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CACNA1A activates calcium(2+). 40 / 40
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"It has been recently reported that BHQ in vitro inhibits Ca V 2.1 voltage-dependent activation, thereby ameliorating gating defects and synaptic transmission due to S218L mutation xref ."
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"As LRRK1 did not significantly alter Ca V 2.1 current density, we hypothesized that LRRK1 would not have any effect on Ca V 2.1 voltage-dependent activation."
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"The CACNA1A gain-of-function (GOF) mutations could enhance the neuronal excitability by increasing the influx of calcium ions and release of glutamate, decreasing the threshold of CSD, resulting in the occurrence of HM and epilepsy."
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"Together, this pattern of severely altered neuronal responses to physiological stimuli suggests that HPCA deficiency might inhibit voltage-dependent Ca channels or, alternatively, modify the mechanism of maintaining the membrane potential and thus affect cellular response to membrane depolarization.In summary, we have presented evidence to support biallelic mutations in HPCA as a cause of AR primary isolated dystonia."
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"The present study indicates that the mechanism of neurodegeneration in SCA6 is associated with cytoplasmic aggregations of the [alpha] 1A calcium channel protein caused by a small CAG repeat and polyglutamine expansion in CACNA1A."
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"Cerebellar Purkinje cells of du mice had 35% smaller whole-cell Ca currents mediated by P-type (Cav2.1) VGCC calcium channels and abnormal morphology of their dendritic trees [71]."
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"Flame shifts or stop codon insertions in episodic ataxia type 2 (EA2) human patients and a splice site mutation in the leaner mouse lead the production of incomplete Ca v 2.1 molecules [8,9] ."
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"Phosphorylation of S1198 (human α 1 3.2) negatively shifts voltage-dependent activation of Ca v 3.2 channels in HEK293 cells."
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"It can be stated that the mechanism of neurodegeneration in SCA6 is associated with cytoplasmic aggregations of the alpha-1A calcium channel protein caused by a small CAG repeat and polyglutamine expansion in CACNA1A."
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"The accessory α 2 δ-1 subunit is known to facilitate Ca V 1.2 voltage-dependent activation, but the underlying mechanism is unknown."
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"We found that CaMKII had no effect on voltage-dependent activation of Ca v 1.3 Ba 2+ currents (I Ba )."
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"While densin+CaMKII did not affect voltage-dependent activation or facilitation of Ca v 1.3 (data not shown), they significantly increased the amplitude of Ca v 1.3 Ca 2+ currents (I Ca ) during trains of depolarizations (100 Hz, xref )."
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"CACNA1A was identified as the genetic cause in 1996, and causes a calcium channelopathy [28]."
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"The depolarization also activates voltage-gated calcium channels, primarily Cav2.1 and Cav3.1, allowing calcium into Purkinje neurons."
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"Abnormal apoptotic T cells from lupus showed persistently elevated mitochondrial membrane potential and mitochondrial hyperpolarisation (MHP), depletion of ATP and glutathione, increased Ca influx and mitochondrial dysfunction, exerting a crucial role in the pathogenesis of SLE."
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"P/Q-type (from Purkinje/Cerebellar) or Cav2.1 mediate P/Q-type Ca currents and are included in the Cav2 family of the VGCCs [36]."
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"Cacna1a [210] encodes the Ca channel and its mutations cause Ca channel inactivation."
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"Two different targeted Cacna1a disruptions that completely abolish Ca V 2.1 activity result in a severe motor disorder that is reminiscent of generalized dystonia in humans [XREF_BIBR, XREF_BIBR]."
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"The a, subunit (a, p) directs the recombinant expression of a dihydropyridine sensitive L-type Ca 2+ channel when coexpressed with the P ([32) and the a2 (a2n) subunits in Xenopus oocytes."
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"The voltage-dependent activation of Ca(v)1.2 (alpha(1C)) versus Ca(v)1.3 Ca(2+) channel subunits was directly compared by using a heterologous expression system without beta coexpression."
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"Expression of the a1D subunit alone, or coexpression with the a26 subunit, did not elicit functional Ca 2+ channel activity."
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"In contrast, a third a, subunit gene, expressed in rabbit brain, directs the synthesis of Ca 2+ channels that are insensitive to both DHPs and w-conotoxin GVIA ((o-CgTx) when coexpressed with the rabb[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The CACNA1A (Cav2.1), coding the alpha 1A subunit protein, which mediates the entry of calcium ions into excitable cells."
