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J Biol Chem, Vol. 273, Issue 44, 28978-28985, October 30, 1998

PR-39, a Syndecan-inducing Antimicrobial Peptide, Binds and Affects p130Cas

Yvonne R. Chan and Richard L. Gallo

From the Department of Dermatology and Division of Developmental and Newborn Medicine, Boston Children's Hospital and Harvard Medical School, Boston, Massachusetts 02115

PR-39 is a proline-arginine-rich antimicrobial peptide and an important component of innate immunity. In addition to its antimicrobial effects, PR-39 can alter mammalian cell gene expression and behavior. To determine the mechanism through which PR-39 affects mesenchymal cells, we identify a number of binding targets for PR-39 using a biologically active fragment of PR-39 (PR-39(15)). We found that PR-39 binds NIH 3T3 in a saturable manner consistent with the existence of a binding target. Similar to full-length PR-39, PR-39(15) interacts with lipid bilayers. After interacting with the membrane, PR-39(15) rapidly enters human microvascular endothelial cells and binds a number of cytoplasmic proteins. PR-39 selectively binds recombinant SH3-containing proteins and was also found to bind a native SH3-containing protein, p130Cas. PR-39(15) treatment of endothelial cells results in altered p130 localization. These results show that PR-39(15) binds an SH3-containing signal transduction molecule that has the potential to explain a myriad of effects PR-39 has on mammalian cell behaviors.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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