Collagen-Induced Changes in the Pattern of Protein Synthesis of Fibroblasts

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Abstract
Cells were cultured on plastic, collagen fibrils or gelatin. General protein synthetic activity of cells did not show any significant difference among the three substrates, whereas the pattern of protein synthesis was substrate-dependent. Profiles of protein synthesis (polypeptide maps) were obtained by subjecting two-dimensional autoradiograms of polyacrylamide gel electrophoresis to a computer-assisted image analyzer. Major polypeptide spots expressed on gelatin were rather like those on plastic. Collagen fibrils caused significant changes in the polypeptides map. Fibroblasts on collagen fibrils produced 364 spots of polypeptides, 26% of which were synthesized specifically on collagen fibrils. The remaining was shared by cells on plastic and was categorized into three groups: (1) polypeptides whose synthesis was up-regulated by collagen fibrils (26% of the total); (2) polypeptides that were expressed equally on both plastic and collagen fibrils (51%); and (3) polypeptides down-regulated by collagen fibrils (23%). A protein with molecular weight of 150 K and an isoelectric point (pI) of 7.3 was one of the collagen-induced and worthy of further analysis. This protein was found to change its pI depending upon the amounts of collagen fibrils and was shown to be located in the mitochondrial fraction.