Selective Inhibitors of Human Neutrophil Proteinase 3

Author(s): Brice Korkmaz, Christine Kellenberger, Marie-Claude Viaud-Massuard, Francis Gauthier

Journal Name: Current Pharmaceutical Design

Volume 19 , Issue 6 , 2013


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Abstract:

Human neutrophil proteinase 3 (PR3) and elastase (HNE) are homologous serine proteinases involved in the proteolytic events associated with inflammation and infection. Their close structural and functional resemblance makes it difficult to understand their respective biological functions. Thus, all natural inhibitors of PR3 identified to date preferentially target HNE, and only recently have inhibitors that target PR3 selectively been described. This review describes how differences in the structures of the extended active sites of PR3 and HNE can be exploited to produce selective inhibitors of PR3.

Keywords: Proteinase 3 (myeloblastin), neutrophil, azapeptide, serpin, drug development.

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Article Details

VOLUME: 19
ISSUE: 6
Year: 2013
Published on: 17 December, 2012
Page: [966 - 976]
Pages: 11
DOI: 10.2174/1381612811319060002
Price: $65

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