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Volume 272, Number 49, Issue of December 5, 1997 pp. 30911-30917
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

The Role of 11 Integrin in Wound Contraction
A QUANTITATIVE ANALYSIS OF LIVER MYOFIBROBLASTS IN VIVO AND IN PRIMARY CULTURE

(Received for publication, May 13, 1997, and in revised form, September 10, 1997)

From the Liver Center Laboratory, San Francisco General Hospital, and the Department of Medicine, University of California, San Francisco, California 94110

An unresolved question in wound contraction concerns the identity of integrins mediating the attachment of tissue myofibroblasts to matrix in the injury site. Previous studies with cell lines have focussed on 11 and 21, the principal collagen-binding integrins, but have yielded conflicting data. We have examined this issue in wound healing in the liver, isolating the myofibroblast population (activated stellate cells) and quantitating expression of the 1 and 2 integrin subunits during the in vivo injury. Normal stellate cells displayed 1 but no detectable 2. During injury, 1 expression was maintained; 2 became detectable at the mRNA level but at all times was <8% of 1 mRNA. Contraction of collagen lattices, studied with 24-h cultured cells and initiated by endothelin 1, was blocked 70% by anti-1 and 30% by anti-2 (both significant, p < 0.05). The inhibition by anti-2, which was unexpected, was attributable to culture-induced change in integrin expression; both the mRNA and protein for 2 increased strikingly within 24 h of plating stellate cells on a collagen gel. We conclude that 11 is the sole integrin utilized by contracting myofibroblasts in vivo. Although 21 is capable of mediating contraction, its expression by myofibroblasts occurs largely, if not exclusively, in response to culture.

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