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

   


1. Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences
2. Blokhin Cancer Center, Russian Academy of Medical Sciences
Type: Experimental/clinical study
UDK: 613.632.615. 36      PubMed Id: 19205427
Year: 2008 vol: 54  issue:6  pages: 679-686
Abstract: 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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Reference: Severina I.S., Pyatakova N.V., Shchegolev A.Y., Sidorova T.A., YC-1-like potentiation of nitric oxide-dependent activation of soluble guanylyl cyclase by adrenochrome, Biomeditsinskaya khimiya, 2008, vol: 54(6), 679-686.
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