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J. Biol. Chem., Vol. 280, Issue 8, 6915-6922, February 25, 2005

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Heparin II Domain of Fibronectin Uses 41 Integrin to Control Focal Adhesion and Stress Fiber Formation, Independent of Syndecan-4^*

Jennifer A. Peterson, Nader Sheibani¶, Guido David||, Angeles Garcia-Pardo**, and Donna M. Peters

From the Departments of Pathology and Laboratory Medicine and Ophthalmology and Visual Sciences, University of Wisconsin, Madison, Wisconsin 53706, ^||Human Genetics, Flanders Interuniversity Institute for Biotechnology, University of Leuven, 3000 Leuven, Belgium, and ^**Departamento de Inmunologia, Centro de Investigaciones Biologicas, Consejo Superior de Investigaciones Cientificas, 28006 Madrid, Spain

Co-signaling events between integrins and cell surface proteoglycans play a critical role in the organization of the cytoskeleton and adhesion forces of cells. These processes, which appear to be responsible for maintaining intraocular pressure in the human eye, involve a novel cooperative co-signaling pathway between 51 and 41 integrins and are independent of heparan sulfate proteoglycans. Human trabecular meshwork cells isolated from the eye were plated on type III 7–10 repeats of fibronectin (51 ligand) in the absence or presence of the heparin (Hep) II domain of fibronectin. In the absence of the Hep II domain, cells had a bipolar morphology with few focal adhesions and stress fibers. The addition of the Hep II domain increased cell spreading and the numbers of focal adhesions and stress fibers. Cell spreading and stress fiber formation were not mediated by heparan sulfate proteoglycans because treatment with chlorate, heparinase, or soluble heparin did not prevent Hep II domain-mediated cell spreading. Cell spreading and stress fiber formation were mediated by 41 integrin because soluble anti-4 integrin antibodies inhibited Hep II domain-mediated cell spreading and soluble vascular cell adhesion molecule-1 (41 ligand)-induced cell spreading. This is the first demonstration of the Hep II domain mediating cell spreading and stress fiber formation through 41 integrin. This novel pathway demonstrates a cooperative, rather than antagonistic, role between 51 and 41 integrins and suggests that interactions between the Hep II domain and 41 integrin could modulate the strength of cytoskeleton-mediated processes in the trabecular meshwork of the human eye.

Received for publication, June 14, 2004 , and in revised form, November 24, 2004.

^* This work was supported in part by NEI Grants EY12515 (to D. M. P.) and EY13700 (to N. S.), National Fund for Scientific Research-Flanders Grant G.0239.01 (to G. D.), and Ministerio de Educacion y Ciencia (Spain) Grant SAF2003-00824 (to A. G.-P.). 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.

^¶ Recipient of a Career Development Award from the Research to Prevent Blindness Foundation.

To whom correspondence should be addressed: Dept. of Pathology and Laboratory Medicine, Rm. 6590 MSC, 1300 University Ave., Madison, WI 53706. Tel.: 608-262-4626; Fax: 608-265-3301; E-mail: dmpeter2{at}facstaff.wisc.edu.

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