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Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds.
studies demonstrate that TGase (show F13A1 Antibodies)-catalyzed transamidation and activation of rac1 and cdc42 (show CDC42 Antibodies) results from stimulation of multiple types of receptors and this novel signaling pathway can regulate dendritic spine morphology and plasticity.
The two enzymes PADI3 (show PADI3 Antibodies) and TGM3, responsible for posttranslational protein modifications, and their target structural protein TCHH (show TCHH Antibodies) are all involved in hair shaft formation.
Data indicate a decrease in transglutaminases TG1 and TG3 transcripts by about 70% in foreskins from patients with balanitis xerotica obliterans (BXO) BXO in comparison with patients without BXO and an increase in transglutaminase TG2 (show TGM2 Antibodies) mRNA levels by 2.9 fold.
Our data collectively demonstrate that TGM3 can be a candidate tumor suppressor that is able to induce esophageal cancer cell proliferation and migration
mRNA expression of transglutaminase 1 (show TGM1 Antibodies) and transglutaminase 3 was significantly decreased in patients with chronic periodontitis compared with a healthy control group.
Transglutaminase 3 present in the IgA aggregates in dermatitis herpetiformis skin is enzymatically active and binds soluble fibrinogen.
New basal cell carcinoma susceptibility loci were identified at TGM3 (rs214782) and RGS22 (show RGS22 Antibodies)(rs7006527).
IgA-anti-TG1 antibodies were found in 2% and IgA-anti-TG3 antibodies in 3% of patients with active atopic dermatitis (AD). Two out of the 5 patients with AD and concomitant celiac disease had IgA-anti-TG1 and IgA-anti-TG2 (show TGM2 Antibodies) antibodies.
TGM3, a candidate tumor suppressor, contributes to the carcinogenesis and development of human head and neck cancer.
Genetic variation in the epidermal transglutaminase genes is not associated with atopic dermatitis.
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 consists of two polypeptide chains activated from a single precursor protein by proteolysis. The encoded protein is involved the later stages of cell envelope formation in the epidermis and hair follicle.
E polypeptide, protein-glutamine-gamma-glutamyltransferase
, TGase E
, protein-glutamine gamma-glutamyltransferase E
, transglutaminase E