Specific inactivation of prolyl 4-hydroxylase and inhibition of collagen synthesis by oxaproline-containing peptides in cultured human skin fibroblasts.

@article{Karvonen1990SpecificIO,
  title={Specific inactivation of prolyl 4-hydroxylase and inhibition of collagen synthesis by oxaproline-containing peptides in cultured human skin fibroblasts.},
  author={K. Karvonen and L. Ala‐Kokko and T. Pihlajaniemi and T. Helaakoski and S. Henke and V. Günzler and K. Kivirikko and E. Savolainen},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 15},
  pages={
          8415-9
        }
}
The crucial role of collagen in fibrotic disorders has prompted attempts to develop drugs that inhibit collagen accumulation. Peptides containing the unphysiological amino acid 5-oxaproline (Opr) have recently been found to act as specific syncatalytic inactivators of pure prolyl 4-hydroxylase, the enzyme that catalyzes the formation of 4-hydroxyproline in collagens. The present study indicates that oxaproline-containing peptides benzyloxycarbonyl-Phe-Opr-Gly-benzyl ester (I) and… Expand
17 Citations
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Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases.
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