Macrophage elastase kills bacteria within murine macrophages

A. McGarry Houghton (), William O. Hartzell, Clinton S. Robbins, F. Xavier Gomis-Rüth and Steven D. Shapiro
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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

Nature, 2009, vol. 460, issue 7255, 637-641

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.

Date: 2009
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DOI: 10.1038/nature08181

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