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Volume 272, Number 52, Issue of December 26, 1997 pp. 32798-32803

Aortic Smooth Muscle Cells Interact with Tenascin-C through Its Fibrinogen-like Domain

(Received for publication, August 11, 1997, and in revised form, October 8, 1997)

David W. LaFleur , Julie Chiang , James A. Fagin , Stephen M. Schwartz , Prediman K. Shah , Kurt Wallner , James S. Forrester and Behrooz G. Sharifi

From the Atherosclerosis Research Center, Division of Cardiology, Burns and Allen Research Institute, Cedar-Sinai Medical Center, University of California School of Medicine, Los Angeles, California 90048 and  Division of Pathology, University of Washington, Seattle, Washington 98195

The extracellular matrix protein tenascin-C is a multidomain protein that regulates cell adhesion. We used two different smooth muscle cell subtypes derived from adult and newborn rat aorta to investigate the interaction of tenascin-C or its various domains with these cells using an adhesion assay. Newborn cells were three times more adherent to tenascin-C than adult cells. Tenascin C-adhering cells remained round, whereas they spread rapidly on a fibronectin substrate. Adhesion assays showed the interaction between tenascin-C and newborn cells to be predominantly RGD-independent. Mg²⁺ increased newborn cell adhesion to tenascin-C in a concentration-dependent manner, whereas Ca²⁺ had no effect. To analyze the structure-function relationships of different domains of tenascin-C, we used recombinant full-length fibronectin-like and fibrinogen-like domains and various subdomains corresponding to the alternatively spliced regions of tenascin-C. The cells adhered to the fibrinogen-like domain but not to the fibronectin-like domain or its subdomains. As with the intact tenascin-C molecule, adherent cells remained round, and the Mg²⁺, but not Ca²⁺, promoted this interaction. The interaction of cells with the fibrinogen-like region was further mapped to a 30-amino acid peptide located near the carboxyl-terminal part of the tenascin-C molecule. The same 30-amino acid peptide was active in promoting cell migration. Our results provide a basis for understanding the mechanism of interaction of tenascin-C with smooth muscle cells and a framework for isolating membrane binding sites that mediate the cellular responses to this molecule.

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