The Ca2+/calmodulin signaling system in the neural response to excitability. involvement of neuronal and glial cells

Solà, Carme; Barrón, Sonia; Tusell, Josep Maria; Serratosa, Joan

doi:10.1016/s0301-0082(98)00082-3

Cited by 29 publications

(15 citation statements)

References 142 publications

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“…Calmodulin (CaM) is an effector of calcium signaling and has a central role in neurodegenerative processes such as plasticity, learning, and memory (Klee et al, 1980;Sola et al, 1999). CaM participates in synaptic function and neurotransmitter release, playing a role in Ca 21 -stimulated phosphorylation of synaptic proteins (Delorenzo et al, 1982).…”

Section: Calcium Signaling Proteinsmentioning

confidence: 99%

The wheat germ agglutinin‐fractionated proteome of subjects with Alzheimer's disease and mild cognitive impairment hippocampus and inferior parietal lobule: Implications for disease pathogenesis and progression

Domenico

Owen

Sultana

et al. 2010

J of Neuroscience Research

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Lectin affinity chromatography is a powerful separation technique that fractionates proteins by selectively binding to specific carbohydrate moieties characteristic of protein glycosylation type. Wheat germ agglutinin (WGA) selectively binds terminal N-acetylglucosamine (O-GlcNAc) and sialic acid moieties characteristic of O-linked glycosylation. The current study utilizes WGA affinity chromatography to fractionate proteins from hippocampus and inferior parietal lobule (IPL) from subjects with Alzheimer's disease (AD) and arguably its earliest form, mild cognitive impairment (MCI). Proteins identified by proteomics that were fractionated from MCI and AD hippocampus by WGA affinity chromatography with altered levels compared with age-matched controls included GP96, γ-enolase, glutamate dehydrogenase, glucosidase IIα, 14-3-3ϵ, 14-3-3γ, 14-3-3ζ, tropomyosin-2, calmodulin 2, gelsolin, β-synuclein, α1-antichymotrypsin, and dimethylguanosine tRNA methyltransferase. Proteins identified by proteomics that were fractionated from MCI and AD IPL by WGA affinity chromatography showing altered levels compared with age-matched controls included protein disulfide isomerase, calreticulin, and GP96. The proteins described in this study are involved in diverse processes, including glucose metabolism, endoplasmic reticulum (ER) functions, chaperoning, cytoskeletal assembly, and proteolysis, all of which are affected in AD. This study, the first to use proteomics to identify WGA-fractionated proteins isolated from brains from subjects with MCI and AD, provides additional information about the active proteome of the brain throughout AD progression.

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Section: Calcium Signaling Proteinsmentioning

confidence: 99%

The wheat germ agglutinin‐fractionated proteome of subjects with Alzheimer's disease and mild cognitive impairment hippocampus and inferior parietal lobule: Implications for disease pathogenesis and progression

Domenico

Owen

Sultana

et al. 2010

J of Neuroscience Research

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“…has been shown to regulate ion channels and neuronal excitability in both vertebrates (1)(2)(3)(4)(5)(6) and invertebrates (4,5,(7)(8)(9)(10)(11). Regulation of excitability has been proposed as a mechanism by which neurons can globally modify their firing to keep spike rates in a scalable range in the presence of synapse-specific plasticity (12)(13)(14).…”

mentioning

confidence: 99%

The eag Potassium Channel Binds and Locally Activates Calcium/Calmodulin-dependent Protein Kinase II

