Stimulation of chondromucoprotein synthesis in chondrocytes by extracellular chondromucoprotein.

Chondrocytes in suspension culture preserve their differentiated state, as expressed by a high rate of chondromucoprotein synthesis. Purified chondromuco-protein added to a suspension of cultured embryonic epiphyseal cartilage cells stimulates the rate of synthesis of chondromucoprotein at concentrations up to 2 mg/ml. The stimulation involved synthesis of the entire molecule since incorporation of labeled serine (into core protein), glucosamine, acetate, or sulfate was increased. Neither the amount of synthesis of total protein nor that of collagen was increased. No elevation of xylosyltransferase and N-acetylgalactosaminyltransferase activities was observed. The stimulation was produced by several other polyanionic substances. No evidence was found of the entry of chondromucoprotein into chondrocytes under the conditions of the experiments. Mild trypsinization lowered the response to added chondromucoprotein and decreased the endogenous rate of chondromucoprotein synthesis. Incubation of cells after trypsinization results in restoration of the rates of chondromucoprotein synthesis. The endogenous, as well as the stimulated, rate of chondromucoprotein synthesis varied with the density of chondrocytes in culture. It is suggested that the rate of chondromucoprotein synthesis may be partially controlled by cell surface receptors.