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Divisions of
*
Neonatology and Pulmonary Biology and
Critical Care Medicine, Cincinnati Children’s Hospital Medical Center, Cincinnati, OH 45229; and
Division of Pulmonary and Critical Care Medicine, Brigham and Women’s Hospital, Boston, MA 02115
Surfactant protein D (SP-D) and CD14 are important innate immune defense molecules that mediate clearance of pathogens and apoptotic cells from the lung. To test whether CD14 expression and function were influenced by SP-D, the surface expression of CD14 was assessed on alveolar macrophages from SP-D–/– mice. CD14 was reduced on alveolar macrophages from SP-D–/– mice and was associated with reduced uptake of LPS and decreased production of TNF-
after LPS stimulation. CD14 is proteolytically cleaved from the cell surface to form a soluble peptide. Soluble CD14 (sCD14) was increased in the bronchoalveolar lavage fluid from SP-D–/– mice. Because matrix metalloproteinase (MMP)-9 and -12 activities were increased in the lungs of SP-D–/– mice, the role of these metalloproteases in the production of sCD14 was assessed. sCD14 was decreased in both MMP9–/–/SP-D–/– and MMP12–/–/SP-D–/– mice demonstrating MMP-9 and MMP-12 contribute to proteolytic shedding of CD14. The increased sCD14 seen in SP-D–/– mice was dependent upon the activation of MMP-12 via an MMP-9-dependent mechanism. Supporting this observation, MMP-12 caused the release of sCD14 from RAW 264.7 cells in vitro. In conclusion, SP-D influences innate host defense, in part, by regulating sCD14 in a process mediated by MMP-9 and MMP-12.
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