Analysis of glycosaminoglycan substitution in decorin by site-directed mutagenesis.

@article{Mann1990AnalysisOG,
  title={Analysis of glycosaminoglycan substitution in decorin by site-directed mutagenesis.},
  author={David M. Mann and Yoshiki Yamaguchi and Mario A. Bourdon and Erkki Ruoslahti},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 9},
  pages={5317-23}
}
Posttranslational glycosaminoglycan attachment to decorin, a chondroitin/dermatan sulfate proteoglycan, was studied by expression of a wild-type decorin cDNA and several mutagenized forms in two types of mammalian cells. Transfection of the wild-type cDNA resulted in the synthesis of an authentic chondroitin/dermatan sulfate proteoglycan similar to the decorin molecule synthesized by cultured human fibroblasts. Conversion of the serine residue that serves as the attachment site for the sole… CONTINUE READING

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