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Originally published In Press as doi:10.1074/jbc.M204202200 on May 28, 2002

J. Biol. Chem., Vol. 277, Issue 33, 30208-30218, August 16, 2002
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Efficiency of Protein Transduction Is Cell Type-dependent and Is Enhanced by Dextran Sulfate*

Jeffrey C. MaiDagger , Hongmei Shen§, Simon C. Watkins, Tao Cheng§, and Paul D. RobbinsDagger ||

From the Dagger  Department of Molecular Genetics and Biochemistry and the § University of Pittsburgh Cancer Institute, Department of Radiation Oncology, University of Pittsburgh School of Medicine, and the  Department of Cell Biology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261

Protein transduction domains (PTDs), both naturally occurring and synthetic, have been increasingly utilized to deliver biologically active agents to a variety of cell types in vitro and in vivo. We report that in addition to previously characterized arginine-rich PTDs, including TAT, lysine homopolymers were able to mediate transduction of a wide variety of cell types, as measured by flow cytometric and enzymatic assays. The efficiency of PTD-mediated transduction was influenced by the cell type tested, although polylysine homopolymers demonstrate levels of internalization that consistently exceeded those of TAT and arginine homopolymers. Transduction of arginine/lysine-rich PTDs occurred at 4 °C and following depletion of cellular ATP pools, albeit generally at reduced levels. Although transduction was reduced in Chinese hamster ovary mutant lines deficient in either heparan sulfate or glycosaminoglycan synthesis, uptake was restored to wild-type levels by incubating target cells with dextran sulfate. The enhancement of transduction by dextran sulfate suggests that electrostatic interactions play an important first step in the process by which PTDs and their cargoes traverse the plasma membrane.

* This work was supported by grants from the Muscular Dystrophy Association and the Cystic Fibrosis Foundation and by National Institutes of Health Contract AR6-2225.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, Pittsburgh, PA 15261. Tel.: 412-648-9268; Fax: 412-383-8837; E-mail: probb@pitt.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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