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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
Data suggest that disulfide bond switch in allosteric activation/inactivation of TGM2 is example of post-translational redox regulation that is reversibly and allosterically modulated by two proteins (ERp57 and TRX). (TGM2 = transglutaminase 2; ERp57 = endoplasmic reticulum resident protein 57; TRX = thioredoxin-1)
This suggests that TGase 2 has an allosteric binding site (81-116 a.a) which changes the conformation of TGase 2 enough to accelerate inactivation through self-polymer formation.
Taken together, the present data suggested a potentially important role for TGM2 in the regulation of osteosarcoma chemosensitivity. TGM2 might therefore serve as a therapeutic target for osteosarcoma.
Multiple symptoms and high serum anti-tTG antibody levels correlated with mucosal damage in children with Celiac disease.
A role for TG2 has been demonstrated in both endothelial tubule formation and in tubule loss, which involves its function in the regulation of TGFbeta1 and Smad signaling.
Production of anti-TG2 antibodies could be due to a general state of inflammation or could indicate a very early stage of a gluten-dependent pathology.
A long non-coding RNA is located within the first intron of transglutaminase 2 gene. LOC107987281 lncRNA is induced when levels of TGM2 transcripts are also increased, for example after drug treatment. In addition, correlation analysis between the expression of this lncRNA and TGM2 demonstrated that occurs in relation to the development of several tumors affecting pancreas, stomach and kidney.
TG2 plays a crucial role in the proliferative process
The results point to regulation of alternative splicing of tissue transglutaminase could account for the complex physiopathology of celiac disease.
Our data revealed that patients with lower level of TG2 expression detected in cancer tissues had longer disease free survival and overall survival as compared to the patients with higher TG2 expression.
Gluten-free diet compliance and lower antitissue transglutaminase (atTG) at diagnosis are predictors of earlier normalization of atTG levels in patients with celiac disease. Patients with type 1 diabetes mellitus are less likely to normalize atTG levels, with longer normalization time.
expression in psoriasis was higher than in normal skin
Serum tissue transglutaminase antibody was elevated in almost one-quarter of an eosinophilic esophagitis (EoE) cohort, and at least 20% of these patients did not have potential celiac disease, suggesting EoE is a heterogeneous disease with differing immune mechanisms activated in some patients.
Study indicates that TGM2 affects the metastatic potential and stemness of colorectal cancer stem cells by regulating EMT- and stemness-related proteins.
PARP3 controls of TGFbeta-induced epithelial mesenchymal transformation and acquisition of stem-like cell features by stimulation transglutaminase 2/SNAI1 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 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)
TG2 contributes to 5-hydroxytryptamine-induced distal pulmonary artery smooth muscle cell proliferation via promotion of AKT signaling, likely via its serotonylation.
An important role for TG2, mediated by intracellular calcium fluxes and HIF1A, in hypoxia-induced pulmonary artery smooth muscle cells proliferation.
externalized GTP-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 binding
TG2 activity enhanced p65 phosphorylation, leading to an increase in NF-kappaB transcriptional activity. These results indicate that TG2 is a critical mediator of cytokine expression in the UV-induced inflammatory response of keratinocytes.
Following pressure overload, endogenous tTG mediates matrix cross-linking, while protecting the remodelling myocardium from dilation by exerting matrix-preserving actions
that TG2 depletion increases nuclear factor-kappaB (NF-kappaB) signaling
Factor XIII-A and TG2 regulate resorption, adipogenesis and plasma fibronectin homeostasis in bone and bone marrow.
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-TGM2 double knock-out mouse epidermis showed that unlike TGM2, TGM1 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, 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 (EST) 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 and TG2.
findings support the potential pathophysiological relevance of TRX in celiac disease and establish the Cys(370)-Cys(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-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 did not alter the early compaction.
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