Recombinant Human Voltage-dependent L-type calcium channel subunit alpha-1D (CACNA1D), partial

1. Although both otoferlin and synaptotagmin bind membrane fusion SNARE proteins, only otoferlin interacts with the L-type calcium channel Cav1.3. PMID: 28696301
2. Study have showned a significant effect of the autism-associated mutation A760G on the gating of CaV1.3 such that channel activation is significantly left-shifted, Ca(2+)-dependent inactivation is decreased, and deactivation is slowed, resulting in excess Ca2+ entry. However, these effects are mitigated by an increase in voltage-dependent inactivation. Also, A760G mutation differentially affects CaV1.3 splice variants. PMID: 27255217
3. Data suggest that p.G403D mutation in CACNA1D causes persistent hyperinsulinaemic hypoglycaemia with heart defects (presenting as aortic valve insufficiency) and severe neuromuscular disease (presenting as hypotonia); this study involves DNA mutational analysis in one patient plus 2 unrelated patients. [CASE REPORT] PMID: 28318089
4. These results provide the evidence of a direct regulatory role of Snapin on Cav1.3 channels in atrial myocytes. PMID: 27915047
5. Study used structure modeling and MD simulations to predict omega-currents in CaV1.1 and CaV1.3 channel VSDs when one of the first three S4 gating charges harbors a disease-causing mutation. Using site-directed mutagenesis and electrophysiology, experimentally confirmed that the mutation of R3 charge to His in VSD III of CaV1.3 channels results in an omega-current at hyperpolarizing potentials. PMID: 28978442
6. CACNA1D mutations predominate in small zona glomerulosa (ZG)-like Aldosterone-producing Adenomas. PMID: 28584012
7. The CACNA1C-L762F mutation is associated with development of long QT syndrome through slower channel inactivation and increased sustained and window current. Timothy syndrome -associated mutations localize to specific areas of CACNA1C and are associated with a younger age at presentation, higher QTc, and 2:1 AV block than isolated LQTS-associated mutations. PMID: 27390944
8. Mutations in CACNA1D cause the excessive autonomous aldosterone secretion of Aldosterone-producing Adenomas. PMID: 28584016
9. While the relative contribution of Cav1.3 to intestinal Ca(2+) absorption and its value as a therapeutic target remain to be established, we postulate that Cav1.3 downregulation in IBD may contribute to the negative systemic Ca(2+) balance, to increased bone resorption, and to reduced bone mineral density in IBD patients. PMID: 27932504
10. E2 upregulated the expression of Cav1.3 for Ca2+ influx to promote the expression of p-ERK1/2 for cell proliferation in breast cancer cells PMID: 27572936
11. LRP1B, BRD2 and CACNA1D are new candidate genes in fetal metabolic programming of newborns exposed to maternal hyperglycemia. PMID: 26586120
12. CACNA1D might not be a risk gene for SCZ in Han Chinese population, which add to the current state of knowledge regarding the susceptibility of CACNA1D to schizophrenia. PMID: 26255836
13. patients with CACNA1D mutations displayed characteristics similar to wild-type aldosterone-producing adenomas PMID: 26606680
14. Studies indicate the function of L-type calcium channels Cav1.3 in chromaffin cells. PMID: 25966692
15. Studies indicate a role for L-type calcium channel Cav1.3 and Cav1.4 in cochlear inner hair cells (IHCs) and retinal photoreceptors (PRs). PMID: 25966695
16. Mutations in CACNA1D gene is associated with aldosterone-producing adenomas. PMID: 26285814
17. Study found that two de novo CACNA1D missense mutations affect evolutionary highly conserved regions in the channel's activation gate and disrupt normal channel activity by inducing a pronounced gain of channel function PMID: 25620733
18. Cav1.3 was overexpressed in atypical hyperplasia and endometrial carcinoma, and the estrogen-induced phosphorylation of downstream molecular ERK1/2 and CREB is the result of activation of the GPER pathway. PMID: 25805831
19. A meta-analysis of genome-wide association studies of blood pressure and hypertension in Chinese identified three new loci (CACNA1D, CYP21A2, and MED13L) and a newly discovered variant near SLC4A7. PMID: 25249183
