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A more recent version of this article appeared on June 1, 2004

Papers In Press, published online ahead of print March 16, 2004
J. Lipid Res., doi:10.1194/jlr.M300360-JLR200
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Submitted on August 26, 2003
Revised on March 4, 2004
Accepted on March 5, 2004

Surfactant protein oxidation: surfactant lipid peroxidation damages surfactant protein A (SP-A) and inhibits interactions with phospholipid vesicles

A. I. Kuzmenko, H. Wu, J. P. Bridges, and F. X. McCormack

Division of Pulmonary and Critical Care Medicine, University of Cincinnati, Cincinnati, OH 45267

Corresponding Author: akuzm{at}yahoo.com

The goal of these studies was to examine the effect of phospholipid peroxidation (LPO) on the function of surfactant protein A (SP-A). Surfactant phospholipids were incubated with free-radical generators, in the absence or presence of the SP-A, or bovine serum albumin as a control. We found that SP-A inhibited copper-initiated LPO to an extent that was similar to bovine serum albumin (p<0.05). Exposure of SP-A to LPO was associated with an increase in the level of SP-A-associated carbonyl moieties and a marked reduction in SP-A mediated aggregation of liposomes. LPO initiated by an azo-compound also resulted in enhanced protein oxidation, and markedly inhibited SP-A-mediated liposome aggregation. The kinetics of aggregation of auto-oxidized and non-oxidized liposomes by non-oxidized SP-A was similar suggesting that SP-A has similar affinities for oxidized and non-oxidized lipids. Oxidative inactivation of SP-A did not occur upon direct incubation of the protein with malondialdehyde alone. We conclude that exposure of SP-A to LPO results in oxidative modification and functional inactivation of SP-A by phospholipid radicals.


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