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J. Biol. Chem., Vol. 280, Issue 17, 16546-16549, April 29, 2005

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Integrin Activation and Matrix Binding Mediate Cellular Responses to Mechanical Stretch^*

Akira Katsumi, Tomoki Naoe, Tadashi Matsushita, Kozo Kaibuchi¶, and Martin Alexander Schwartz||**

From the Cardiovascular Research Center, ^||Departments of Microbiology and Biomedical Engineering, Mellon Prostate Research Institute, University of Virginia, Charlottesville, Virginia 22908 and the Department of Hematology, ^¶Department of Cell Pharmacology, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa, Nagoya, Aichi 466-8550, Japan

Mechanical tension is a critical determinant of cell growth, differentiation, apoptosis, migration, and development. Integrins have been implicated in sensing force but little is known about how forces are transduced to biochemical signals. We now show that mechanical strain stimulates conformational activation of integrin v3 in NIH3T3 cells. Integrin activation is mediated by phosphoinositol 3-kinase and is followed by an increase in integrin binding to extracellular matrix proteins. Mechanical stretch stimulation of JNK was dependent on new integrin binding to extracellular matrix. These data define a molecular mechanism for the role of integrins in mechanotransduction.

Received for publication, September 28, 2004 , and in revised form, March 2, 2005.

^* This work was supported by National Institutes of Health Grants RO1 HL075092 and RO1GM47214 (to M. A. S.). 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.

^** To whom correspondence should be addressed. E-mail: maschwartz{at}virginia.edu.

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