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1 Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710; and 2 Department of Anesthesiology, Hannover Medical School, 30625 Hannover, Germany
Surfactant protein (SP) A and SP-D are involved
in multiple immunomodulatory functions of innate host defense partly
via their interaction with alveolar macrophages (AMs). In addition,
both SP-A and SP-D bind to bacterial lipopolysaccharide (LPS). To
investigate the functional significance of this interaction, we first
tested the ability of SP-A and SP-D to enhance the binding of
tritium-labeled Escherichia coli LPS
to AMs. In contrast to SP-D, SP-A enhanced the binding of LPS by AMs in
a time-, temperature-, and concentration-dependent manner. Coincubation
with surfactant-like lipids did not affect the SP-A-mediated
enhancement of LPS binding. At SP-A-to-LPS molar ratios of
1:2-1:3, the LPS binding by AMs reached 270% of control values.
Second, we investigated the role of SP-A in regulating the degradation
of LPS by AMs. In the presence of SP-A, deacylation of LPS by AMs
increased by ~2.3-fold. Pretreatment of AMs with phosphatidylinositol-specific phospholipase C had no effect on the
SP-A-enhanced LPS binding but did reduce the amount of serum-enhanced LPS binding by 50%, suggesting that a cell surface molecule distinct from CD14 mediates the effect of SP-A. Together the results for the
first time provide direct evidence that SP-A enhances LPS binding and
degradation by AMs.
collectins; Escherichia coli lipopolysaccharide
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