Effect of isatin on nitric oxide-stimulated soluble guanylate cyclase from human platelets

Медведев, А. Е.; Bussygyna, Olga; Pyatakova, Natalia; Glover, Vivette; Severina, I. S.

doi:10.1016/s0006-2952(01)00809-7

Cited by 36 publications

(34 citation statements)

References 19 publications

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“…Представленные в настоящей работе результаты подтверждают колоколообразный характер торможения изатином стимулированной NO (но не базальной) активности рГЦ [7]; в диапазоне концентраций изатина от 1 до 100 нМ интенсивность торможения остается примерно на одном и том же уровне (38, 46 и 43%, соответственно) и затем снижается при более высоких концентрациях (до 33 и 19% при 1 и 10 мкМ, соответственно) (рис. 1).…”

Section: +unclassified

“…Изатин обладает широким спектром биологических эффектов in vivo и in vitro [1][2][3]. В физиологических концентрациях (в диапазоне от 1 нМ до 10 мкМ) изатин служит эндогенным ингибитором стимуляции мембраносвязанной гуанилатциклазы натрийуретическими пептидами [4,5]; он также тормозит активность моноаминоксидазы Б [6] и ингибирует индуцированную нитропруссидом натрия активацию растворимой гуанилатциклазы [7].…”

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“…Несколько лет назад мы показали, что изатин ингибирует индуцированную нитропруссидом натрия (SNP) активацию рГЦ [7]. Наиболее выраженное торможение, наблюдаемое при 10 -8 М концентрации изатина, -самый мощный (в концентрационном плане) эффект изатина.…”

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“…Кривая зависимости торможения рГЦ от концентрации изатина имела колоколообразную форму, и торможение этого фермента при высоких концентрациях изатина становилось менее сильным. Изатин не влиял на гем-независимую стимуляцию гуанилатциклазы протопорфиртном IX [7]. Это дает основание предположить, что в регуляции рГЦ изатином возможно участвует гем гуанилатциклазы.…”

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“…В соответствии с результатами наших предыдущих исследований [7], изатин в диапазоне концентраций от 1 нМ до 10 мкМ не влиял на базальную активность рГЦ тромбоцитов человека, но вызывал "колоколообразное торможение" активации рГЦ, индуцированной 10 мМ нитропруссидом натрия (SNP) (рис. 1).…”

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

et al. 2011

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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 M) 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.

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

et al. 2011

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Isatin, an endogenous nonpeptide biofactor: A review of its molecular targets, mechanisms of actions, and their biomedical implications

et al. 2018

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Isatin (indole-2,3-dione) is an oxidized indole. It is widely distributed in mammalian tissues and body fluids, where isatin concentrations vary significantly from <0.1 to > 10 µM. Isatin output is increased under conditions of stress. Exogenously administered isatin is characterized by low toxicity, mutagenicity, and genotoxicity in vivo. Cytotoxic effects of isatin on various cell cultures are usually observed at concentrations exceeding 100 µM. Binding of [ H]isatin to rat brain sections is consistent with its physiological concentrations. Proteomic analysis of mouse and rat brain isatin-binding proteins revealed about 90 individual proteins, which demonstrated significant interspecies differences (rat versus mouse). Certain evidence exist that redox state(s) and possibly other types of posttranslational modifications regulate affinity of target proteins to isatin. Recent data suggest that interacting with numerous intracellular isatin binding proteins, isatin can act as a regulator of complex protein networks in norm and pathology. Physiological concentrations of isatin in vitro inhibit monoamine oxidase B and natriuretic peptide receptor guanylate cyclase, higher (neuroprotective) concentrations (50-400 μM) cause apoptosis of various (including malignant tumor) cell lines and influence expression of certain apoptosis-related genes. Being administered in vivo, isatin exhibits various behavioral effects; it attenuates manifestations of MPTP-induced parkinsonism and tumor growth in experimental animal models. © 2017 BioFactors, 44(2):95-108, 2018.

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Isatin binding proteins in rat brain: In situ imaging, quantitative characterization of specific [³H]isatin binding, and proteomic profiling

Crumeyrolle-Arias¹,

Buneeva²,

Zgoda³

et al. 2009

J of Neuroscience Research

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Isatin (indole-2,3-dione) is an endogenous indole that has a distinct and discontinuous distribution in the brain and in other mammalian tissues and body fluids. Its output is increased under conditions of stress and anxiety. Its biological targets remain poorly characterized, although [(3)H]isatin binding sites have been demonstrated in various brain structures. In this study, by using a real-time beta-imager, [(3)H]isatin radioligand binding analysis, and proteomic identification of proteins specifically bound to the affinity sorbent 5-aminocaproyl-isatin-Sepharose, we have investigated the distribution of [(3)H]isatin specific binding sites in the rat brain, characterized their K(d) and B(max), and identified some individual brain isatin binding proteins. The binding of [(3)H]isatin to rat brain sections was saturable and characterized by K(d) values (of 0.2-0.3 microM) consistent with physiological concentrations. The highest B(max) was found in the hypothalamus, consistent with a role in stress. In most brain regions, the homologous inhibition of [(3)H]isatin binding by increasing concentrations of cold isatin demonstrated complex behavior suggesting involvement of various binding proteins characterized by different affinity to isatin. Affinity chromatography of Triton X-100 lysates of whole-brain homogenates on 5-aminocaproyl-isatin-Sepharose followed by subsequent proteomic analysis resulted in identification of 25 individual proteins, including glyceraldehyde-3-phosphate dehydrogenase, one of few previously reported isatin binding proteins, and a group of cytoskeleton-related proteins. These binding sites may be related to the known antiproliferative and proapoptotic activities of isatin.

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Effect of isatin on nitric oxide-stimulated soluble guanylate cyclase from human platelets

Cited by 36 publications

References 19 publications

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

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

Isatin, an endogenous nonpeptide biofactor: A review of its molecular targets, mechanisms of actions, and their biomedical implications

Isatin binding proteins in rat brain: In situ imaging, quantitative characterization of specific [³H]isatin binding, and proteomic profiling

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Effect of isatin on nitric oxide-stimulated soluble guanylate cyclase from human platelets

Cited by 36 publications

References 19 publications

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

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

Isatin, an endogenous nonpeptide biofactor: A review of its molecular targets, mechanisms of actions, and their biomedical implications

Isatin binding proteins in rat brain: In situ imaging, quantitative characterization of specific [3H]isatin binding, and proteomic profiling

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Isatin binding proteins in rat brain: In situ imaging, quantitative characterization of specific [³H]isatin binding, and proteomic profiling