title: Interstitial collagenase from rat mammary carcinoma cells: interaction with substrates and inhibitors.
abstract: Functional characteristics of the interstitial collagenase purified from the BCl rat mammary carcinoma cell line were examined and compared with literature reports of the corresponding characteristics of collagenase from non-neoplastic cells. BCl collagenase degraded soluble collagen types I, II and III at the same rate and degraded fibrillar tendon collagen with an activation energy of 75 kcal/mol; these characteristics were identical to collagenase from normal rat uterine smooth muscle cells. Degradation of fibrillar collagen by BCl collagenase was completely inhibited by rat alpha 2-macroglobulin which was concomitantly cleaved into half-fragments. BCl collagenase was also inhibited by native and recombinant tissue inhibitor of metalloproteinases, a synthetic peptide collagenase inhibitor (Z-pro-leugly-NHOH), and Zn2+. In all functional characteristics examined, BCl collagenase was the same as interstitial collagenases from non-neoplastic sources.
authors.affiliation: Department of Pathology, University of Sydney, Australia.
authors.forename: A
authors.initials: A
authors.lastname: Nethery
authors.forename: R L
authors.initials: RL
authors.lastname: O'Grady
mesh_terms: D000818:Animals; D003094:Collagen / Q000378:metabolism; D005110:Extracellular Space / Q000201:enzymology*; D015674:Mammary Neoplasms, Animal / Q000201:enzymology*; D003012:Microbial Collagenase / Q000037:antagonists & inhibitors / Q000502:physiology*; D051381:Rats; D013379:Substrate Specificity
chemical_list: D003094:Collagen; D003012:Microbial Collagenase