CACNA1H Antibody

1. These findings reveal spectrin (alpha/beta) / ankyrin B cytoskeletal and signaling proteins as key regulators of T-type calcium channels expressed in the nervous system. PMID:29720258
2. In colonic biopsies, the Cav3.2 mRNA level was significantly higher in the irritable bowel syndrome group compared to controls. PMID:27196538
3. Here we show that T-type channels Cav3.1 and Cav3.2 are present in the lung and PASMCs from iPAH patients and control subjects. The blockade of T-type channels by the specific blocker, TTA-A2, prevents cell cycle progression and PASMCs growth PMID:28655554
4. Our data establish Stac1 as an important modulator of T-type channel expression and provide new insights into the molecular mechanisms underlying the trafficking of T-type channels to the plasma membrane. PMID:27149520
5. CACNA1H variant is associated with differential antiepileptic drug response in childhood absence epilepsy. PMID:28165634
6. There is a direct link between CACNA1H(M1549V) mutation and an increased aldosterone production. This suggests that calcium channel blockers may be beneficial in the treatment of a subset of patients with primary aldosteronism. PMID:27258646
7. CACNA1H might be a susceptibility gene predisposing to PA with different phenotypic presentations, opening new perspectives for genetic diagnosis and management of patients with PA. PMID:27729216
8. modulation of N-linked glycosylation of hCav3.2 channels may play an important physiological role PMID:26745591
9. heterozygous mutations identified in a pediatric patient with chronic pain and absence seizures result in loss of channel function, with significantly smaller current densities across a wide range of voltages when co-expressed in tsA-201 cells. PMID:26706850
10. Study revealed no association between the 15 tagSNPs of CACNA1A, 1C, and 1H and antiepileptic drug efficacy in the Chinese Han epileptic population; the TAGAA haplotype of CACNA1A may be a risk factor for drug resistance PMID:26216687
11. Cav3.2 channels are highly phosphorylated in the mammalian brain and establish phosphorylation as an important mechanism involved in the dynamic regulation of Cav3.2 channel gating properties PMID:26483470
12. Recurrent gain of function mutation in calcium channel CACNA1H causes early-onset hypertension with primary aldosteronism. PMID:25907736
13. reveal an unexpected role of CaV3.2 channels in regulating NMDA-R-mediated transmission and a novel epileptogenic mechanism for human childhood absence epilepsy PMID:26220996
14. The I-II loop of the Cav3.2 protein inhibits neuronal Cav3.1 and Cav3.2 channels. PMID:25931121
15. C456S mutation leads to substantially increased excitability of cultured neurons due to increased spontaneous firing rate. PMID:24277868
16. N-linked glycosylation of Cav3.2 not only controls surface expression. PMID:23503728
17. Data indicate that endogenous/exogenous hydrogen sulfide regulates function of T-type Ca(2+) channel Cav3.2 expressed in HEK293 cells PMID:24508802
18. It plays pivotal roles in processing of pain signals.(review) PMID:23903007
19. Both Asp residues critically control the biophysical properties of Ca(v)3.2, including relative permeability between Ba2+ and Ca2+, voltage dependency of channel activation, Cd2+ blocking sensitivity, and pH effects, in distinctive ways. PMID:23849427
20. Cav3.2 is differently expressed in normal pleura and malignant pleural mesothelioma PMID:22564432
21. Data suggest a pathway in which thioredoxin (Trx) acts as a tonic, endogenous regulator of Cav3.2 channels, while heme oxygenase-1 (HO-1)-derived carbon dioxide (CO) disrupts this regulation, causing channel inhibition. PMID:23671274
22. Results indicate that the S4-S5 and S6 helices from adjacent domains are energetically coupled during the activation of a low voltage-gated T-type CaV3.2 channel. PMID:23970551
23. A novel Cav3-KCa1.1 signaling complex has been identified where Cav3-mediated calcium entry enables KCa1.1 activation over a wide range of membrane potentials. PMID:23626738
24. Cav3.2 regulates calcineurin/NFAT pathway through both the Ca(2+) influx and calcineurin binding PMID:23669360
25. Our results support the notion that ion channel autoimmunity might at least partially contribute to HaNDL pathogenesis and occurrence of neurological symptoms. PMID:23111027