20. ablation of Cav1.3 results in a decrease in the protein expression of myosin light chain 2, which interacts and increases the membrane localization of SK2 channels. PMID: 25538241
21. CACNA1D gene overexpression is associated with prostate cancer progression and might play an important role in Ca(2+) influx, AR activation, and cell growth in prostate cancer cells PMID: 24054868
22. RNA editing of CaV1.3 channels(CDI) acts to modulate CDI in ways that substantiate a recently emerging mechanism where apoCaM begins preassociated with the IQ domain and other channel elements. PMID: 24120865
23. in patients with aldosterone-producing adenomas, CACNA1D mutations were associated with smaller adenomas. PMID: 24866132
24. Results illustrate that the voltage sensors of Cav1.3 channels respond more sensitively to depolarization than those of Cav1.2 or Cav3.1 PMID: 24703308
25. The calcium inflow through Cav1.2 and Cav1.3 channels in murine spiral ganglion neurons. PMID: 24849370
26. These findings implicate gain-of-function CACNA1D Ca(2+) channel mutations in adrenal aldosterone-producing adenomas and primary aldosteronism. PMID: 23913001
27. A novel mechanism for modulation of the pharmacologic properties of the CaV1.3 channel is identified through posttranscriptional modification of the C terminus. PMID: 23924992
28. N-lobe of Ca(2+)-calmodulin binds an N-terminal spatial Ca(2+) transforming element module on the channel amino terminus, whereas the C-lobe binds an EF-hand region upstream of the IQ domain PMID: 23591884
29. modulation of Cav1.3 Ca channel by calreticulin may be involved in pathological settings such as autoimmune associated congenital heart block where Cav1.3 Ca channels are downregulated PMID: 23791743
30. conclude that the L-type calcium channel Cav1.3 is important in human glucose-induced insulin secretion, and common variants in CACNA1D might contribute to type 2 diabetes. PMID: 23229155
31. analysis of functional characterization of alternative splicing in the C terminus of L-type CaV1.3 channels PMID: 21998309
32. Functional properties of a newly identified C-terminal splice variant of Cav1.3 L-type Ca2+ channels PMID: 21998310
33. A novel pathway for ankyrin-B-dependent regulation of Cav1.3 channel membrane targeting and regulation is found in atrial myocytes. PMID: 21859974
34. CaV1.3 channels and intracellular calcium mediate osmotic stress-induced N-terminal c-Jun kinase activation and disruption of tight junctions in Caco-2 CELL MONOLAYERS. PMID: 21737448
35. We describe a human channelopathy (termed SANDD syndrome, sinoatrial node dysfunction and deafness) with a cardiac and auditory phenotype that closely resembles that of Cacna1d-/- mice. PMID: 21131953
36. These data suggest that RIM2beta contributes to the stabilization of Ca(v)1.3 gating kinetics in immature cochlear inner hair cells. PMID: 20363327
37. Ca(v)1.3 was the sole apical channel responsible for the PRL-stimulated transcellular calcium transport in intestine-like Caco-2 monolayer. PMID: 19885716
38. demonstrate (1) expression of the alpha1D Ca channel in human fetal heart, (2) inhibition of alpha1D I(Ca-L) by positive IgG, and (3) direct cross-reactivity of positive IgG with the alpha1D Ca channel protein PMID: 15939813
39. The modulation of alpha(1D) Ca(2+) channel by PKC was prevented by dialyzing cells with a 35-amino acid peptide mimicking the alpha(1D) NH(2)-terminal region comprising S81. PMID: 16973824
40. analysis of Ca2+-dependent gating of CaV1.3 L-type calcium channels by alternative splicing of a C-terminal regulatory domain PMID: 18482979
41. Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1.3. PMID: 19004828
42. Enhancement of calcium transport in Caco-2 monolayer through PKCzeta-dependent Cav1.3-mediated transcellular and rectifying paracellular pathways by prolactin. PMID: 19339512
43. Overexpression of the intracellular II-III loop domains of Cav1.2, and possibly Cav1.3, can dislodge the corresponding endogenous channels from the lipid raft regions of the membrane in rat insulinoma (INS-1) cells. PMID: 19351867

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HGNC: 1391

OMIM: 114206

KEGG: hsa:776

STRING: 9606.ENSP00000288139

UniGene: Hs.476358