Isatin interaction with glyceraldehyde-3-phosphate dehydrogenase, a putative target of neuroprotective drugs: partial agonism with deprenyl

Медведев, А.Е.; Buneeva, O. A.; Gnedenko, O. V.; Fedchenko, V. I.; Медведева, М. В.; Ivanov, Yu. D.; Glover, Vivette; Sandler, M.

doi:10.1007/978-3-211-33328-0_11

Cited by 28 publications

(27 citation statements)

References 27 publications

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“…One of the proteins, “fished” from the brain homogenate by means of aminocaproyl‐isatin‐Sepharose, glyceraldehyde‐3‐phosphate dehydrogenase, was already known as an isatin binding protein (Medvedev et al,2006). A specific interaction between isatin and purified glyceraldehyde‐3‐phosphate dehydrogenase was demonstrated by means of two independent approaches, a biosensor technique (using an isatin analogue immobilized onto an optical biosensor cell) and a radioligand analysis employing [ 3 H]isatin (Medvedev et al,2006). The Spectrum Mill search score for glyceraldehyde‐3‐phosphate dehydrogenase of 27.1 was at the eighteenth position from the top of the best scored proteins, which suggests that the other proteins identified in this study might also exhibit interaction with isatin.…”

Section: Discussionmentioning

confidence: 99%

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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Section: Discussionmentioning

confidence: 99%

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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“…Con sequences of the decreased affinity of GAPDH for (putative) neuroprotector agents need better under standing and further studies. Isatin may be considered as a partial agonist of known neuroprotector deprenyl [3], which binds to GAPDH and prevents its translo cation to the nucleus and apoptosis [18,19].…”

Section: Resultsmentioning

confidence: 99%

“…Glyceraldehyde 3 phosphate dehydrogenase (GAPDH; EC 1.2.1.12), a classical glycolytic enzyme, attracts much attentions as the protein exhibiting var ious (patho)biological activities (see for review [1,2]) and a putative target for neuroprotective drugs [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

Oxidative modification of glyceraldehyde-3-phosphate dehydrogenase influences its interaction with endogenous neuroprotector isatin

Buneeva

Gnedenko

Медведева

et al. 2015

Biochem. Moscow Suppl. Ser. B

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Glyceraldehyde 3 phosphate dehydrogenase (GAPDH), a classical glycolytic redox sensitive enzyme, exhibits various non glycolytic functions, which are considered to be especially important for pro gression of various neurodegenerative diseases. GAPDH binds isatin (indole dione 2,3), an endogenous indole often used as a parent component in numerous derivatives demonstrating diverse pharmacological (including neuroprotector) activities. In this study we have investigated binding of intact and mildly oxidized GAPDH to immobilized isatin, using an optical biosensor technique, employing surface plasmon resonance (SPR), and the effect of isatin as a probe for this binding. Mild GAPDH oxidation by 70 µM H 2 O 2 increased enzyme dissociation from immobilized isatin. Since GAPDH is considered as a putative target for various neuroprotector agents, this suggests that its redox state determines sensitivity to neuroprotective agents, and oxidative stress typical for various neurodegenerative disorders may significantly reduce pharmacological effectiveness of such compounds.

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“…Accordingly, isatin ( Fig. 15; Table 11), an endogenous reversible MAO B inhibitor, was identified to bind to GAPDH without significant influence on its activity, where It binds to the same site as deprenyl and it was also proposed to possess similar neuroprotective properties [197]. …”

Section: Glyceraldehyde-3-phosphate Dehydro-genase (Gapdh)mentioning

confidence: 99%

A Direct Interaction Between Mitochondrial Proteins and Amyloid-β Peptide and its Significance for the Progression and Treatment of Alzheimer’s Disease

Benek¹,

Aitken²,

Hroch³

et al. 2015

CMC

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Abstract:The amyloid-β peptide (Aβ) has been associated with Alzheimer's disease (AD) for decades. The original amyloid cascade hypothesis declared that the insoluble extracellular plaques were responsible for Aβ toxicity. Later, this hypothesis has been updated and soluble intracellular Aβ forms and their effects within the cell have come into focus. Mitochondrial dysfunction plays an important role in the pathophysiology of AD. Aβ was detected inside mitochondria and several mitochondrial proteins were found to interact directly with Aβ. Such interactions can affect a protein's function and cause damage to the mitochondria and finally to the whole cell. This review summarizes the current knowledge of mitochondrial proteins directly interacting with Aβ and discusses their significance for the development of therapeutics in the treatment of AD.

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Isatin interaction with glyceraldehyde-3-phosphate dehydrogenase, a putative target of neuroprotective drugs: partial agonism with deprenyl

Cited by 28 publications

References 27 publications

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

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

Oxidative modification of glyceraldehyde-3-phosphate dehydrogenase influences its interaction with endogenous neuroprotector isatin

A Direct Interaction Between Mitochondrial Proteins and Amyloid-β Peptide and its Significance for the Progression and Treatment of Alzheimer’s Disease

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Isatin interaction with glyceraldehyde-3-phosphate dehydrogenase, a putative target of neuroprotective drugs: partial agonism with deprenyl

Cited by 28 publications

References 27 publications

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

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

Oxidative modification of glyceraldehyde-3-phosphate dehydrogenase influences its interaction with endogenous neuroprotector isatin

A Direct Interaction Between Mitochondrial Proteins and Amyloid-&#946; Peptide and its Significance for the Progression and Treatment of Alzheimer&#8217;s Disease

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

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

A Direct Interaction Between Mitochondrial Proteins and Amyloid-β Peptide and its Significance for the Progression and Treatment of Alzheimer’s Disease