic cells and engulfing macrophages contributes to the appearance of TGM2 in dying thymocytes.
TG2 is expressed in infiltrating and adhering to spinal cord monocytes during experimental autoimmune encephalomyelitis in transgenic mice.
Characterization of TGM2 and TGM1 (show TGM1 Proteins)-TGM2 double knock-out mouse epidermis showed that unlike TGM2, TGM1 (show TGM1 Proteins) is indispensable for skin formation.
These results indicate that TG2-mediated Th17 cell differentiation is not required for the pathogenesis of dextran sulfate sodium-induced acute colitis.
The increased expression of TGM2 in the TM increases N-epsilon(gamma-glutamyl) lysine crosslinking in the TM, increases aqueous outflow resistance, and elevates IOP in mice. TGM2 may be at least partially responsible for ocular hypertension in POAG.
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
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