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Originally published In Press as doi:10.1074/jbc.M207700200 on January 9, 2003

J. Biol. Chem., Vol. 278, Issue 11, 9862-9868, March 14, 2003
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Protection of Islets by in Situ Peptide-mediated Transduction of the Ikappa B Kinase Inhibitor Nemo-binding Domain Peptide*

Khaja K. RehmanDagger , Suzanne Bertera§, Rita Bottino§, A. N. Balamurugan§, Jeffrey C. MaiDagger , Zhibao MiDagger , Massimo Trucco§, and Paul D. RobbinsDagger

From the Dagger  Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261 and the § Department of Pediatrics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261

We have previously demonstrated that adenoviral gene transfer of the NF-kappa B inhibitor Ikappa B to human islets results in protection from interleukin (IL)-1beta -mediated dysfunction and apoptosis. Here we report that human and mouse islets can be efficiently transduced by a cationic peptide transduction domain (PTD-5) without impairment of islet function. PTD mediated delivery of a peptide inhibitor of the IL-1beta -induced Ikappa B kinase (IKK), derived from IKKbeta (NBD; Nemo-binding domain), and completely blocked the detrimental effects of IL-1beta on islet function and NF-kappa B activity, in a similar manner to Ad-Ikappa B. We also demonstrate that mouse islets can be transduced in situ by infusion of the transduction peptide through the bile duct prior to isolation, resulting in 40% peptide transduction of the beta -cells. Delivery of the IKK inhibitor transduction fusion peptide (PTD-5-NBD) in situ to mouse islets resulted in improved islet function and viability after isolation. These results demonstrate the feasibility of using PTD-mediated delivery to transiently modify islets in situ to improve their viability and function during isolation, prior to transplantation.

* This work was supported by a grants from the Juvenile Diabetes Research Foundation, the Muscular Dystrophy Association, and National Institutes of Health Contract AR-6-2225.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom all correspondence should be addressed: Dept. of Molecular Genetics and Biochemistry, University of Pittsburgh, School of Medicine, W1246, Biomedical Science Tower, Pittsburgh, PA 15261. Tel.: 412-648-9268; Fax: 412-383-8837; E-mail: probb@pitt.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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