Interaction of synapsin IIb with calmodulin: Identification of a high affinity site

Nicol, Scott; Rahman, Daisy; Baines, Anthony J.

doi:10.1042/bst026s109

Cited by 2 publications

(2 citation statements)

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“…Out of three synapsin IIb expression forms, only one (spot 3) was increased pointing to hypoxia-specific regulation or at least hypoxia-ischemia-dependent regulation. The consequence of altered synapsin IIb levels may also lead to changes in levels and probably function of the many binding partners and interactions in particular with signaling proteins. , …”

Section: Discussionmentioning

confidence: 99%

“…The consequence of altered synapsin IIb levels may also lead to changes in levels and probably function of the many binding partners and interactions in particular with signaling proteins. 65,66 One of the signaling proteins observed herein with increased levels at the early phase of PA is adenylyl cyclase-associated protein 1(CAP); it is an adenylyl cyclase activating protein cooperating with Ras, that binds to the cyclase at a different region. With another domain, CAP can bind monomeric actin and is therefore carrying out scaffolding functions.…”

Section: Differences In Hippocampal Proteinmentioning

confidence: 99%

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Differences in Hippocampal Protein Expression at 3 Days, 3 Weeks, and 3 Months Following Induction of Perinatal Asphyxia in the Rat

et al. 2008

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Perinatal asphyxia (PA) was induced in Sprague-Dawley rats; pups were sacrificed 3 days, 3 weeks, and 3 months following the asphyctic insult, and hippocampal protein levels were determined by a gel-based proteomic method. Levels of antioxidant, metabolic, cytoskeleton, signaling, channel, proteasomal, chaperone, splicing, and synaptosomal proteins were dysregulated depending on the age following induction of PA. These proteins are proposed to be potential markers or pharmacological targets for PA.

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Section: Discussionmentioning

confidence: 99%

Section: Differences In Hippocampal Proteinmentioning

confidence: 99%

Differences in Hippocampal Protein Expression at 3 Days, 3 Weeks, and 3 Months Following Induction of Perinatal Asphyxia in the Rat

et al. 2008

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Molecular mechanisms of the non-coenzyme action of thiamin in brain: biochemical, structural and pathway analysis

Mkrtchyan

Aleshin

Parkhomenko

et al. 2015

Sci Rep

114

124

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Thiamin (vitamin B1) is a pharmacological agent boosting central metabolism through the action of the coenzyme thiamin diphosphate (ThDP). However, positive effects, including improved cognition, of high thiamin doses in neurodegeneration may be observed without increased ThDP or ThDP-dependent enzymes in brain. Here, we determine protein partners and metabolic pathways where thiamin acts beyond its coenzyme role. Malate dehydrogenase, glutamate dehydrogenase and pyridoxal kinase were identified as abundant proteins binding to thiamin- or thiazolium-modified sorbents. Kinetic studies, supported by structural analysis, revealed allosteric regulation of these proteins by thiamin and/or its derivatives. Thiamin triphosphate and adenylated thiamin triphosphate activate glutamate dehydrogenase. Thiamin and ThDP regulate malate dehydrogenase isoforms and pyridoxal kinase. Thiamin regulation of enzymes related to malate-aspartate shuttle may impact on malate/citrate exchange, responsible for exporting acetyl residues from mitochondria. Indeed, bioinformatic analyses found an association between thiamin- and thiazolium-binding proteins and the term acetylation. Our interdisciplinary study shows that thiamin is not only a coenzyme for acetyl-CoA production, but also an allosteric regulator of acetyl-CoA metabolism including regulatory acetylation of proteins and acetylcholine biosynthesis. Moreover, thiamin action in neurodegeneration may also involve neurodegeneration-related 14-3-3, DJ-1 and β-amyloid precursor proteins identified among the thiamin- and/or thiazolium-binding proteins.

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Interaction of synapsin IIb with calmodulin: Identification of a high affinity site

Cited by 2 publications

References 4 publications

Differences in Hippocampal Protein Expression at 3 Days, 3 Weeks, and 3 Months Following Induction of Perinatal Asphyxia in the Rat

Differences in Hippocampal Protein Expression at 3 Days, 3 Weeks, and 3 Months Following Induction of Perinatal Asphyxia in the Rat

Molecular mechanisms of the non-coenzyme action of thiamin in brain: biochemical, structural and pathway analysis

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