Tissue transglutaminase
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Tissue transglutaminase drawn from PDB 1FAU. | |
transglutaminase 2
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Identifiers | |
Symbol(s) | TGM2 |
Entrez | 7052 |
OMIM | 190196 |
RefSeq | NM_198951 |
UniProt | P21980 |
Other data | |
EC number | 2.3.2.13 |
Locus | Chr. 20 q12 |
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]
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[edit] Genetics
The human tTG gene is located on the 20th chromosome (20q11.2-q12).
[edit] Physiology
tTG is expressed ubiquitously. It requires calcium as a cofactor. Transcription is increased by retinoic acid. Amongst its many supposed functions, it appears to play a role wound healing, apoptosis and extracellular matrix development[1]
[edit] Role in disease
tTG 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]
[edit] Diagnostic use
Serology for anti-tTG antibodies has superseded older serological tests (anti-endomysium, anti-gliadin and anti-reticulin) and has a strong sensitivity (99%) and specificity (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]
[edit] Therapeutic use
Use of tTG as a form of surgical glue is still experimental. It is also being studied as an attenuator of metastasis in certain tumours.[1]
[edit] References
- ^ a b c d Griffin M, Casadio R, Bergamini CM. Transglutaminases: nature's biological glues. Biochem J 2002;368:377-96. PMID 12366374.
- ^ Dieterich W, Ehnis T, Bauer M, Donner P, Volta U, Riecken EO, Schuppan D. Identification of tissue transglutaminase as the autoantigen of celiac disease. Nature Med 1997;3:797-801. PMID 9212111.
- ^ Sblattero D, Berti I, Trevisiol C, Marzari R, Tommasini A, Bradbury A, Fasano A, Ventura A, Not T. Human recombinant tissue transglutaminase ELISA: an innovative diagnostic assay for celiac disease. Am J Gastroenterol 2000;95:1253-7. PMID 10811336.