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Papers In Press, published online ahead of print August 4, 2004
Internal Medicine, University of Michigan, Ann Arbor, MI 48109-0676
Corresponding Author: jshayman{at}umich.edu
Lung surfactant is the surface-active agent comprised of phospholipids and proteins that lines pulmonary alveolae. Surfactant stabilizes the alveolar volume by reducing surface tension. Previously, we identified a phospholipase A2, termed LPLA2, with specificity towards phosphatidylcholine and phosphatidylethanolamine. The phospholipase is localized to lysosomes, is calcium independent, has an acidic pH optimum, and transacylates ceramide. Here, we demonstrate that LPLA2 is selectively expressed in alveolar macrophages but not in peritoneal macrophages, peripheral blood monocytes, or other tissues. Other macrophage-associated phospholipase A2s do not show a comparable distribution. LPLA2 is of high specific activity and recognizes disaturated-phosphatidylcholine as substrate. The lysosomal phospholipase A2 activity is six times lower in alveolar macrophages from mice with a targeted deletion of GM-CSF, a model of impaired surfactant catabolism, compared to those from wild type mice. However, LPLA2 activity and protein levels are expressed in GM-CSF null mice in which GM-CSF is expressed as a transgene under the control of the SP-C promoter. Thus LPLA2 may be a major enzyme of pulmonary surfactant phospholipid degradation by alveolar macrophages and may be deficient in disorders of surfactant metabolism.
J. Biol. Chem, 10.1074/jbc.M407834200
Submitted on July 12, 2004
Revised on August 4, 2004
Accepted on August 4, 2004
Lysosomal phospholipase A2 is selectively expressed in alveolar macrophages
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