Am. J. Respir. Cell Mol. Biol., Volume 20, Number 5, May, 1999 1049-1058

Ultrastructure of Phospholipid Mixtures Reconstituted with Surfactant Proteins B and D

Francis R. Poulain, Jennifer Akiyama, Lennell Allen, Cindy Brown, Rupert Chang, Jon Goerke, Leland Dobbs, and Sam Hawgood

Cardiovascular Research Institute and Departments of Pediatrics, Medicine, and Physiology, University of California San Francisco, San Francisco, California

Surfactant protein (SP)-D is secreted from pulmonary alveolar type II cells into the alveolar lumen where potential interactions with surfactant lipids might occur. SP-D binds phosphatidylinositol (PI), a component of mammalian surfactants that is increased in a variety of injury states. We investigated the ultrastructure and properties of lipid protein recombinants that included SP-D, PI, and SP-B and compared these with recombinants based on SP-A. SP-D had a profound effect on the organization of phospholipid vesicles containing PI and SP-B, promoting the formation of atypical but highly ordered and surface-active tubular aggregates distinct in their dimensions and shape from the classical tubular myelin formed by SP-A. We also found both types of tubules in the secretions of type II cells maintained in long-term culture. These results suggest that surface atypical tubules can be formed with SP-D in vitro and in vivo.

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