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Am J Physiol Lung Cell Mol Physiol (June 21, 2002). doi:10.1152/ajplung.00064.2002
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Articles in PresS, published online ahead of print June 21, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00064.2002
Submitted on February 20, 2002
Accepted on June 10, 2002

Nitric oxide inhibits ADP-ribosyl cyclase through a cyclic GMP independent pathway in airway smooth muscle

Thomas A. White1, Timothy F. Walseth2, and Mathur S. Kannan1*

1 Department of Veterinary PathoBiology, University of Minnesota, St. Paul, MN, USA
2 Department of Pharmacology, University of Minnesota, Minneapolis, MN, USA

* To whom correspondence should be addressed. E-mail: kanna001{at}tc.umn.edu.

There is evidence for a role of cyclic ADP-ribose (cADPR) in intracellular calcium regulation in smooth muscle. cADPR is synthesized and degraded by ADP-ribosyl cyclase and cADPR hydrolase, respectively by a bifunctional protein, CD38. Nitric oxide (NO) inhibits intracellular calcium mobilization in airway smooth muscle. The present study was designed to determine if this inhibition is due to regulation of ADP-ribosyl cyclase and/or cADPR hydrolase activities. Sodium nitroprusside (SNP) and s-nitroso-n-acetylpenicillamine (SNAP), NO donors, produced a concentration-dependent decrease in ADP-ribosyl cyclase, but not cADPR hydrolase, activity. The NO scavenger carboxy-PTIO prevented and reversed, and reduced glutathione prevented the inhibition of ADP-ribosyl cyclase by SNP, suggesting S-nitrosylation by NO as a mechanism. N-ethylmaleimide (NEM), which covalently modifies protein sulfhydryl groups making them incapable of nitrosylation, produced a marked inhibition of ADP-ribosyl cyclase, but not cADPR hydrolase, activity. Both SNP and NEM significantly inhibited the ADP-ribosyl cyclase activity in recombinant human CD38 without affecting the cADPR hydrolase activity. These results provide a novel mechanism for differential regulation of CD38 by NO through a cGMP-independent pathway involving S-nitrosylation of thiols.




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