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Macrophage elastase kills bacteria within murine macrophages

Author

Listed:
  • A. McGarry Houghton

    (Allergy, and Critical Care Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, USA)

  • William O. Hartzell

    (Brigham and Women’s Hospital, Boston, Massachusetts 02115, USA)

  • Clinton S. Robbins

    (Allergy, and Critical Care Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, USA)

  • F. Xavier Gomis-Rüth

    (Proteolysis Lab, Molecular Biology Institute of Barcelona (CSIC), Barcelona Science Park, Helix Building, c/ Baldiri Reixac 15-21, 08028 Barcelona, Spain)

  • Steven D. Shapiro

    (Allergy, and Critical Care Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, USA)

Abstract

Antibacterial macrophages Normal physiologic roles for many of the matrix metalloproteinases (MMPs), an extensive family of zinc-dependent endopeptidases, remain poorly understood. Matrix metalloproteinase-12 (MMP-12, also known as macrophage elastase) is now shown to possess direct antimicrobial activity against Gram-positive and Gram-negative bacteria. This function of MMP-12 is associated with the carboxy-terminal domain of the molecule, rather than its catalytic site. And surprisingly — since MMPs are in the main active within the extracellular space — its antimicrobial activity is exerted within the cell. This work also highlights a role for macrophages in the earliest stages of acute bacterial infection, more familiarly regarded as the province of neutrophils.

Suggested Citation

  • A. McGarry Houghton & William O. Hartzell & Clinton S. Robbins & F. Xavier Gomis-Rüth & Steven D. Shapiro, 2009. "Macrophage elastase kills bacteria within murine macrophages," Nature, Nature, vol. 460(7255), pages 637-641, July.
    • Handle: RePEc:nat:nature:v:460:y:2009:i:7255:d:10.1038_nature08181
    DOI: 10.1038/nature08181
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