Synthesis and secretion of under-hydroxylated procollagen at various temperatures by cells subject to temporary anoxia. Academic Article uri icon


  • Cells isolated by enzymic digestion of embryonic tendon were incubated under N2 so that they synthesized and accumulated the unhydroxylated form of procollagen which is known as protocollagen and which is largely comprised of pro- chains linked by interchain disulfide bonds. The cells were then exposed to O2 so that the intracellular protocollagen was hydroxylated and secreted as procollagen. When the hydroxylation was allowed to proceed at 31 or 34, the procollagen secreted into the medium was triple-helical but its hydroxyproline content was less than two-thirds and its hydroxylysine content was less than half the control. Even when the hydroxylation was allowed to occur at 37, the procollagen secreted by the cells was under-hydroxylated by about 15% in terms of its hydroxyproline content and about 45% in terms of its hydroxylysine content. The results may have consequences for collagen synthesis by tendons and similar tissues in vivo, since temporary anoxia in such tissues may well lead to the synthesis of a less stable procollagen or to fibers of decreased tensile strength. 1974.

published proceedings

  • Biochem Biophys Res Commun

author list (cited authors)

  • Uitto, J., & Prockop, D. J.

citation count

  • 50

complete list of authors

  • Uitto, J||Prockop, DJ

publication date

  • January 1974