Literature DB >> 8123672

Proteolysis of human native and oxidised alpha 1-proteinase inhibitor by matrilysin and stromelysin.

Z Zhang1, P G Winyard, K Chidwick, G Murphy, M Wardell, R W Carrell, D R Blake.   

Abstract

Matrilysin is shown to rapidly inactivate alpha 1PI, an inhibitor of elastase, by cleaving the Pro357-Met358 peptide bond of its reactive centre. The rate of inactivation of alpha 1PI by matrilysin is four times higher than stromelysin. Matrilysin cleaves oxidised alpha 1PI at the Phe352-Leu353 bond, whilst stromelysin cleaves oxidised alpha 1PI at the Met358-Ser359 bond. We conclude that matrilysin is a potent serpinase which could play a role in inflammatory tissue damage by proteolytically inactivating alpha 1PI.

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Year:  1994        PMID： 8123672     DOI： 10.1016/0304-4165(94)90119-8

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  13 in total

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5.  Elevation of intact and proteolytic fragments of acute phase proteins constitutes the earliest systemic antiviral response in HIV-1 infection.

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6.  Antiproteases as therapeutics to target inflammation in cystic fibrosis.

Authors:  Derek J Quinn; Sinéad Weldon; Clifford C Taggart
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7.  Enhanced expression of matrilysin, collagenase, and stromelysin-1 in gastrointestinal ulcers.

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9.  alpha1-antitrypsin and its C-terminal fragment attenuate effects of degranulated neutrophil-conditioned medium on lung cancer HCC cells, in vitro.

Authors:  Inga Zelvyte; Tim Stevens; Ulla Westin; Sabina Janciauskiene
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Review 10.  The Role of Serine Proteases and Antiproteases in the Cystic Fibrosis Lung.

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