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"These results demonstrate that BHQ inhibits voltage-dependent activation of Ca v 2.1 and has distinct actions on I Ba and I Ca ."
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"Discussion Distinct Neuronal Call Channel Subunits Comprise a Novel DHP Sensitive Subtype Our results demonstrate that the a, p subunit mediates DHP- sensitive, high voltage activated, long lasting Ca[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The ability of the ApCa 2a1 Y-F short isoform to reduce heterosynaptic inhibition of the whole calcium current, but not the synaptic calcium current to a similar extant, indicates that the short isoform is unable to substitute or replace the endogenous, wildtype channels which presumably remain at the synapses and are subject to heterosynaptic inhibition."
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"We conclude that BHQ stabilizes the opening and weakens voltage-dependent activation of Ca v 2.1, which causes slower tail currents and a reduction in the steady- state current, respectively."
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"Familial hemiplegic migraine type 1 (FHM1) is caused by mutations in the CACNA1A gene, encoding neuronal presynaptic Ca (V) 2.1 (P/Q-type) Ca (2+) channels."
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"The S218L mutation enhances voltage-dependent activation of Ca v 2.1, which augments excitatory transmission in S218L knock-in mice ( xref ; xref ; xref )."
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"FHM Type 1, which accounts for around 50% of all FHM cases, is caused by mutations in the CACNA1A gene encoding the Ca v 2.1 P/Q voltage dependent calcium channel."
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"Also of note, mild depolarization of the sperm membrane by addition of high K + (60mM) failed to stimulate Ca 2+ transients ( xref ), further suggesting that in sperm, Ca V 2.3 voltage dependent activation is strongly modulated by its lipid environment."
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"FHM Type 1, which accounts for around 50% of all FHM cases, is caused by mutations in the CACNA1A gene encoding the Ca v 2.1 P/Q voltage dependent calcium channel."
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"Comparative analysis of functional presynaptic calcium currents and freeze-fractured immunogold labeling of CaV2.1 α subunits demonstrated that CaV2.1 α subunit overexpression could increase synaptic calcium current, CaV2.1 channel number, and thus synaptic strength at both developing and mature synapses, arguing against a CaV2 channel slot preference and saturation hypothesis (Lubbert et al., 2019)."
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"Thus, 2,50-di(tertbutyl)-1,4,-benzohydroquinone (BHQ), a synthetic phenolic compound that inhibits sarcoendoplasmic Ca 2+ ATPases (SERCAs) and with pro-oxidant properties, can also inhibit Ca V 2.1 voltage-dependent activation to ameliorate gating defects in the channel and subsequently prevent synaptic transmission problems produced by the S218L CACNA1A mutation causing a severe form of FHM with slowly progressive cerebellar ataxia and atrophy in humans [ xref ]."
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"Interestingly, dysfunction of Ca 2.1 caused by mutations in CACNA1A has been identified in Familial hemiplegic migraine 1 (FHM1; Ophoff et al., 1996), where altered channel kinetics were identified as a pathomechanism (Kraus et al., 1998, 2000)."
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"XREF_BIBR XREF_BIBR - XREF_BIBR A mutation in the CACNA1A gene, causing calcium channelopathy, has been reported in some patients with PTU."
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"Our ApCa 2a1 short isoform retains a significant portion of the early C-terminus which includes the EF-hand and the pre-IQ domain, and when expressed contributes to the calcium current suggesting surface expression of a functional calcium channel."
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"The higher synaptic depolarization in sector II than in sector I resulted in a stronger voltage-dependent activation of Ca channels in the former than in the latter (Figure xref )."
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"Their study about the functional consequences of ΔF1502 on Ca V 2.1 channel function in Xenopus oocytes using Ba 2+ as the charge carrier (instead of the physiological permeant ion Ca 2+ ), revealed: 1) an ~ 11 mV hyperpolarizing shift in Ca V 2.1 voltage-dependent activation, 2) a 30% decrease in Ba 2+ current density at high depolarizing voltages, 3) a shift in the voltage dependence of steady-state inactivation to hyperpolarizing voltages by ~ 14 mV, and 4) a slightly slower recovery from channel inactivation."
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"To directly verify that the documented hyperpolarizing shift in the steady-state voltage-dependent activation of Ca v 1.3 compared to Ca v 1.2 L-type Ca 2+ channel contributes importantly to the observed decrease in the AV node firing frequency in the null mutant mice, we generated computer modeling to directly assess the effect of Ca v 1.2 and Ca v 1.3 currents on the properties and characteristics of spontaneous APs of mouse AV node cells."
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