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Latent collagenase from human polymorphonuclear leucocytes and activation to collagenase by removal of an inhibitor
Author(s) -
Macartney H.W.,
Tschesche H.
Publication year - 1980
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(80)80282-1
Subject(s) - collagenase , chemistry , citation , microbiology and biotechnology , computer science , biology , enzyme , biochemistry , library science
Human leucocytes contain several enzymes which participate in the degradation of collagen [l-3]. The cleavage of the tropocollagen molecule, (preferentially type I collagen), is initiated by a true collagenase splitting the collagen molecule into two distinct fragments [l]. Since the initial demonstration of collagenolytic activity in leucocytes [ 11, it has been shown that the enzyme exists in both active and latent forms in extracts of human leucocytes [2]. The latent collagenase can be activated by other active neutral proteases [4-S] and recently cathepsin G, a chymotrypsin-like enzyme, isolated from human leucocytes has been shown to be capable of activating the latent enzyme [7]. In previous years proteolytic enzymes have been used by many groups to activate the latent collagenases obtained from a variety of other tissues and a multistep scheme has been proposed for collagenase activation by limited proteoly sis [8-l 11. There also exists evidence to support the hypothesis that activation of the latent enzyme takes place through the removal of an inhibitor from an enzyme-inhibitor complex [2,5,6,1 l-131. In this paper we wish to report on the isolation of a latent collagenase from human leucocytes and its activation to active collagenase by enzymically active and non-active agents, that remove an inhibitor protein (24 000 M,) from the latent enzyme which is capable of inhibiting the active enzyme.