Transglutaminase 5 is acetylated at the N-terminal end.
Rufini A,
Vilbois F,
Paradisi A,
Oddi S,
Tartaglione R,
Leta A,
Bagetta G,
Guerrieri P,
Finazzi-Agro' A,
Melino G,
Candi E.
Biochemistry Laboratory, IDI-IRCCS, University of Rome Tor Vergata, Rome, Italy.
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.
PMID: 15290349 [PubMed - indexed for MEDLINE]