CaV2.2 | voltage-dependent, N type, alpha 1B subunit calcium channel
L-Type (CaV1.1–CaV1.4), P/Q-Type (CaV2.1), N-Type (CaV2.2), R-Type (CaV2.3), T-Type (CaV3.1–CaV3.3)
Six transmembrane alpha helices (S1–S6), total of four homologous domains make up the tetrameric alpha subunit structure
One large alpha subunit forms a functional channel, accessory subunits ( α1, α2δ, β1-4, and γ) are crucial for robust expression, they functionally modulate the alpha subunit
CaV2.2 Background Information
CaV2.2 give rise to the N-type calcium currents and is distributed thourghout the entire body. These channels are known for their importance in the nervous system. They play a small role in the migration of immature neurons before the establishment of their mature synapses, and they are critically involved in the release of neurotransmitters, which is also similar to another type of calcium channels, known as P-type calcium channels. N-type calcium channels are targets for the development of drugs to relieve chronic and neuropathic pain. They are also used for the treatment of hypertension, Autism Spectrum Disorder, Osteoarthritis, and other medical diagnoses. Additionally, N-type calcium channels have known functions in the kidney, and heart.
brain, heart, lung, kidney
Neurotransmitter release in neurons, neurite outgrowth
Chronic pain, osteoarthritis, congenital generalized lipodystrophy, mental retardation, hypertension, diabetic neuropathy, Myoclonus-Dystonia syndrome, cancer, autism spectrum disorder
β1, β3, β4, α2δ, and possibly γ, laminin, ATP, RIMS1, FMR1, Amyloid Beta Precursor Protein Binding Family A Member 1, CaV2.1, CaV1.3, CaV3.1, CaV2.3, calmodulin, Guanine nucleotide binding protein gamma 4 and gamma 12
ω-Conotoxins, cadmium, gabapentin, nicardipine, TROX-1, ziconitide, (+-) Bay K 8644, cadmium
Patch Clamp: whole cell, room temperature
CaV channels often show a rundown phenomenon. Adequate intra- and extracellular solutions are essential for a good data quality.
Reviews and Links
- Catterall et al. (2005) International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels. Pharmacol Rev. 57 (4): 411–25.