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Am J Physiol Lung Cell Mol Physiol (July 22, 2002). doi:10.1152/ajplung.00366.2001
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Articles in PresS, published online ahead of print July 22, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00366.2001
Submitted on September 14, 2001
Accepted on July 10, 2002

Surfactant Protein A Enhances the Phagocytosis of C1q-coated Particles by Alveolar Macrophages1

Wendy T. Watford1, Molly B. Smithers1, Michael M. Frank2, and Jo Rae Wright1*

1 Department of Cell Biology, Duke University Medical Center, Durham, NC, USA
2 Department of Pediatrics, Duke University Medical Center, Durham, NC, USA

* To whom correspondence should be addressed. E-mail: j.wright{at}cellbio.duke.edu.

Surfactant protein A (SP-A) plays multiple roles in pulmonary host defense including stimulating bacterial phagocytosis by innate immune cells. Previously, SP-A was shown to interact with complement protein C1q. Our goal was to characterize further this interaction and elucidate its functional consequences. Radiolabeled SP-A bound solid-phase C1q but not other complement proteins tested. The lectin activity of SP-A was not required for binding to C1q. Because C1q is involved in bacterial clearance but alone does not efficiently enhance the phagocytosis of most bacteria, we hypothesize that SP-A enhances phagocytosis of C1q-coated antigens. SP-A enhanced by six-fold the percentage of rat alveolar macrophages in suspension which phagocytosed C1q-coated fluorescent beads. Furthermore, uptake of C1q-coated beads was enhanced when either beads or alveolar macrophages were pre-incubated with SP-A. In contrast, SP-A had no significant effect on the uptake of C1q-coated beads by alveolar macrophages adhered to plastic slides. We conclude that SP-A may serve a protective role in the lung by interacting with C1q to enhance the clearance of foreign particles.




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