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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
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 (show TGFB1 Proteins) and Smad (show SMAD1 Proteins) 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.
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.
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
TG2 activity enhanced p65 (show NFkBP65 Proteins) phosphorylation, leading to an increase in NF-kappaB (show NFKB1 Proteins) 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 (show NFKB1 Proteins)) signaling
Factor XIII (show UGDH Proteins)-A and TG2 regulate resorption, adipogenesis and plasma fibronectin (show FN1 Proteins) 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 (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.
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