Tkivna transglutaminaza

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Transglutaminaza 2 (C polipeptid, protein-glutamin-gama-glutamiltransferaza)

Prikaz tkivne transglutaminaze baziran na PDB 1KV3.
Dostupne strukture
1KV3, 2Q3Z, 3LY6, 3S3J, 3S3P, 3S3S
Identifikatori
Simboli TGM2; G-ALPHA-h; GNAH; TG2; TGC
Vanjski ID OMIM190196 MGI98731 HomoloGene3391 GeneCards: TGM2 Gene
EC broj 2.3.2.13
Pregled RNK izražavanja
PBB GE TGM2 201042 at tn.png
PBB GE TGM2 211003 x at tn.png
PBB GE TGM2 211573 x at tn.png
podaci
Ortolozi
Vrsta Čovek Miš
Entrez 7052 21817
Ensembl ENSG00000198959 ENSMUSG00000037820
UniProt P21980 P21981
RefSeq (mRNA) NM_004613 NM_009373
RefSeq (protein) NP_004604 NP_033399
Lokacija (UCSC) Chr 20:
36.76 - 36.79 Mb
Chr 2:
158.12 - 158.15 Mb
PubMed pretraga [1] [2]
Protein-glutamine gamma-glutamyltransferase
Identifikatori
EC broj 2.3.2.13
CAS broj 80146-85-6
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures
Ontologija gena AmiGO / EGO

Tkivna transglutaminaza (tTG, TG2) je 78 kDa, od kalcijuma zavisni enzim (EC 2.3.2.13) iz familije γ-glutamiltransferaza (transglutaminaza).[1][2] Poput drugih transglutaminaza, on formira unakrsne veze u proteinima između ε-amino grupe lizinskih ostataka i γ-karboksamidne grupe glutaminskih ostataka. Nastale inter- ili intramolekulske veze su veoma otporne na proteolizu (proteinsku degradaciju). Pored unakrsnog vezivanja, tTG katalizuje i druge tipove reakcija uključujući deaminaciju, GTP-vezivanje/hidrolizu, i ima izopeptidazno dejstvo.[3] Za razliku od drugih članova transglutaminazne familije, tTG se može naći u intracelularnim i ekstracelularnim prostorima raznih tipova tkiva i prisutan je u mnoštvu različitih organa uključujući srce, jetru, i tanka creva. Intracelularni tTG je izobilan u citosolu, a u malim količinama je prisutan i u jedru i mitohondrijama.[2] Smatra se da intracelularni tTG ima važnu ulogu u apoptozi.[4] U ekstracelularnom prostoru, tTG se vezuje za proteine ekstracelularnog matriksa (ECM),[5] sa posebno jakim vezivanjem za fibronektin.[6] Ekstracelularni tTG uzima udela u ćelijskoh adheziji, ECM stabilizaciji, zarastanju rana, receptorskog signalizaciji, ćelijskoj proliferaciji, i ćelijskoj motilnosti.[2]

tTG je posebno poznat po tome što je autoantigen u celijačnoj bolesti, doživotnoj bolesti usled koje konzumiranje dijetarnog gluten uzrokuje patološki imunski respons koji dovodi do inflamacije tankih creva i naknadne atrofije.[7][8][9]

Reference[uredi - уреди]

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  2. Greška citiranja Invalid <ref> tag; no text was provided for refs named Klock; $2
  3. Greška citiranja Invalid <ref> tag; no text was provided for refs named Facchiano; $2
  4. Greška citiranja Invalid <ref> tag; no text was provided for refs named McConkey; $2
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  6. Greška citiranja Invalid <ref> tag; no text was provided for refs named Akimov; $2
  7. Griffin M, Casadio R, Bergamini CM (December 2002). "Transglutaminases: nature's biological glues". Biochem. J. 368 (Pt 2): 377–96. doi:10.1042/BJ20021234. PMC 1223021. PMID 12366374. 
  8. Greška citiranja Invalid <ref> tag; no text was provided for refs named DiRaimondo; $2
  9. Greška citiranja Invalid <ref> tag; no text was provided for refs named Sabatino; $2

Literatura[uredi - уреди]

refs = [1]

[2]

[3]

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Spoljašnje veze[uredi - уреди]

  • Endomysial antibodies
  • A collection of substrates and interaction partners of TG2 is accessible in the TRANSDAB, an interactive transglutaminase substrate database.
  1. Király R, Demény M, Fésüs L (December 2011). "Protein transamidation by transglutaminase 2 in cells: a disputed Ca2+-dependent action of a multifunctional protein". FEBS J. 278 (24): 4717–39. doi:10.1111/j.1742-4658.2011.08345.x. PMID 21902809. 
  2. Klöck C, Diraimondo TR, Khosla C (July 2012). "Role of transglutaminase 2 in celiac disease pathogenesis". Semin Immunopathol 34 (4): 513–22. doi:10.1007/s00281-012-0305-0. PMID 22437759. 
  3. Facchiano F, Facchiano A, Facchiano AM (2006). "The role of transglutaminase-2 and its substrates in human diseases". Front. Biosci. 11: 1758–73. doi:10.2741/1921. PMID 16368554. 
  4. McConkey DJ, Orrenius S (October 1997). "The role of calcium in the regulation of apoptosis". Biochem. Biophys. Res. Commun. 239 (2): 357–66. doi:10.1006/bbrc.1997.7409. PMID 9344835. 
  5. Akimov SS, Krylov D, Fleischman LF, Belkin AM (February 2000). "Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin". J. Cell Biol. 148 (4): 825–38. doi:10.1083/jcb.148.4.825. PMC 2169362. PMID 10684262. 
  6. Diraimondo TR, Klöck C, Khosla C (April 2012). "Interferon-γ activates transglutaminase 2 via a phosphatidylinositol-3-kinase-dependent pathway: implications for celiac sprue therapy". J. Pharmacol. Exp. Ther. 341 (1): 104–14. doi:10.1124/jpet.111.187385. PMC 3310700. PMID 22228808. 
  7. Lortat-Jacob H, Burhan I, Scarpellini A, Thomas A, Imberty A, Vivès RR, Johnson T, Gutierrez A, Verderio EA (May 2012). "Transglutaminase-2 interaction with heparin: identification of a heparin binding site that regulates cell adhesion to fibronectin-transglutaminase-2 matrix". J. Biol. Chem. 287 (22): 18005–17. doi:10.1074/jbc.M111.337089. PMC 3365763. PMID 22442151. 
  8. Di Sabatino A, Vanoli A, Giuffrida P, Luinetti O, Solcia E, Corazza GR (August 2012). "The function of tissue transglutaminase in celiac disease". Autoimmun Rev 11 (10): 746–53. doi:10.1016/j.autrev.2012.01.007. PMID 22326684.