Introduction of CACNA1E
CACNA1E, Calcium channel, voltage-dependent, R-type calcium channel subunit alpha-1E (also known as Cav2.3) is a protein that in humans is encoded by the CACNA1E gene. The α1 subunit forms the pore through which calcium enters the cell and determines most properties of the channel. It’s strongly expressed in cortex, hippocampus, striatum, amygdala and interpeduncular nucleus, and has a high threshold of activation and relatively slow kinetics.
|Basic Information of CACNA1E|
|Protein Name||Voltage-dependent R-type calcium channel subunit alpha-1E|
|Aliases||Brain calcium channel II, BII, Calcium channel, L type, alpha-1 polypeptide, isoform 6, Voltage-gated calcium channel subunit alpha Cav2.3, CACH6, CACNL1A6|
|Organism||Homo sapiens (Human)|
Function of CACNA1E Membrane Protein
CACNA1E is a voltage-dependent, R-type calcium channel subunit alpha-1E. Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, gene expression, hormone or neurotransmitter release, cell motility, as well as cell division and cell death. The isoform alpha-1E will cause R-type calcium currents. R-type calcium channels are members of the 'high-voltage activated' (HVA) group and are blocked by nickel, and partially blocked by omega-agatoxin-IIIA (omega-Aga-IIIA). CACNA1E is insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA), and omega-agatoxin-IVA (omega-Aga-IVA), as well as dihydropyridines (DHP). Calcium channels containing alpha-1E subunit also have been reported to be involved in the regulation of firing patterns of neurons which are necessary for information processing.
Fig.1 Transmembrane topology of the Cav2.3. (Parajuli, 2012)
Application of CACNA1E Membrane Protein in Literature
This article shows that Cav2.3 is a new mechanistic target for a key pronociceptive miRNA, miR-34c-5p, in the context of cancer pain and indicates an antinociceptive role for Cav2.3 in peripheral sensory neurons. The current study provides a good understanding of molecular mechanisms underlying cancer pain and suggests a potential novel therapeutic strategy targeting miR-34c-5p and Cav2.3 in cancer pain.
This article is to search for differences in the prevalence of a CACNA1E variant between a migraine without aura, various phenotypes of a migraine with aura, and healthy controls, and shows that the missense variant might modulate the function of R-type Ca2+ channels.
This study suggests that pain-related phenotypes after gastrointestinal surgery are enhanced in carriers of the minor G allele of the rs3845446 SNP, possibly through impairment of Cav2.3 VACC function that is responsible for the activation of visceral inflammatory pain stimulus-elicited antinociception.
This article indicates that SK2-containing channels are functionally coupled to NMDARs and KV4.2-containing channels to Cav2.3 channels to provide negative feedback regulation of EPSPs in the spines of CA1 pyramidal neurons.
This article indicates that Cav2.3 channel is critically involved in the Zn2+-mediated suppression of glucagon secretion during hyperglycemia. Especially under conditions of Zn2+ deficiency, ablation or dysfunction of Cav2.3 channels may lead to severe disturbances in glucose homeostasis.
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