YC-1-like potentiation of nitric oxide-dependent activation of soluble guanylyl cyclase by adrenochrome

   
Severina I.S.1 , Pyatakova N.V.1, Shchegolev A.Y.1, Sidorova T.A.2

1. Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences
2. Blokhin Cancer Center, Russian Academy of Medical Sciences
Section: Experimental/Clinical Study
PubMed Id: 19205427
Year: 2008  Volume: 54  Issue: 6  Pages: 679-686
The influence of adrenochrome and YC-1 on spermine NONO-induced activation of human soluble guanylyl cyclase was investigated. Adrenochrome (0.1-10 μM) had no effect on the basal activity, but it potentiated in concentration-dependent manner the spermine NONO-induced activation of this enzyme. Adrenochrome, like YC-1, sensitized guanylyl cyclase towards nitric oxide (NO) and produced the leftward shift of spermine NONO concentration responce curve. Addition of adrenochrome decreased the YC-1-induced leftward shift of spermine NONO concentration response curve. Adrenochrome also inhibited (by 63%) the enzyme activation by YC-1. These data demonstrates the possible competition between adrenochrome and YC-1. Thus, synergistic activation of NO-stimulated guanylyl cyclase activity by adrenochrome represents a new biochemical effect of this compound and indicates that adrenochrome may act as an endogenous regulator of NO-dependent stimulation of soluble guanylyl cyclase. This new property of adrenochrome, similar to YC-1, is necessary taking into account, especially under conditions of overproduction of adrenochrome in organism.
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Keywords: guanylyl cyclase, nitric oxide (NO), adrenochrome
Citation:

Severina, I. S., Pyatakova, N. V., Shchegolev, A. Y., Sidorova, T. A. (2008). YC-1-like potentiation of nitric oxide-dependent activation of soluble guanylyl cyclase by adrenochrome. Biomeditsinskaya Khimiya, 54(6), 679-686.
This paper is also available as the English translation: 10.1134/S1990750809010053
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