Fibronectin-independent adhesion of fibroblasts to extracellular matrix material: partial characterization of the matrix components.
Fibroblasts can adhere to extracellular matrix (ECM) material by fibronectin-dependent (type I) and fibronectin-independent (type II) mechanisms. In this report we investigate the biochemical characteristics of ECM that contribute to type II adhesion. ECM capable of mediating type II adhesions is produced primarily by normal diploid fibroblasts, but not by transformed cells or epithelial cells. Treatment of fibroblast ECM under conditions that result in the removal of most of the ECM lipid or most of the ECM glycosaminoglycan does not impair type II adhesion. Likewise, treatment of the ECM with large amounts of purified collagenase does not block type II adhesion. However, treatment of ECM with low doses of trypsin or with an agent that reacts with tyrosine residues, results in complete ablation of the ability of the ECM to support type II adhesion. On the basis of these observations we suggest that the matrix component(s) mediating type II adhesion are non-collagenous proteins or glycoproteins.
D000818:Animals; D002448:Cell Adhesion / Q000187:drug effects; D002478:Cells, Cultured; D003094:Collagen / Q000494:pharmacology; D003470:Culture Media; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005109:Extracellular Matrix / Q000032:analysis / Q000187:drug effects / Q000502:physiology*; D005347:Fibroblasts / Q000502:physiology*; D005353:Fibronectins / Q000502:physiology*; D006025:Glycosaminoglycans / Q000494:pharmacology; D006801:Humans; D014357:Trypsin / Q000494:pharmacology
D003470:Culture Media; D005353:Fibronectins; D006025:Glycosaminoglycans; D003094:Collagen; D014357:Trypsin