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Identification of a protein in sera of normal humans that inhibits fibroblast chemotactic and random migration in vitro.

Normal human serum contains a 230,000 Mr protein that inhibits fibroblast chemotactic and random migration. This serum inhibitor of fibroblast migration (SIFM) is a heat-stable, trypsin-sensitive protein with a pI of 4.8 that reversibly inhibits the random and chemotactic migration of fibroblasts in vitro. Although SIFM effectively inhibits the chemotaxis of fibroblasts to interstitial collagens, fibronectin, lymphocyte-derived chemotactic factor for fibroblasts, and serum-derived chemotactic factor, it does not alter the chemotactic migration of human peripheral blood neutrophils or monocytes, and does not act as a cytotoxin to human dermal fibroblasts. The SIFM appears to act through a cell-directed mechanism to alter the fibroblast's ability to migrate. Serum inhibitor of fibroblast migration may function in vivo to modulate fibroblast migration under physiologic and pathologic conditions.