Transglutaminase 5 is acetylated at the N-terminal end.
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Rufini A, Vilbois F, Paradisi A, Oddi S, Tartaglione R, Leta A, Bagetta G, Guerrieri P, Finazzi-Agro' A, Melino G, Candi E
Transglutaminase 5 is acetylated at the N-terminal end.
Amino Acids. 2004 Jul;26(4):425-30. Epub 2004 Jun 17.
- PubMed ID
- 15290349 [ View in PubMed]
- Abstract
Transglutaminases (TGases) are calcium-dependent enzymes that catalyse cross-linking between proteins by acyl transfer reaction; they are involved in many biological processes including coagulation, differentiation, and tissue repair. Transglutaminase 5 was originally cloned from keratinocytes, and a partial biochemical characterisation showed its involvement in skin differentiation, in parallel to TGase 1 and TGase 3. Here, we demonstrate, by electrospray tandem mass spectrometry that TGase 5 is acetylated at the N-terminal end. Moreover, in situ measurement of TGase activity shows that endogenous TGase 5 is active upon treatment with phorbol acetate, and the enzyme co-localises with vimentin intermediate filaments.