Cleavage of type I procollagen by human mast cell chymase initiates collagen fibril formation and generates a unique carboxyl-terminal propeptide.

@article{Kofford1997CleavageOT,
  title={Cleavage of type I procollagen by human mast cell chymase initiates collagen fibril formation and generates a unique carboxyl-terminal propeptide.},
  author={M W Kofford and Lawrence B. Schwartz and Norman M. Schechter and Dorne R. Yager and Robert F. Diegelmann and Martin F. Graham},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 11},
  pages={7127-31}
}
The ability of human mast cell chymase and tryptase to process procollagen was examined. Purified human intestinal smooth muscle cell procollagen was incubated with human mast cell tryptase or human mast cell chymase. Purified chymase, but not tryptase, exhibited procollagen proteinase activity in the presence of EDTA. Addition of purified porcine heparin over a range of 0.1-100 microg/ml did not affect either the rate or the products of procollagen chymase cleavage. The cleavage site of… CONTINUE READING

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