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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.
Afiliación
  • Rufini A; Biochemistry Laboratory, IDI-IRCCS, University of Rome Tor Vergata, Rome, Italy.
Amino Acids ; 26(4): 425-30, 2004 Jul.
Article en En | MEDLINE | ID: mdl-15290349
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.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Transglutaminasas Límite: Animals / Humans Idioma: En Revista: Amino Acids Asunto de la revista: BIOQUIMICA Año: 2004 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Austria
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Transglutaminasas Límite: Animals / Humans Idioma: En Revista: Amino Acids Asunto de la revista: BIOQUIMICA Año: 2004 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Austria