Expression of the neuronal calcium sensor protein family in the rat brain

Paterlini, Marta; Revilla, Victoria Cuartero; Grant, A.L.; Wisden, William

doi:10.1016/s0306-4522(00)00201-3

Cited by 110 publications

(85 citation statements)

References 50 publications

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“…Colocalization of VILIP-2 and Ca V 2.1 channels in the brain VILIP-2 is expressed in the neocortex, caudate-putamen, and hippocampus, including both pyramidal neurons and dentate granule cells, and in the Purkinje neurons of the cerebellum (Paterlini et al, 2000). Ca V 2.1, ␤ 2a , and ␤ 1b are also expressed in these regions (Stea et al, 1994;Tanaka et al, 1995;Westenbroek et al, 1995;Sakurai et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

Modulation of Ca_V2.1 Channels by the Neuronal Calcium-Binding Protein Visinin-Like Protein-2

Lautermilch¹,

Few²,

Scheuer³

et al. 2005

J. Neurosci.

102

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CaV2.1 channels conduct P/Q-type Ca2+currents that are modulated by calmodulin (CaM) and the structurally related Ca2+-binding protein 1 (CaBP1). Visinin-like protein-2 (VILIP-2) is a CaM-related Ca2+-binding protein expressed in the neocortex and hippocampus. Coexpression of CaV2.1 and VILIP-2 in tsA-201 cells resulted in Ca2+channel modulation distinct from CaM and CaBP1. CaV2.1 channels with β2asubunits undergo Ca2+-dependent facilitation and inactivation attributable to association of endogenous Ca2+/CaM. VILIP-2 coexpression does not alter facilitation measured in paired-pulse experiments but slows the rate of inactivation to that seen without Ca2+/CaM binding and reduces inactivation of Ca2+currents during trains of repetitive depolarizations. CaV2.1 channels with β1bsubunits have rapid voltage-dependent inactivation, and VILIP-2 has no effect on the rate of inactivation or facilitation of the Ca2+current. In contrast, when Ba2+replaces Ca2+as the charge carrier, VILIP-2 slows inactivation. The effects of VILIP-2 are prevented by deletion of the CaM-binding domain (CBD) in the C terminus of CaV2.1 channels. However, both the CBD and an upstream IQ-like domain must be deleted to prevent VILIP-2 binding. Our results indicate that VILIP-2 binds to the CBD and IQ-like domains of CaV2.1 channels like CaM but slows inactivation, which enhances facilitation of CaV2.1 channels during extended trains of stimuli. Comparison of VILIP-2 effects with those of CaBP1 indicates striking differences in modulation of both facilitation and inactivation. Differential regulation of CaV2.1 channels by CaM, VILIP-2, CaBP1, and other neurospecific Ca2+-binding proteins is a potentially important determinant of Ca2+entry in neurotransmission.

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Section: Discussionmentioning

confidence: 99%

Modulation of Ca_V2.1 Channels by the Neuronal Calcium-Binding Protein Visinin-Like Protein-2

Lautermilch¹,

Few²,

Scheuer³

et al. 2005

J. Neurosci.

102

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“…Recent studies have extended the area of expression of NCS-1 from the nervous system to neuroendocrine cells and even cardiac myocytes (21,26,33). In these cell types, NCS-1 modulates synaptic transmission (14,22,34), secretion (21,25), or cellular excitability (18,20) via complex processes that include regulation of key enzymes for membrane transport (15,17,23,24,35) and specific regulation of various ion channels (16, 18 -20, 28).…”

Section: Discussionmentioning

confidence: 99%

Down-regulation of Voltage-gated Ca2+ Channels by Neuronal Calcium Sensor-1 Is β Subunit-specific

Rousset¹,

Cens²,

Gavarini³

et al. 2003

Journal of Biological Chemistry

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Neuronal Ca 2؉ sensor protein-1 (NCS-1) is a member of the Ca 2؉ binding protein family, with three functional Ca 2؉ binding EF-hands and an N-terminal myristoylation site. NCS-1 is expressed in brain and heart during embryonic and postnatal development. In neurons, NCS-1 facilitates neurotransmitter release, but both inhibition and facilitation of the Ca 2؉ current amplitude have been reported. In heart, NCS-1 co-immunoprecipitates with K ؉ channels and modulates their activity, but the potential effects of NCS-1 on cardiac Ca 2؉ channels have not been investigated. To directly assess the effect of NCS-1 on the various types of Ca 2؉ channels we have co-expressed NCS-1 in Xenopus oocytes, with Ca V 1.2, Ca V 2.1, and Ca V 2.2 Ca 2؉ channels, using various subunit combinations. The major effect of NCS-1 was to decrease Ca 2؉ current amplitude, recorded with the three different types of ␣ 1 subunit. When expressed with Ca V 2.1, the depression of Ca 2؉ current amplitude induced by NCS-1 was dependent upon the identity of the ␤ subunit expressed, with no block recorded without ␤ subunit or with the ␤ 3 subunit. Current-voltage and inactivation curves were also slightly modified and displayed a different specificity toward the ␤ subunits. Taken together, these data suggest that NCS-1 is able to modulate cardiac and neuronal voltage-gated Ca 2؉ channels in a ␤ subunit specific manner.

