AJP - Lung Cellular and Molecular Physiology, Vol 261, Issue 2 77-L83, Copyright © 1991 by American Physiological Society

ARTICLES

Structural and functional changes of surfactant protein A induced by ozone

R. S. Oosting, M. M. van Greevenbroek, J. Verhoef, L. M. van Golde and H. P. Haagsman
Laboratory of Veterinary Biochemistry, Utrecht University, The Netherlands.

The major surfactant protein SP-A is thought to play an important role in the regulation of the structure and the metabolism of pulmonary surfactant. We investigated whether this protein may be a target in ozone toxicity. Several properties were studied that are probably relevant to the physiological functions of SP-A. In vitro exposure of human and canine SP-A to ozone led to decreases in 1) self-association of SP-A, 2) SP-A-mediated lipid aggregation, and 3) binding of SP-A to immobilized mannose. SP-A was neither degraded nor cross-linked by ozone exposure. Exposure of canine SP-A to ozone led to an increase in the apparent molecular weight of monomeric SP-A. Human SP-A did not show this change. Oxidation of methionine and tryptophan residues in canine SP-A was detected following ozone exposure. Reactions of ozone with other amino acid residues were not observed. The impairments of structure and properties of SP-A may contribute to the toxic action of ozone in the lungs.

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