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Articles in PresS, published online ahead of print July 3, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00365.2001
Submitted on September 13, 2001
Accepted on June 3, 2002
1 Department of Pharmacology, New York Medical College, Valhalla, NY, USA
2 Department of Physiology, New York Medical College, Valhalla, NY, USA
3 Department of Medicine, New York Medical College, Valhalla, NY, USA
* To whom correspondence should be addressed. E-mail: nader_abraha{at}nymc.edu.
Carbon monoxide (CO) stimulates guanylate cyclase (GC) and increases cyclic GMP (cGMP) levels. We transfected rat lung microvessel (RLMV) endothelial cells with a retroviral-mediated human HO-1. RLMV cells expressing human HO-1 (RLMV-HHO-1) exhibited a 4-fold increase in HO activity associated with decreases in the steady-state levels of heme and cGMP, without changes in sGC and eNOS proteins or basal nitrite production. Heme elicited significant increases in CO production and intracellular cGMP levels in both RLMV and RLMV-HHO-1 cells. L-NAME, an inhibitor of nitric oxide synthase (NOS), significantly decreased cGMP levels in heme-treated RLMV cells, but not in heme-treated RLMV-HHO-1 cells. In the presence of exogenous heme, CO and cGMP levels in RLMV-HHO-1 cells exceeded the corresponding levels in RLMV cells. Acute exposure of endothelial cells to SnCl2, an inducer of HO-1, increased cGMP whereas chronic exposure decreased heme levels along with cGMP. These results indicate that prolonged overexpression of HO-1 ultimately decreases sGC activity by limiting the availability of cellular heme. Heme activates sGC and enhances cGMP levels via a mechanism that is largely insensitive to NOS inhibition.
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