Human lung mast cell tryptase fails to activate procollagenase or degrade proteoglycan.
Pig synovial and human skin fibroblast procollagenases were treated with highly purified tryptase, the major proteinase of human mast cells, to determine whether this trypsin-like proteinase could activate the latent form of collagenase and so be involved in connective tissue breakdown. No significant activation of either human or pig procollagenase was found, but the highest concentration of tryptase partially destroyed procollagenase. Tryptase did not degrade type I collagen or proteoglycan. These data indicate that human mast cell tryptase does not contribute to connective tissue breakdown via procollagenase activation or via proteoglycan degradation.
D000818:Animals; D003094:Collagen / Q000378:metabolism; D017364:Collagenases; D003238:Connective Tissue / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D004792:Enzyme Precursors / Q000378:metabolism*; D006801:Humans; D008168:Lung / Q000166:cytology; D008407:Mast Cells / Q000201:enzymology*; D003012:Microbial Collagenase / Q000378:metabolism*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism* / Q000494:pharmacology; D011499:Protein Processing, Post-Translational; D011509:Proteoglycans / Q000378:metabolism; D013552:Swine; D014357:Trypsin / Q000378:metabolism
D004792:Enzyme Precursors; D011509:Proteoglycans; D003094:Collagen; D010447:Peptide Hydrolases; C023073:tosylarginine methyl ester hydrolase; D014357:Trypsin; D017364:Collagenases; C022440:procollagenase; D003012:Microbial Collagenase