[HTML][HTML] Cleavage of type I procollagen by human mast cell chymase initiates collagen fibril formation and generates a unique carboxyl-terminal propeptide
MW Kofford, LB Schwartz, NM Schechter… - Journal of Biological …, 1997 - ASBMB
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 μg/ml did not affect either the rate or the products of procollagen
chymase cleavage. The cleavage site of chymase on the pro-α1 (I) collagen carboxyl …
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 μg/ml did not affect either the rate or the products of procollagen
chymase cleavage. The cleavage site of chymase on the pro-α1 (I) collagen carboxyl …