Abstract
Abstract Development of a method permitting quantitative analysis of tissue culture medium for protein-bound hydroxyproline led to the detection of large amounts of soluble collagen formed by human synovial fibroblasts. The soluble collagen was found in greatest concentration in media from mature cultures where deposition of fibrous collagen was in process. Viscometric studies revealed intrinsic viscosity values in excess of 11.0 dl. per gram, suggesting a molecular weight similar to undegraded collagen. Ascorbic acid, 200 μg per milliliter of culture medium, markedly enhanced formation of hyaluronic acid without evidence of a depolymerizing effect. Both soluble and fibrous collagen formation in cultures of synovial fibroblasts were greatly enhanced by ascorbate. Cortisol, on the other hand, markedly depressed formation of hyaluronate, fibrous, and soluble collagen, even in the presence of the stimulatory vitamin. This cell culture system may be a valuable model for studying factors regulating the transition between the soluble and fibrous forms of collagen in living systems.
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