Abstract

Fibroblasts of the synovium of sheathed tendons were isolated, and their biochemical properties were compared with those of the fibroblasts of the remaining tendon. The synovial cells had a lower attachment efficiency than did the tendon cells. On the day of cell isolation the synovial cells synthesized collagen as 10% of their total protein, whereas the tendon cells synthesized 30% collagen. After growth in fetal bovine serum (FBS), the percentage of collagen synthesized by both populations decreased; however, the synovial cells still made less collagen than did the tendon cells (5 versus 11%). On the basis of cyanogen bromide peptide analysis, the synovial cells were found to synthesize Types I and III collagen in primary culture, whereas the tendon cells synthesized only Type I. The synovial cells also synthesized two to three times less sulfated glycosaminoglycans in culture than did the tendon cells. Thus, the two cell populations differed in attachment efficiency and in their biosynthesis of collagen and sulfated glycosaminoglycans. These differences reflect extracellular matrix differences that have been observed in the tendon in vivo. In addition, the results augment existing data showing that not all fibroblasts have identical phenotypes.

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