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Originally published In Press as doi:10.1074/jbc.M007324200 on January 30, 2001

J. Biol. Chem., Vol. 276, Issue 17, 14474-14481, April 27, 2001
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L-plastin Peptide Activation of alpha vbeta 3-mediated Adhesion Requires Integrin Conformational Change and Actin Filament Disassembly*

Jun WangDagger , Hua Chen§, and Eric J. Brown§

From the Dagger  Program in Molecular Cell Biology, Division of Biology and Biomedical Sciences, Washington University School of Medicine, St. Louis, Missouri 63110 and the § Program in Host-Pathogen Interactions, University of California, San Francisco, San Francisco, California 94143

L-plastin (LPL) is a leukocyte actin binding protein previously implicated in the activation of the integrin alpha Mbeta 2 on polymorphonuclear neutrophils. To determine the role for LPL in integrin activation, K562 cell adhesion to vitronectin via alpha vbeta 3, a well-studied model for activable integrins, was examined. Cell permeant versions of peptides based on the N-terminal sequence of LPL and the LPL headpiece domain both activated alpha vbeta 3-mediated adhesion. In contrast to adhesion induced by treatment with phorbol 12-myristate 13-acetate (PMA), LPL peptide-activated adhesion was independent of integrin beta 3 cytoplasmic domain tyrosines and was not inhibited by cytochalasin D. Also in contrast to PMA, LPL peptides synergized with RGD ligand or Mn2+ for generation of a conformational change in alpha vbeta 3 associated with the high affinity state of the integrin, as determined by binding of a ligand-induced binding site antibody. Although LPL and ligand showed synergy for ligand-induced binding site expression when actin depolymerization was inhibited by jasplakinolide, LPL peptide-induced adhesion was inhibited. Thus, both actin depolymerization and ligand-induced integrin conformational change are required for LPL peptide-induced adhesion. We hypothesize that the critical steps of increased integrin diffusion and affinity enhancement may be linked via modulation of the function of the actin binding protein L-plastin.

* This work was supported by Grant AI35811 from the National Institutes of Health (to E. J. B.).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 correspondence should be addressed: Program in Host Pathogen Interactions, Campus Box 0654, University of California at San Francisco, 513 Parnassus Ave., San Francisco, CA 94143-0654. Tel.: 415-514-0167; Fax: 415-514-0169; E-mail: ebrown@medicine.ucsf.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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