Inhibition of NO-dependent soluble human platelet guanylate cyclase by isatin View Full Text


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Article Info

DATE

2011-08-18

AUTHORS

I. S. Severina, A. Yu. Schegolev, G. V. Ponomarev, A. E. Medvedev

ABSTRACT

Isatin (indole-dione-2,3) is an endogenous indole that exhibits a wide spectrum of biological and pharmacological activities. Physiologically relevant concentrations of isatin (ranged from 1 nM to 10 μM) did not influence basal activity of soluble human platelet guanylate cyclase (sGC), but caused a bell-shaped inhibition of the NO-activated enzyme. Inhibition of the NO-dependent activation by isatin did not depend on a chemical nature of the NO donors. The inhibitory effects of ODC (a heme-dependent inhibitor of sGC) and isatin were non-additive suggesting that the inhibitory effect of isatin may involve the heme binding domain (possibly heme iron) and experiments with hemin revealed some isatin-dependent changes in its spectrum. Isatin also inhibited sGC activation by the allosteric activator YC-1. It is suggested that the bell shaped inhibition of the NO-dependent activation of sGC by isatin may be attributed to complex interaction of isatin with the heme binding domain and the allosteric YC-1-binding site of sGC. More... »

PAGES

263

References to SciGraph publications

  • 2009. NO-Independent, Haem-Dependent Soluble Guanylate Cyclase Stimulators in CGMP: GENERATORS, EFFECTORS AND THERAPEUTIC IMPLICATIONS
  • 2006-09. NO-independent stimulators and activators of soluble guanylate cyclase: discovery and therapeutic potential in NATURE REVIEWS DRUG DISCOVERY
  • 2009. A Short History of cGMP, Guanylyl Cyclases, and cGMP-Dependent Protein Kinases in CGMP: GENERATORS, EFFECTORS AND THERAPEUTIC IMPLICATIONS
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    http://scigraph.springernature.com/pub.10.1134/s1990750811030115

    DOI

    http://dx.doi.org/10.1134/s1990750811030115

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