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Originally published In Press as doi:10.1074/jbc.M303159200 on June 13, 2003

J. Biol. Chem., Vol. 278, Issue 36, 34605-34616, September 5, 2003
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Cell Adhesion to Fibrillin-1 Molecules and Microfibrils Is Mediated by {alpha}5{beta}1 and {alpha}v{beta}3 Integrins*

Daniel. V. Bax {ddagger} § ¶, Sarah E. Bernard § ¶ ||, Amanda Lomas {ddagger} §, Amanda Morgan § ||, Jon Humphries § ||, C. Adrian Shuttleworth § ||, Martin J. Humphries § || and Cay M. Kielty {ddagger} || ** {ddagger}{ddagger}

From the {ddagger}United Kingdom Centre for Tissue Engineering, the ||Wellcome Trust Centre for Cell-Matrix Research, the §School of Biological Sciences, and **School of Medicine, 2.205 Stopford Bldg., University of Manchester, Manchester M13 9PT, United Kingdom

Fibrillins are the major glycoprotein components of microfibrils that form a template for tropoelastin during elastic fibrillogenesis. We have examined cell adhesion to assembled purified microfibrils, and its molecular basis. Human dermal fibroblasts exhibited Arg-Gly-Asp and cation-dependent adhesion to microfibrils and recombinant fibrillin-1 protein fragments. Strong integrin {alpha}5{beta}1 interactions with fibrillin ligands were identified, but integrin {alpha}v{beta}3 also contributed to cell adhesion. Fluorescence-activated cell sorting analysis confirmed the presence of abundant {alpha}5{beta}1 and some {alpha}v{beta}3 receptors on these cells. Adhesion to microfibrils and to Arg-Gly-Aspcontaining fibrillin-1 protein fragments induced signaling events that led to cell spreading, altered cytoskeletal organization, and enhanced extracellular fibrillin-1 deposition. Differences in cell shape when plated on fibrillin or fibronectin implied substrate-specific {alpha}5{beta}1-mediated cellular responses. An Arg-Gly-Asp-independent cell adhesion sequence was also identified within fibrillin-1. Adhesion and spreading of smooth muscle cells on fibrillin ligands was enhanced by antibody-induced {beta}1 integrin activation. A375-SM melanoma cells bound Arg-Gly-Asp-containing fibrillin-1 protein fragments mainly through {alpha}v{beta}3, whereas HT1080 cells used mainly {alpha}5{beta}1. This study has shown that fibrillin microfibrils mediate cell adhesion, that {alpha}5{beta}1 and {alpha}v{beta}3 are both important but cell-specific fibrillin-1 receptors, and that cellular interactions with fibrillin-1 influence cell behavior.

Received for publication, March 27, 2003 , and in revised form, June 3, 2003.

* This work was funded by the Medical Research Council, British Heart Foundation, Biotechnology and Biological Sciences Research Council, and Engineering and and Physical Sciences Research Council. 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.

{ddagger}{ddagger} To whom correspondence should be addressed. Tel.: 44-161-275-5739; Fax: 44-161-275-5082; E-mail: cay.kielty{at}man.ac.uk.


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