Biological Significance of Peptide containing Hydroxyproline during the Development of Carrageenin Granuloma

Abstract

ALTHOUGH it is generally accepted that free hydroxyproline cannot be utilized for the synthesis of collagen^1–3, we have demonstrated in previous papers a close interrelation between the level of free hydroxyproline in tissues of rats⁴, or in the body of chicken embryos⁵, and the rate of collagen synthesis (after cortisone administration). In a recent paper Green and Lowther⁶ presented proofs that the formation of protein-bound hydroxyproline proceeds by way of ‘activated’ proline which is hydroxylated during the incubation in granuloma slices to form ‘activated’ hydroxyproline. The possibility of such a hydroxylation of proline in vitro has been demonstrated recently⁷. Some hypotheses dealing with collagen synthesis presume in connective tissue the presence of peptide with hydroxyproline, the biochemical existence of which has not yet been proved. In an ultrafiltrate of extracts from bovine embryonic tissues homogenates (subcutis, growth-zone of bones) we found repeatedly several peptides containing hydroxyproline. Their chromatographic and other biochemical characteristics will be published elsewhere (Kobrle, V., and Chvapil, M.).