Abstract
Surfactant protein A (SP-A) forms large complexes with other surfactant molecules such as tubular myelin. Functionally, SP-A contributes to tubular myelin formation, increased surfactant spreading, the stabilization of phospholipid complexes, or inhibition of surfactant secretion. SP-A can enhance the uptake of bacteria and viruses by alveolar macrophages. This chapter presents a study in which, at high phospholipid concentrations, SP-A–/– mice produced the same surface tension as wild-type mice and had no apparent defects in lung morphology, type II cell morphology, lung compliance, phospholipid composition, or the surfactant proteins B, C, and D. At low phospholipid concentrations, SP-A–/– mice displayed reduced surface activity. Tubular myelin figures were decreased, indicating that SP-A primarily regulates tubular myelin formation without changes in survival or lung functions.
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