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Tissue transglutaminase (TG2, tTG) is an enzyme (EC 2.3.2.13) of the transglutaminase family. Like other transglutaminases, it crosslinks proteins between an ε-N of a lysine residue and a glutamine residue in two protein chains, creating a bond that is highly resistant to proteolysis (protein degradation). It is particularly notable for being the autoantigen in coeliac disease, but is also known to play a role in apoptosis, cellular differentiation and matrix stabilisation[1]
GeneticsThe human tTG gene is located on the 20th chromosome (20q11.2-q12). Physiology
Role in diseasetTG is best known for its link with coeliac disease, an allergy to gluten (wheat protein) in which the immune response crossreacts with tTG, leading to malabsorption.[2] Recent developments are the possible role of tTG in inflammation, degenerative diseases and tumour biology.[1] Diagnostic useSerology for anti-tTG antibodies has superseded older serological tests (anti-endomysium, anti-gliadin and anti-reticulin) and has a strong sensitivity (99%) and specificity (>90%) for identifying coeliac disease. Modern anti-tTG assays rely on a human recombinant protein as an antigen[3] Therapeutic use
References
Carnitine O-palmitoyltransferase - Glyceronephosphate O-acyltransferase - Lecithin-cholesterol acyltransferase - Citrate synthase Acetyltransferases: Beta-galactoside transacetylase - Choline acetyltransferase - Chloramphenicol acetyltransferase - Histone acetyltransferase (P300/CBP)- N-Acetylglutamate synthase - Serotonin N-acetyl transferase Aminoacyltransferases: Peptidyl transferase - Transglutaminase (Tissue transglutaminase, Factor XIII)
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