Constancy of proline hydroxylation in collagen synthesized at different temperatures by poikilotherms

Abstract

Previous experiments have suggested that the body temperature of an organism may in part regulate the hydroxyproline content of its collagen. In order to test this hypothesis, the hydroxyproline content of the collagen synthesized at different temperatures by fish cells in culture and by intact amphibian larvae was measured. High levels of prolyl hydroxylation were found at both low and high temperatures, which eliminates the possibility that temperature can directly modulate prolyl hydroxylation in vivo. Synthesis and hydroxylation of collagen appear to be coordinated so that unstable underhydroxylated molecules are not produced under normal circumstances.