Literature DB >> 8776752

Azurocidin, a natural antibiotic from human neutrophils: expression, antimicrobial activity, and secretion.

R P Almeida1, A Vanet, V Witko-Sarsat, M Melchior, D McCabe, J E Gabay.   

Abstract

The azurophil granules of human PMN contain four antibiotic proteins, the serprocidins, which have extensive homology to one another and to serine proteases. Azurocidin, a member of this family, is a 29-kDa glycoprotein with broad spectrum antimicrobial activity and chemotactic activity toward monocytes. Insect cells transfected with a baculovirus vector carrying azurocidin cDNA produced a recombinant azurocidin protein. We purified the recombinant azurocidin protein from the culture medium of the infected cells and showed that it retained the antimicrobial activity of the native neutrophil-derived molecule. In addition, we present evidence that a 49-amino-acid region of the recombinant azurocidin protein is required for its secretion from insect cells.

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Year:  1996        PMID: 8776752     DOI: 10.1006/prep.1996.0053

Source DB:  PubMed          Journal:  Protein Expr Purif        ISSN: 1046-5928            Impact factor:   1.650


  8 in total

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Review 2.  Neutrophil serine proteases fine-tune the inflammatory response.

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3.  High-throughput proteomic analysis of candidate biomarker changes in gingival crevicular fluid after treatment of chronic periodontitis.

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6.  Identification of azurocidin as a potential periodontitis biomarker by a proteomic analysis of gingival crevicular fluid.

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Journal:  Sci Rep       Date:  2016-06-13       Impact factor: 4.379

  8 in total

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