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28 March 2024
 
  » pubmed » pmid11242081

 Article overview


NO-independent regulatory site on soluble guanylate cyclase
J P Stasch ; E M Becker ; C Alonso-Alija ; H Apeler ; K Dembowsky ; A Feurer ; R Gerzer ; T Minuth ; E Perzborn ; U Pleiss ; H Schröder ; W Schroeder ; E Stahl ; W Steinke ; A Straub ; M Schramm ;
Date 8 Mar 2001
Journal Nature, 410 (6825), 212-5
AbstractNitric oxide (NO) is a widespread, potent, biological mediator that has many physiological and pathophysiological roles. Research in the field of NO appears to have followed a straightforward path, and the findings have been progressive: NO and cyclic GMP are involved in vasodilatation; glycerol trinitrate relaxes vascular smooth muscles by bioconversion to NO; mammalian cells synthesize NO; and last, NO mediates vasodilatation by stimulating the soluble guanylate cyclase (sGC), a heterodimeric (alpha/beta) haem protein that converts GTP to cGMP2-4. Here we report the discovery of a regulatory site on sGC. Using photoaffinity labelling, we have identified the cysteine 238 and cysteine 243 region in the alpha1-subunit of sGC as the target for a new type of sGC stimulator. Moreover, we present a pyrazolopyridine, BAY 41-2272, that potently stimulates sGC through this site by a mechanism that is independent of NO. This results in antiplatelet activity, a strong decrease in blood pressure and an increase in survival in a low-NO rat model of hypertension, and as such may offer an approach for treating cardiovascular diseases.
Source PubMed, pmid11242081 doi: 10.1038/35065611
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