26. The abnormal mRNA expressions of T-type channel alpha1H and alpha1G may be one of the causes of declined semen quality and infertility in varicocele patients. PMID:22574369
27. ZnT-1 enhances the activity of CaV3.1 and CaV3.2 via activation of Ras-ERK signaling pathways in the plasma membrane. PMID:22572848
28. Cav3.2 channels were expressed at the membrane of large portions of cells, with no likely relation to Cav3.1 expression or apoptosis. PMID:22469755
29. A Ca(v)3.2/syntaxin-1A signaling complex controls T-type channel activity and low-threshold exocytosis. PMID:22130660
30. Data showed expression of L-type (Ca(v) 1.2), P/Q-type (Ca(v) 2.1), and T-type subtype (Ca(v) 3.1 and Ca(v) 3.2) voltage-gated calcium channels (Ca(v)s) in renal artery and dissected intrarenal blood vessels from nephrectomies. PMID:21788606
31. The function of T-type Ca(2+) channels is important for the proliferation of human ovarian cancer cells. PMID:21438841
32. Review: I-II loops of T-channels play critical roles in the trafficking and gating of these channels. This loop contains an intracellular gating brake that is essential to their ability open after small depolarizations of the membrane. PMID:21099341
33. Ca(V)3.2 alternative splicing generates significant T-type Ca channel structural and functional diversity with potential implications relevant to cardiac developmental and pathophysiological states PMID:20699644
34. Present evidence that N2O-based inhibition of Cav3.2 channels is mediated by free radical signalling and results in analgesia. PMID:21059758
35. functional modulation of the Ca(v)3.2 channels by Cav-3 is important for understanding the compartmentalized regulation of Ca(2+) signaling during normal and pathological processes. PMID:21084288
36. T-type calcium channel gene-CACNA1H might be a susceptibility gene to childhood absence epilepsy. PMID:15833171
37. Review discusses mutations of the Cav3.2 isoform (CACNA1H gene) that enhance channel activity and their association with idiopathic generalized epilepsies, whereas mutations that disrupt its activity are associated with autism spectrum disorders. PMID:19903827
38. We conclude that low voltage activated voltage-operated Ca(2+) channels are expressed in cells of the human male germ line. PMID:11751928
39. characterization in terms of activation and inactivation properties as well as cation permeability PMID:14529577
40. Ca(v)3.2 has a role in calcium influx during physiological activation and mutations may be causative in the propensity for seizures in patients with childhood absence epilepsy PMID:14729682
41. recombinant low voltage-activated T-type Ca channels exhibit a small, though clearly evident, window T-type Ca(2)(+) current which is also present in native channels from different neuronal types--REVIEW PMID:15498803
42. CACNA1H is a susceptibility gene in complex idiopathic generalized epilepsy PMID:15852375
43. Data indicate that Domain IV/S4 of Ca(v)3.2 is an activation domain and is not involved in inactivation from the open state. PMID:16133267
44. Cloning and calcium channel characteristics of Cav3.2 isoforms. PMID:16301824
45. His-191 in the S3-S4 loop is a critical residue conferring nickel block to Ca(v)3.2 PMID:16377633
46. inhibitory effects of amiodarone on the modified T-type Cav3.2 Ca2+ channel created by long-term amiodarone treatment PMID:16443692
47. The expression of CACNA1H in breast cancer has been confirmed by RT-PCR. PMID:16475676
48. Linkage analysis of 44 pedigrees provided no evidence for a locus in the CACNA1H region; no Chinese variants were found in 220 unrelated patients. PMID:16504478
49. CACNA1H RNA is alternatively spliced at 12-14 sites where it can destroy, create or change the regulatory specificity of predicted exonic splicing enhancer sequences that may control splicing regulation. PMID:16565161
50. functional analysis shows that missense mutations significantly reduce Ca(V)3.2 channel activity and thus could affect neuronal function and potentially brain development and could contribute to the development of the ASD phenotype PMID:16754686

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HGNC: 1395

UNIGENE: Hs.459642

KEGG: hsa:8912

STRING: 9606.ENSP00000334198

OMIM: 607904