Incorporation of cis-hydroxyproline into collagen by tendon cells. Failure of the intracellular collagen to assume a triple-helical conformation.
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Matrix-free cells from the tendons of chick embryos were incubated with cis-4-hydroxy-L-proline, a proline analogue previously shown to be incorporated into collagen and other proteins. The analogue (200 g/ml) decreased the secretion of 14C-labeled collagen by the cells by about 60% and produced a small increase in the amount of intracellular 14C-labeled collagen. The small amount of 14C-labeled protein still secreted in the presence of the analogue consisted of small peptides which were at least in part derived from 14C-labeled collagen. Limited pepsin digestion of the 14C-labeled protein from the cell fraction indicated that the incorporation of the proline analogue into collagen interfered with the formation of the triple-helical conformation. 1972.
author list (cited authors)
Uitto, J., Dehm, P., & Prockop, D. J.
complete list of authors
Uitto, J||Dehm, P||Prockop, DJ