BIOLOGICAL-ACTIVITY OF HUMAN COLLAGEN BREAKDOWN PRODUCTS ON FIBROBLASTS

Bacterial collagenase rapidly attacks and degrades human collagen into small peptides. Human type I and III collagen, extracted and purified from placental tissue, was digested by incubation with bacterial coll agenase. Following analysis on Superdex-30 gel sieve-chromatography, t he breakdown products were shown to be of the size of di- and tripepti des. The collagen-derived peptides were added to rat fibroblast cultur e to evaluate the effects of these breakdown products on cell prolifer ation and biosynthetic activity. Using the neutral red test, stimulate d cell proliferation was demonstrated when collagen breakdown products , at a concentration of 5-50ng/mL of medium, were added. The incorpora tion of radiolabelled precursors H-3-proline and S-35-sulphate into th e secreted macromolecules of fibroblast cultures after 2 and 24 hours did not show significant differences in synthesis of protein or sulfat ed glycosaminoglycan between collagen peptide-treated cultures and the controls.