Human Neutrophil Granule Cationic Protein CAP37 is a Specific Macrophage Chemotaxin that Shares Homology with Inflammatory Proteinases

  • John G. Morgan
  • H. Anne Pereira
  • Teresa Sukiennicki
  • John K. Spitznagel
  • James W. Larrick
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 305)

Abstract

Cationic antimicrobial protein CAP37 (Mr = 37 kD) is derived from the azurophilic granules of human PMN. In vitro and in vivo studies demonstrate that CAP37 is a novel monocyte-specific chemoattractant. The N-terminal amino acid sequence of CAP37 shares significant homology with a number of inflammatory molecules with protease activity including elastase and cathepsin G. However, substitutions in the catalytic triad (serine for a histidine at position 41 and glycine for a serine at position 175), may account for its lack of serine protease activity. A full length cDNA for CAP37 was identified in an HL60 cDNA library screened with oligonucleotide probes designed from the N-terminal amino acid sequence. Sequencing of the cDNA reveals a protein of 225 amino acids with significant nucleotide homology to cathepsin G and human neutrophil elastase.

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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • John G. Morgan
    • 1
  • H. Anne Pereira
    • 2
  • Teresa Sukiennicki
    • 1
  • John K. Spitznagel
    • 2
  • James W. Larrick
    • 1
  1. 1.Genelabs Inc.Redwood CityUSA
  2. 2.Dept. of Microbiology and ImmunologyEmory University School of MedicineAtlantaUSA

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