Introduction of CACNA1D
CACNA1D, Calcium channel, voltage-dependent, L type, alpha 1D subunit (also known as Cav1.3) is a protein that in humans is encoded by the CACNA1D gene. Cav1.3 channel is a member of the Cav1 family, which form L-type calcium currents and is sensitive to selective inhibition by dihydropyridines (DHP). It mediates the entry of calcium ions into excitable cells and is also involved in a variety of calcium-dependent processes, including muscle contraction, neurotransmitter or hormone release, gene expression, cell division cell motility, and cell death.
|Basic Information of CACNA1D|
|Protein Name||Voltage-dependent L-type calcium channel subunit alpha-1D|
|Aliases||Calcium channel, L type, alpha-1 polypeptide, isoform 2, Voltage-gated calcium channel subunit alpha Cav1.3, CACH3, CACN4, CACNL1A2, CCHL1A2|
|Organism||Homo sapiens (Human)|
Function of CACNA1D Membrane Protein
CACNA1D is a member of voltage-sensitive calcium channels (VSCC) which mediates the entry of calcium ions into excitable cells and is also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division, and cell death. The isoform alpha-1D gives rise to L-type calcium currents. It has been identified that Long-lasting (L-type) calcium channels are members of the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
Fig.1 Cav1.3 isoform structure. (Zuccotti, 2011)
Application of CACNA1D Membrane Protein in Literature
This article found that mutations of CACNA1D ATP1A1 and caused a shift of voltage-dependent gating to more negative voltages, suppressed inactivation or increased currents. Identification of the distinct genotype and phenotype for this subset could facilitate diagnosis.
This article found that the mutation in CACNA1D caused a hyperpolarizing shift of the voltage-dependent inactivation and activation and slowed the channel's inactivation kinetics. ATP1A1 and CACNA1D mutant adenomas had a specific histopathologic phenotype.
This study provided an overview of clinical studies that had evaluated LTCC blockers for BD, SCZ, and drug dependence-associated symptoms, in addition, rodent studies that had identified Cav1.2 and Cav1.3 specific molecular and cellular cascades that underlie mood (anxiety, depression), social behavior, cognition, and addiction.
This article proved that CACNA1D could be as a new candidate autism risk gene and encouraged experimental therapy with available channel-blockers for this mutation. The additional presence of seizures and neurological abnormalities in our patient defined a novel phenotype partially overlapping with symptoms in two individuals with PASNA (congenital primary aldosteronism, seizures, and neurological abnormalities) caused by similar Cav1.3 gain-of-function mutations.
This article showed that this synaptic process involved long and short C-terminal isoforms of the Cav1.3 Ca2+ channel that differed in the kinetics of their Ca2+-dependent inactivation and their relative sensitivity to the L-type Ca2+ channel blocker nifedipine. The long isoforms, with slow inactivation and great sensitivity to nifedipine, mainly regulated the vesicular replenishment of the RRP; that was, the sustained or tonic exocytosis.
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