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“…NCALD, also known as VSNL3, is a high-affinity Ca 2 þ sensor that has been found to interact with cytoskeletal proteins (Paterlini et al, 2000). In SCZ, evidence for brain mitochondrial dysfunction has been reported, including findings of impaired brain energy metabolism, developmental deviations, abnormal neurotransmission, and connectivity (Manji et al, 2012;Rosenfeld et al, 2011), along with mitochondrial hypoplasia, oxidative phosphorylation system imbalance, and altered mitochondrial protein expression (Karry et al, 2004;Prabakaran et al, 2004).…”

Section: Biological Functions P-values Proteins Biological Functions mentioning

confidence: 99%

A Combined Metabonomic and Proteomic Approach Identifies Frontal Cortex Changes in a Chronic Phencyclidine Rat Model in Relation to Human Schizophrenia Brain Pathology

Wesseling

Chan

Tsang

et al. 2013

Neuropsychopharmacol

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Current schizophrenia (SCZ) treatments fail to treat the broad range of manifestations associated with this devastating disorder. Thus, new translational models that reproduce the core pathological features are urgently needed to facilitate novel drug discovery efforts. Here, we report findings from the first comprehensive label-free liquid-mass spectrometry proteomic-and proton nuclear magnetic resonance-based metabonomic profiling of the rat frontal cortex after chronic phencyclidine (PCP) intervention, which induces SCZ-like symptoms. The findings were compared with results from a proteomic profiling of post-mortem prefrontal cortex from SCZ patients and with relevant findings in the literature. Through this approach, we identified proteomic alterations in glutamate-mediated Ca 2 þ signaling (Ca 2 þ /calmodulin-dependent protein kinase II, PPP3CA, and VISL1), mitochondrial function (GOT2 and PKLR), and cytoskeletal remodeling (ARP3). Metabonomic profiling revealed changes in the levels of glutamate, glutamine, glycine, pyruvate, and the Ca 2 þ regulator taurine. Effects on similar pathways were also identified in the prefrontal cortex tissue from human SCZ subjects. The discovery of similar but not identical proteomic and metabonomic alterations in the chronic PCP rat model and human brain indicates that this model recapitulates only some of the molecular alterations of the disease. This knowledge may be helpful in understanding mechanisms underlying psychosis, which, in turn, can facilitate improved therapy and drug discovery for SCZ and other psychiatric diseases. Most importantly, these molecular findings suggest that the combined use of multiple models may be required for more effective translation to studies of human SCZ.

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Expression of the neuronal calcium sensor protein family in the rat brain

Cited by 110 publications

References 50 publications

Modulation of Ca_V2.1 Channels by the Neuronal Calcium-Binding Protein Visinin-Like Protein-2

Modulation of Ca_V2.1 Channels by the Neuronal Calcium-Binding Protein Visinin-Like Protein-2

Down-regulation of Voltage-gated Ca2+ Channels by Neuronal Calcium Sensor-1 Is β Subunit-specific

A Combined Metabonomic and Proteomic Approach Identifies Frontal Cortex Changes in a Chronic Phencyclidine Rat Model in Relation to Human Schizophrenia Brain Pathology

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Expression of the neuronal calcium sensor protein family in the rat brain

Cited by 110 publications

References 50 publications

Modulation of CaV2.1 Channels by the Neuronal Calcium-Binding Protein Visinin-Like Protein-2

Modulation of CaV2.1 Channels by the Neuronal Calcium-Binding Protein Visinin-Like Protein-2

Down-regulation of Voltage-gated Ca2+ Channels by Neuronal Calcium Sensor-1 Is β Subunit-specific

A Combined Metabonomic and Proteomic Approach Identifies Frontal Cortex Changes in a Chronic Phencyclidine Rat Model in Relation to Human Schizophrenia Brain Pathology

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Modulation of Ca_V2.1 Channels by the Neuronal Calcium-Binding Protein Visinin-Like Protein-2

Modulation of Ca_V2.1 Channels by the Neuronal Calcium-Binding Protein Visinin-Like Protein-2