Synthesis and extrusion of collagen by freshly isolated cells from chick embryo tendon Academic Article uri icon

abstract

  • Matrix-free cells were isolated from chick embryo tendons by digesting the tendons with trypsin and bacterial collagenase. Microscopic examination of the isolated cells indicated that they were essentially homogeneous and testing the cells with the Trypan Blue technique indicated that most of the cells were viable. The cells rapidly incorporated [14C]proline into protein for up to 2 h and well over half of the [14C]proline incorporated into protein was in collagen. Centrifuging the samples at low speed at the end of the incubation removed the cells from most of the newly-synthesized extracellular collagen. About 90 % of the [14C]protein in the medium was fully hydroxylated collagen polypeptides which were at least as large as the -chains of interstitial collagen. Incubating the cells with varying concentrations of ,-dipyridyl inhibited the hydroxylation of protocollagen and demonstrated that un-hydroxylated collagen is not extruded at a normal rate. Incubation with cis-hydroxyproline or with azetidine-2-carboxylic acid provided the first quantitative confirmation of earlier suggestions that collagen containing one of several proline analogues is also not extruded at a normal rate. 1971.

published proceedings

  • Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis

author list (cited authors)

  • Dehm, P., & Prockop, D. J.

citation count

  • 254

complete list of authors

  • Dehm, Peter||Prockop, Darwin J

publication date

  • January 1971