Literature DB >> 1655539

Inactivation of human plasma C1-inhibitor by human PMN leucocyte matrix metalloproteinases.

V Knäuper1, S Triebel, H Reinke, H Tschesche.   

Abstract

Highly purified human polymorphonuclear (PMN) leucocyte matrix metalloproteinases, collagenase and gelatinase, cleaved human plasma C1-inhibitor at the carboxyl site of Ala439 (P6). This led to a concomitant loss of C1-inhibitor activity. An additional cleavage site, at the carboxyl site of Ser441 (P4), was observed during PMN leucocyte gelatinase-induced inactivation, and a minor fragment of the plasma C1-inhibitor was generated.

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Year:  1991        PMID: 1655539     DOI: 10.1016/0014-5793(91)81235-z

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Degradation of C1-inhibitor by plasmin: implications for the control of inflammatory processes.

Authors:  E M Wallace; S J Perkins; R B Sim; A C Willis; C Feighery; J Jackson
Journal:  Mol Med       Date:  1997-06       Impact factor: 6.354

2.  Complement-mediated killing of microtumors in vitro.

Authors:  J Hakulinen; S Meri
Journal:  Am J Pathol       Date:  1998-09       Impact factor: 4.307

3.  Fragmentation of human polymorphonuclear-leucocyte collagenase.

Authors:  V Knäuper; A Osthues; Y A DeClerck; K E Langley; J Bläser; H Tschesche
Journal:  Biochem J       Date:  1993-05-01       Impact factor: 3.857

4.  Recombinant C1 inhibitor P5/P3 variants display resistance to catalytic inactivation by stimulated neutrophils.

Authors:  E Eldering; C C Huijbregts; J H Nuijens; A J Verhoeven; C E Hack
Journal:  J Clin Invest       Date:  1993-03       Impact factor: 14.808

  4 in total

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