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J. Biol. Chem., Vol. 278, Issue 34, 31766-31773, August 22, 2003

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Proteomics Identification of Acyl-acceptor and Acyl-donor Substrates for Transglutaminase in a Human Intestinal Epithelial Cell Line

IMPLICATIONS FOR CELIAC DISEASE^*

Stefania Orrù  , Ivana Caputo  ¶, Alfonsina D'Amato , Margherita Ruoppolo || ** and Carla Esposito  

From the Department of Chemistry, University of Salerno, 84081 Baronissi, Salerno, Italy, ^¶Department of Pediatrics & European Laboratory for the Investigation of Food-induced Diseases, University of Naples "Federico II," 80138 Naples, Italy, ^||Department of Biochemistry and Medical Biotechnologies, University of Naples "Federico II," 80138 Naples, Italy, and ^**Centro di Ingegneria Genetica, Biotecnologie Avanzate, scarl, Naples 80138, Italy

Transglutaminase (TG)-catalyzed cross-linking of both intracellular and extracellular proteins is an important biochemical event. However, increased concentrations of cross-linked proteins have been observed in many disorders. Moreover, TG-catalyzed modification of proteins might generate new self-antigens responsible for the autoimmune response, as in celiac disease. The identification of available substrates may offer an understanding of how the TG-catalyzed post-translational modification has an impact on physiology and disease. We used a proteomic approach to identify TG-modified protein targets in human intestinal epithelial cells to determine the extent to which transglutaminase specifically contributes to celiac disease. Two probes were used for endogenous TG activity: 5-(biotinamido)pentylamine, which represents the acyl-acceptor, and a biotinylated glutamine-containing peptide, which represents the acyl-donor. This approach identified >25 proteins, which range from 30,000 to 300,000 Daltons and can serve as acyl-acceptor and/or acyl-donor for transglutaminase. Some of them were known transglutaminase substrates, whereas others had not been previously identified. These targets include proteins involved in cytoskeletal network organization, folding of proteins, transport processes, and miscellaneous metabolic functions.

Received for publication, May 14, 2003

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

To whom correspondence should be addressed: Dept. of Chemistry, University of Salerno, Via S. Allende, 84081 Baronissi, Salerno, Italy. Tel.: 39-089-965298; Fax: 39-089-965296; E-mail: cesposito{at}unisa.it.

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