Antimicrobial Proteins with Homology to Serine Proteases

  1. Joan Marsh Organizer and
  2. Jamie A. Goode
  1. Joelle E. Gabay

Published Online: 28 SEP 2007

DOI: 10.1002/9780470514658.ch14

Ciba Foundation Symposium 186 - Antimicrobial Peptides

Ciba Foundation Symposium 186 - Antimicrobial Peptides

How to Cite

Gabay, J. E. (2007) Antimicrobial Proteins with Homology to Serine Proteases, in Ciba Foundation Symposium 186 - Antimicrobial Peptides (eds J. Marsh and J. A. Goode), John Wiley & Sons, Ltd., Chichester, UK. doi: 10.1002/9780470514658.ch14

Author Information

  1. Department of Medicine, Division of Infectious Diseases, Box 125, Cornell University Medical College, 1300 York Avenue, New York, NY 10021, USA

Publication History

  1. Published Online: 28 SEP 2007

ISBN Information

Print ISBN: 9780471950257

Online ISBN: 9780470514658

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Keywords:

  • antimicrobial proteins;
  • homology;
  • serine proteases;
  • functional genes;
  • haemopoietic differentiation

Summary

The azurophil granule, a specialized lysosome of human neutrophils, contains a family of antimicrobial proteins with structural homology to serine proteases, the serprocidins. Three members of this family are serine proteases (cathepsin G, elastase and proteinase-3) and one is a proteolytically inactive homologue (azurocidin). They are synthesized as preproproteins with a characteristic leader peptide and a propiece, both of which are removed by processing enzymes to yield the mature protein. The functional genes for three serprocidins (elastase, proteinase-3 and azurocidin) are grouped in a single genetic locus on chromosome 19 and are coordinately expressed and regulated during haemopoietic differentiation. Multiple and sometimes overlapping biological functions are a feature of this family, yet they all seem to pertain to host immunity. The structural requirements for the function of one member of this group (azurocidin), particularly its antibiotic function, are under investigation.