Interaction of fibronectin with collagen fibrils

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Abstract
The interaction of fibronectin with native collagen during collagen fibril formation was investigated. Fibronectin, prepared from human serum or from the cell surface, bond to the forming rat collagen fibrils while less fibronectin bound to preformed fibers. Denatured collagen competed with native collagen in binding fibronectin. Fibronectin delayed the precipitation of collagen fibrils but did not alter the total amount of fibrils formed. Fibronectin which as heated to 80.degree. C for 30 min did not promote cell adhesion but still bound to native collagen and delayed fiber formation. The collagen-binding fragment of fibronectin produced by digestion with chymotrypsin or with neutrophil elastase had a similar effect in delaying fibril formation, but the cell-binding fragment was not active. Apparently, fibronectin can bind to aggregating collagen fibers probably at the same site shown previously to bind to denatured collgen. Since fibronectin inhibits the rate of collagen fibrillogenesis, it may regulate the size of collagen fibers.