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, Sam Hawgood

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1049-1058
Number of pages10
JournalAmerican Journal of Respiratory Cell and Molecular Biology
Volume20
Issue number5
StatePublished - 1999
Externally publishedYes

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ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Pulmonary and Respiratory Medicine

Cite this

Poulain, F. R., Akiyama, J., Allen, L., Brown, C., Chang, R., Goerke, J., Dobbs, L., & Hawgood, S. (1999). Ultrastructure of phospholipid mixtures reconstituted with surfactant proteins B and D. American Journal of Respiratory Cell and Molecular Biology, 20(5), 1049-1058.