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Am J Physiol Lung Cell Mol Physiol 279: L216-L223, 2000;
1040-0605/00 $5.00
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Vol. 279, Issue 2, L216-L223, August 2000

Surfactant protein A enhances mycobacterial killing by rat macrophages through a nitric oxide-dependent pathway

Laura F. Weikert1, Joseph P. Lopez2, Rasul Abdolrasulnia1, Zissis C. Chroneos3, and Virginia L. Shepherd2,4

Departments of 1 Medicine and 2 Pathology, Vanderbilt University School of Medicine, and 4 Veterans Affairs Medical Center, Nashville, Tennessee 37212; and 3 Children's Hospital Medical Center, Cincinnati, Ohio 45229

Surfactant-associated protein A (SP-A) is involved in surfactant homeostasis and host defense in the lung. We have previously demonstrated that SP-A specifically binds to and enhances the ingestion of bacillus Calmette-Guerin (BCG) organisms by macrophages. In the current study, we investigated the effect of SP-A on the generation of inflammatory mediators induced by BCG and the subsequent fate of ingested BCG organisms. Rat macrophages were incubated with BCG in the presence and absence of SP-A. Noningested BCG organisms were removed, and the release of tumor necrosis factor-alpha (TNF-alpha ) and nitric oxide were measured at varying times. TNF-alpha and nitric oxide production induced by BCG were enhanced by SP-A. In addition, SP-A enhanced the BCG-induced increase in the level of inducible nitric oxide synthase protein. Addition of antibodies directed against SPR210, a specific macrophage SP-A receptor, inhibited the SP-A-enhanced mediator production. BCG in the absence of SP-A showed increased growth over a 5-day period, whereas inclusion of SP-A dramatically inhibited BCG growth. Inhibition of nitric oxide production blocked BCG killing in the presence and absence of SP-A. These results demonstrate that ingestion of SP-A-BCG complexes by rat macrophages leads to production of inflammatory mediators and increased mycobacterial killing.

phagocytosis; mycobacteria; surfactant-associated protein A


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