The interaction of platelet proteins with three fibroblast-derived collagenases.

Abstract:

:Three collagenases were purified from the culture medium of human skin fibroblasts using ammonium sulfate fractionation, ion-exchange chromatography and gel filtration. The cationic collagenase had a molecular weight of 42,000; two anionic collagenases had molecular weights of 63,000 and 115,000. Preincubation of the individual collagenases with purified human and bovine platelet heparin binding proteins resulted in the inhibition of the two anionic activities, but only by bovine low heparin affinity platelet protein (beta-TG). Such inhibition was dose-dependent at the microgram level, was not antagonized by heparin, and persisted even when the collagenases had been transformed into their 53,000 and 105,000 forms through treatment with p-aminophenylmercuric acetate. Neither human nor bovine high heparin affinity platelet factors (PF-4) nor human low heparin affinity platelet protein (beta-TG) were inhibitory to any of the three collagenases studied. This suggests that the ability of platelet proteins to inhibit collagenase is specifically influenced by the ionic nature of the enzyme and this inhibition is specifically dependent upon the species and type of platelet protein.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Pisoni R,Ciaglowski RE,Brown RK,Walz DA

doi

10.1016/0049-3848(84)90211-1

subject

Has Abstract

pub_date

1984-07-15 00:00:00

pages

159-68

issue

2

eissn

0049-3848

issn

1879-2472

journal_volume

35

pub_type

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