Effect of various aminoacid analogues on chick tendon procollagen synthesis and secretion: Selective inhibition by S-2-aminoethyl cysteine

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Abstract

Matrix-free chick embryo tendon cells were incubated with [14C]-proline in the presence of various aminoacid analogues and the effects of the analogues on [14C]-proline incorporation, [14C]-hydroxyproline synthesis and secretion of labeled molecules were examined. It was found that the structural lysine analogue S-2-aminoethylcysteine was a potent inhibitor of procollagen synthesis and secretion. At a concentration of 1 mM it produced a 75% decrease in [14C]-hydroxyproline synthesis and a 90% decrease in the secretion of [14C]-hydroxyproline-containing macromolecules.

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