Granzyme B and perforin: constitutive expression in human polymorphonuclear neutrophils

Blood. 2004 Feb 1;103(3):1099-104. doi: 10.1182/blood-2003-04-1069. Epub 2003 Sep 25.


Polymorphonuclear neutrophils (PMNs) produce an abundance of bactericidal and cytotoxic molecules consistent with their role as first-line defense against bacterial infection. PMNs, however, also cause efficient cellular cytotoxicity when targeted through Fc receptors to appropriate antibody-coated target cells. Although this so-called antibody-dependent cellular cytotoxicity (ADCC) was described many years ago, the mechanism of killing is still elusive. We now have found that PMNs contain perforin and granzyme B, the 2 molecules known as the cytotoxic entity of natural killer cells and of cytotoxic T lymphocytes as well. Lysates of PMNs were lytic for chicken erythrocytes in a time-, temperature-, and Ca(2+)-dependent manner. Moreover, apoptosis of Jurkat cells was induced, consistent with the observation that the PMN lysates contain enzymatically active granzyme B. Taken together, our data provide evidence for the presence of perforin and granzyme B within the cytotoxic arsenal of PMNs.

MeSH terms

  • Animals
  • Antibody-Dependent Cell Cytotoxicity
  • Apoptosis
  • Cells, Cultured
  • Chickens
  • Erythrocytes / immunology
  • Granzymes
  • Hemolysis
  • Humans
  • In Vitro Techniques
  • Interferon-gamma / pharmacology
  • Jurkat Cells
  • Membrane Glycoproteins / metabolism*
  • Neutrophils / drug effects
  • Neutrophils / immunology*
  • Neutrophils / metabolism*
  • Perforin
  • Pore Forming Cytotoxic Proteins
  • Recombinant Proteins
  • Serine Endopeptidases / metabolism*
  • T-Lymphocytes, Cytotoxic / immunology


  • Membrane Glycoproteins
  • Pore Forming Cytotoxic Proteins
  • Recombinant Proteins
  • Perforin
  • Interferon-gamma
  • GZMB protein, human
  • Granzymes
  • Serine Endopeptidases