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Activation of interstitial collagenase, MMP‐1, by Staphylococcus aureus cells having surface‐bound plasmin: a novel role of plasminogen receptors of bacteria
Author(s) -
Santala A.,
Saarinen J.,
Kovanen P.,
Kuusela P.
Publication year - 1999
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/s0014-5793(99)01440-4
Subject(s) - plasmin , collagenase , matrix metalloproteinase , receptor , biochemistry , staphylococcus aureus , chemistry , extracellular matrix , interstitial collagenase , extracellular , enzyme , microbiology and biotechnology , biology , bacteria , genetics
Plasmin, the enzymatically active form of plasminogen, can activate several matrix metalloproteinases (MMPs). In this study, we investigated the activation of MMP‐1, one of the major interstitial collagenases, by plasmin which was generated on the surface of Staphylococcus aureus cells. Plasmin bound to plasminogen receptors on S. aureus degraded the major 125 I‐labeled 55‐kDa proMMP‐1 into the 42‐kDa form corresponding to the size of active MMP‐1. MMP‐1 formed by S. aureus ‐bound plasmin was also enzymatically active as judged by digestion of the synthetic collagenase substrate, DNP‐Pro‐Leu‐Gly‐Leu‐Trp‐Ala‐ D ‐Arg‐NH 2 . The finding that, in MMP‐1 molecules generated either by soluble plasmin or by S. aureus ‐bound plasmin, the amino‐terminal amino acid sequences were identical indicated that the activation mechanisms of the two plasmin forms do not differ from each other. The present observations emphasise and broaden the physiological importance of bacterial plasminogen receptors. In addition to direct proteolytic effects on components of the extracellular matrix, receptor‐bound plasmin is also capable of initiating an MMP‐1‐dependent matrix‐degrading enzymatic cascade.