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Am J Physiol Lung Cell Mol Physiol 277: L511-L522, 1999;
1040-0605/99 $5.00
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Vol. 277, Issue 3, L511-L522, September 1999

Differential expression of stress proteins in nonhuman primate lung and conducting airway after ozone exposure

Reen Wu1,2,3, Yu Hua Zhao3, Charles G. Plopper2,3, Mary Mann-Jong Chang3, Ken Chmiel3, John J. Cross3, Alison Weir2, Jerold A. Last1,3, and Brian Tarkington3

1 Division of Pulmonary and Critical Care Medicine; 2 Department of Veterinary Anatomy, Physiology, and Cell Biology; and 3 Center for Comparative Respiratory Biology and Medicine, University of California, Davis, California 95616

The presence of seven stress proteins including various heat shock proteins [27-kDa (HSP27), 60-kDa (HSP60), 70-kDa (HSP70) and its constitutive form HSC70, and 90-kDa (HSP90) HSPs] and two glucose-regulated proteins [75-kDa (GRP75) and 78-kDa (GRP78) GRPs] in ozone-exposed lungs of nonhuman primates and in cultured tracheobronchial epithelial cells was examined immunohistochemically by various monoclonal antibodies. Heat treatment (42°C) resulted in increased HSP70, HSP60, and HSP27 and slightly increased HSC70 and GRP75 but no increase in GRP78 in primary cultures of monkey tracheobronchial epithelial cells. Ozone exposure did not elevate the expression of these HSPs and GRPs. All of these HSPs including HSP90, which was undetectable in vitro, were suppressed in vivo in monkey respiratory epithelial cells after ozone exposure. Both GRP75 and GRP78 were very low in control cells, and ozone exposure in vivo significantly elevated these proteins. These results suggest that the stress mechanism exerted on pulmonary epithelial cells by ozone is quite different from that induced by heat. Furthermore, differences between in vitro and in vivo with regard to activation of HSPs and GRPs suggest a secondary mechanism in vivo, perhaps related to inflammatory response after ozone exposure.

oxidant injury; immunohistochemistry; air pollutants


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