Sun

Hodge

Zhou

et al. 2004

Journal of Biological Chemistry

118

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Ca 2؉/calmodulin-dependent protein kinase II (CaMKII) has been implicated in the regulation of neuronal excitability in many systems. Recent studies suggest that local regulation of membrane potential can have important computational consequences for neuronal function. In Drosophila, CaMKII regulates the eag potassium channel, but if and how this regulation was spatially restricted was unknown. Calcium/calmodulin-dependent protein kinase II (CaMKII) 1 has been shown to regulate ion channels and neuronal excitability in both vertebrates (1-6) and invertebrates (4,5,(7)(8)(9)(10)(11). Regulation of excitability has been proposed as a mechanism by which neurons can globally modify their firing to keep spike rates in a scalable range in the presence of synapse-specific plasticity (12)(13)(14). Recently, it has become clear that regulation of excitability can also occur as a local phenomenon (15-19). Regional changes in excitability mediated by differing levels of A-type potassium currents were shown to be important for gating Hebbian plasticity in CA1 pyramidal cell dendrites and limiting propagation of action potentials (19). These effects have important implications for the computational abilities of neurons that integrate over many inputs. Both slow, expression level changes and fast, enzymatic modifications could underlie local phenomena, and in CA1, local regulation of excitability was associated with both regional differences in current density (19) and region-specific post-translational modifications of ion channels (18). Fast modulation offers the advantage of dynamic retooling of the computational capability of the neuron.For signal transduction pathways to effect fast local changes in excitability, the activity of effector enzymes has to be spatially restricted. The ability of protein kinases with many substrates to act with specificity to regulate cellular functions is increasingly being ascribed to interactions with scaffolding molecules that bring kinases and their substrates into close proximity. Signaling platforms range from small complexes containing only a few proteins to very complex cellular specializations like the postsynaptic density of the mammalian central nervous system (20). The advantages of scaffolding enzymes and substrates include enhancement of reaction rates because of elimination of diffusional barriers and increased local concentration of substrates and segregation of the enzyme to prevent reaction with other substrates. Localization of effector enzymes to sources of small molecule regulators can also establish very restricted signaling domains. Scaffolding may be particularly important for regulation of membrane-bound proteins in neurons; diffusion in the membrane bilayer is relatively slow, and the ability of soluble enzymes to access substrates can be influenced by the complex geometry of neurons.The regulation of firing in Drosophila motor axons involves the ether-à -go-go (eag) potassium channel. eag is the founding member of an evolutionarily conserved superfamily of voltageg...

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“…CaMKs are well known as metabolic components appearing downstream of calcium and calmodulin signal transduction pathways (Klee, ; Solà et al, ; Nakanishi and Okazawa, ; Bell et al, ). Activated CaMKs phosphorylate CREB, and phosphorylated CREB in turn increases cFos production (Sato et al, ).…”

Section: Discussionmentioning

confidence: 99%

Nicotinic acetylcholine receptors regulate type 1 inositol 1,4,5-trisphosphate receptor expression via calmodulin kinase IV activation

Mizuno

Kurokawa

Ohkuma

2014

Journal of Neuroscience Research

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Type 1 inositol 1,4,5-trisphosphate receptors (IP3 R-1) are among the important calcium channels regulating intracellular Ca(2+) concentration in the central nervous system. In a previous study, we showed that drugs of abuse, such as cocaine, methamphetamine, and ethanol, induced IP3 R-1 upregulation via the calcium signal transduction pathway in psychological dependence. Although nicotine, a major component in tobacco smoke, participates in psychological and/or physical dependence, it has not yet been clarified how nicotine alters IP3 R-1 expression. The present study, therefore, seeks to clarify the mechanism bgy which nicotine modifies IP3 R-1 expression by using mouse cerebral cortical neurons in primary culture. Nicotine induced dose- and time-dependent upregulation of IP3 R-1 protein following its mRNA increase, and the latter was significantly suppressed by a nonselective nicotinic acetylcholine receptors (nAChR) antagonist, mecamylamine. Both cFos and phosphorylated-cJun (p-cJun) were immediately increased in the nucleus, together with an increase of calmodulin kinase (CaMK) IV but not CaMKII expression after nicotine exposure. A nonselective inhibitor of CaMKs, KN-93, and a calcium chelating regent, BAPTA-AM, completely suppressed the expression of cFos and p-cJun in the nucleus as well as the nicotine-induced IP3 R-1 upregulation. These results indicate that nAChR activation by nicotine upregulates IP3 R-1 via increase of activator protein-1, which is a cFos and cJun dimmer, in the nucleus, with activation of Ca(2+) signaling transduction processes.

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The Ca2+/calmodulin signaling system in the neural response to excitability. involvement of neuronal and glial cells

Cited by 29 publications

References 142 publications

The wheat germ agglutinin‐fractionated proteome of subjects with Alzheimer's disease and mild cognitive impairment hippocampus and inferior parietal lobule: Implications for disease pathogenesis and progression

The wheat germ agglutinin‐fractionated proteome of subjects with Alzheimer's disease and mild cognitive impairment hippocampus and inferior parietal lobule: Implications for disease pathogenesis and progression

The eag Potassium Channel Binds and Locally Activates Calcium/Calmodulin-dependent Protein Kinase II

Nicotinic acetylcholine receptors regulate type 1 inositol 1,4,5-trisphosphate receptor expression via calmodulin kinase IV activation

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