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J. Biol. Chem., Vol. 278, Issue 24, 21886-21892, June 13, 2003

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Rigidity of Collagen Fibrils Controls Collagen Gel-induced Down-regulation of Focal Adhesion Complex Proteins Mediated by ₂₁ Integrin^*

Yang-Kao Wang , Yao-Hsien Wang , Chau-Zen Wang , Junne-Ming Sung , Wen-Tai Chiu ¶, Shu-Han Lin ¶, Yung-Hen Chang ¶ and Ming-Jer Tang  ¶ ||

From the Institute of Basic Medical Sciences, National Cheng-Kung University Medical College, Tainan 701, Taiwan, Republic of China, Department of Internal Medicine, National Cheng-Kung University Medical College, Tainan 701, Taiwan, Republic of China, ^¶ Department of Physiology, National Cheng-Kung University Medical College, Tainan 701, Taiwan, Republic of China

Previous studies have shown that collagen gel overlay induced selective proteolysis of focal adhesion complex proteins in Madin-Darby canine kidney (MDCK) cells. In this study, we examined whether morphological and biochemical changes were present in cells cultured on collagen gel. We found that focal adhesion complex proteins, including focal adhesion kinase (FAK), talin, paxillin, and p130^cas, but not vinculin, were decreased within 1 h when MDCK cells were cultured on collagen gel. Collagen gel-induced selective decrease of focal adhesion proteins was observed in all lines of cells examined, including epithelial, fibroblastic, and cancer cells. Matrigel also induced selective down-regulation of focal adhesion proteins. However, cells cultured on collagen gel- or matrigel-coated dishes did not show any changes of focal adhesion proteins. These data suggest that the physical nature of the gel, i.e. the rigidity, is involved in the expression of focal adhesion proteins. The collagen gel-induced down-regulation of focal adhesion complex proteins was caused by reduction of protein synthesis and activation of proteases such as calpain. Overexpression of a dominant negative mutant of discoidin domain receptor 1 (DDR1) or FAK-related non-kinase (FRNK) did not prevent collagen gel-induced down-regulation of the focal adhesion complex protein, whereas an anti-21 integrin-neutralizing antibody completely blocked it. Taken together, our results indicate that the rigidity of collagen gel controls the expression of focal adhesion complex proteins, which is mediated by ₂₁ integrin but not DDR1.

Received for publication, January 6, 2003 , and in revised form, March 10, 2003.

^* This work was supported by National Health Research Institute Grant NHRI-EX91-9031SL and the Ministry of Education (MOE) program for promoting academic excellence of the University under grant number 91-B-FA09-1-4. 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. Tel.: 886-6-2353535 (ext. 5425); Fax: 886-6-2362780; E-mail: mjtang1{at}mail.ncku.edu.tw.

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