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Department of Cell Biology, Duke University Medical Center, Durham, NC 27710
Surfactant protein A (SP-A) is an innate immune molecule that binds
foreign organisms that invade the lungs and targets them for phagocytic
clearance by the resident pulmonary phagocyte, the alveolar macrophage
(AM). We hypothesized that SP-A binds to and enhances macrophage uptake
of other nonself particles, specifically apoptotic polymorphonuclear
neutrophils (PMNs). PMNs are recruited into the lungs during
inflammation, but as inflammation is resolved, PMNs undergo apoptosis
and are phagocytosed by AMs. We determined that SP-A increases AM
phagocytosis of apoptotic PMNs 280 ± 62% above the no protein
control value. The increase is dose dependent, and heat-treated SP-A
still enhanced uptake, whereas deglycosylated SP-A had significantly
diminished ability to enhance phagocytosis. Surfactant protein D also
increased phagocytosis of apoptotic PMNs by 
125%. However, other
proteins that are structurally homologous to SP-A, mannose-binding
lectin and complement protein 1q, did not. SP-A enhances phagocytosis
via an opsonization-dependent mechanism and binds apoptotic PMNs
4-fold more than viable PMNs. Also, binding of SP-A to apoptotic
PMNs does not appear to involve SP-A’s lectin domain. These data
suggest that the pulmonary collectins SP-A and SP-D facilitate the
resolution of inflammation by accelerating apoptotic PMN
clearance.
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