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Am J Physiol Lung Cell Mol Physiol 276: L642-L649, 1999;
1040-0605/99 $5.00
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Vol. 276, Issue 4, L642-L649, April 1999

Formation of membrane lattice structures and their specific interactions with surfactant protein A

Nades Palaniyar1, Ross A. Ridsdale1, Stephen A. Hearn2, Fred Possmayer3, and George Harauz1

1 Department of Molecular Biology and Genetics, University of Guelph, Guelph N1G 2W1; 2 Department of Pathology, St. Joseph's Health Center, London N6A 4L6; and 3 Medical Research Council Group in Fetal and Neonatal Health and Development, Departments of Obstetrics and Gynaecology and Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5A5

Biological membranes exist in many forms, one of which is known as tubular myelin (TM). This pulmonary surfactant membranous structure contains elongated tubes that form square lattices. To understand the interaction of surfactant protein (SP) A and various lipids commonly found in TM, we undertook a series of transmission-electron-microscopic studies using purified SP-A and lipid vesicles made in vitro and also native surfactant from bovine lung. Specimens from in vitro experiments were negatively stained with 2% uranyl acetate, whereas fixed native surfactant was delipidated, embedded, and sectioned. We found that dipalmitoylphosphatidylcholine-egg phosphatidylcholine (1:1 wt/wt) bilayers formed corrugations, folds, and predominantly 47-nm-square latticelike structures. SP-A specifically interacted with these lipid bilayers and folds. We visualized other proteolipid structures that could act as intermediates for reorganizing lipids and SP-As. Such a reorganization could lead to the localization of SP-A in the lattice corners and could explain, in part, the formation of TM-like structures in vivo.

tubular myelin; surfactant protein A-tubular myelin interaction; pulmonary surfactant; dipalmitoylphosphatidylcholine; phosphatidylcholine


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