Open AccessPreferential digestion of basement membrane collagen by an enzyme derived from a metastatic murine tumor.
Author(s) -
Lance A. Liotta,
Shigeto Abe,
Pamela Gehron Robey,
George R. Martin
Publication year - 1979
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.5.2268
Subject(s) - collagenase , basement membrane , type iv collagen , trypsin , microbial collagenase , chemistry , cleavage (geology) , type i collagen , enzyme , collagen, type i, alpha 1 , microbiology and biotechnology , biochemistry , extracellular matrix , biology , endocrinology , laminin , paleontology , fracture (geology)
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.