Preferential digestion of basement membrane collagen by an enzyme derived from a metastatic murine tumor.
The specificity of human skin collagenase and of an enzyme from an invasive tumor were studied by using types I, II, III, IV, and V (AB) collagen as substrates. Human skin collagenase degraded types I, II, and III collagen, producing the characteristic 3/4 and 1/4 cleavage products, but failed to degrade type IV or V collagen. Collagenase prepared from the invasive tumors showed maximal activity after trypsin treatment. The tumor enzyme degraded type IV (basement membrane) collagen, producing fragments consistent with a single cleavage site but did not attack types I, II, III, and V collagen. Because type IV collagen prepared by pepsinization of placenta was also digested, it is likely that cleavage of type IV collagen by the tumor collagenase occurs within a largely helical domain. A type IV collagenase could play a significant role in tumor metastases and in normal tissues where basement membrane turnover takes place.
D000818:Animals; D001485:Basement Membrane / Q000378:metabolism*; D003094:Collagen / Q000378:metabolism; D006801:Humans; D051379:Mice; D003012:Microbial Collagenase / Q000378:metabolism*; D008970:Molecular Weight; D009362:Neoplasm Metastasis; D009374:Neoplasms, Experimental / Q000201:enzymology*; D012867:Skin / Q000201:enzymology; D013379:Substrate Specificity
D003094:Collagen; D003012:Microbial Collagenase