Kalcijumski kanal N-tipa

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Kalcijumski kanal, od napona zavisna, N tip, alfa 1B podjedinica
Identifikatori
SimboliCACNA1B; CACNN; CACNL1A5; BIII
Vanjski IDOMIM: 601012 MGI: 88296 HomoloGene: 20184 IUPHAR: Cav2.2 GeneCards: CACNA1B Gene
Ontologija gena
Molekularna funkcija • aktivnost naponom-kontrolisanog jonskog kanala
• ATP vezivanje
• aktivnost naponom-kontrolisanog kalcijumskog kanala
• aktivnost jonskog kanala
• vezivanje protein C-terminusa
• proteinsko vezivanje
• vezivanje nukleotida
• vezivanje jona kalcijuma
• aktivnost naponom-kontrolisanog natrijumskog kanala
Celularna komponenta • membrana
• kompleks naponom-kontrolisanog natrijumskog kanala
• integralno sa membranom
• ćelijska membrana
• ćelijska soma
• kompleks naponom-kontrolisanog kalcijumskog kanala
Biološki proces • regulacija krvnog pritiska
• transport jona kalcijuma
• jonski transport
• lokomotorno ponašanje
• sekrecija neurotransmitera
• regulacija srčanih kontrakcija
• sinaptička transmisija
• transport jona natrijuma
Ortolozi
VrstaČovekMiš
Entrez77412287
EnsemblENSG00000148408ENSMUSG00000004113
UniProtQ00975O55017
RefSeq (mRNA)NM_000718NM_007579
RefSeq (protein)NP_000709NP_031605
Lokacija (UCSC)Chr 9:
139.89 - 140.14 Mb		Chr 2:
24.46 - 24.62 Mb
PubMed pretraga[1][2]

N-tip kalcijumski kanal je tip naponom-kontrolisanih kalcijumskih kanala. Poput drugih kanala ove klase, α1 podjedinica određuje većinu osobina kanala. α1 podjedinica je takođe poznata kao kalcijumski kanal, napon-zavisna, N tip, alfa 1B podjedinica (CACNA1B) ili Cav2.2[1] koju kod ljudi kodira gen CACNA1B.[2][3][4]

Strukture

Pored α1 podjedinice, sledeće podjedinice su prisutne u N-tipu kalcijumskog kanala:

  • α2δ – CACNA2D1, CACNA2D2
  • β1 – CACNB1
  • β3 – CACNB3
  • β4 – CACNB4

Funkcija

N-tip ('N' za „Nervni-Tip“ kalcijumskih kanala je nađen prvenstveno u presinaptičkim terminalima i učestvuje u otpuštanju neurotransmitera.[5] Jaka depolarizacija akcionim potencijalom uzrokuje otvaranje ovih kanala, čime se omogućava unos Ca2+, inicira fuzija vezikula i oslobađanje uskladištenog neurotransmitera. N-tip kanali mogu biti blokirani ω-konotoksinom.[1]

Reference

  1. ↑ 1,0 1,1 Williams ME, Brust PF, Feldman DH, Patthi S, Simerson S, Maroufi A, McCue AF, Veliçelebi G, Ellis SB, Harpold MM (July 1992). „Structure and functional expression of an omega-conotoxin-sensitive human N-type calcium channel”. Science (journal) 257 (5068): 389–95. DOI:10.1126/science.1321501. PMID 1321501. 
  2. ↑ „Entrez Gene: CACNA1B calcium channel, voltage-dependent, N type, alpha 1B subunit”. 
  3. ↑ Diriong S, Lory P, Williams ME, Ellis SB, Harpold MM, Taviaux S (December 1995). „Chromosomal localization of the human genes for alpha 1A, alpha 1B, and alpha 1E voltage-dependent Ca2+ channel subunits”. Genomics 30 (3): 605–9. DOI:10.1006/geno.1995.1284. PMID 8825650. 
  4. ↑ Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J (December 2005). „International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels”. Pharmacol. Rev. 57 (4): 411–25. DOI:10.1124/pr.57.4.5. PMID 16382099. 
  5. ↑ Kurihara T, Tanabe T (April 2003). „N-type Ca2+ channel”. Nippon Yakurigaku Zasshi. Folia Pharmacologica Japonica 121 (4): 211–22. PMID 12777840. 

Literatura

  • Mould J, Yasuda T, Schroeder CI, et al. (2004). „The alpha2delta auxiliary subunit reduces affinity of omega-conotoxins for recombinant N-type (Cav2.2) calcium channels.”. J. Biol. Chem. 279 (33): 34705–14. DOI:10.1074/jbc.M310848200. PMID 15166237. 
  • Park SY, Park YT, Kim KE, et al. (2002). „A direct repeat of N-type Ca2+ channel alpha1B gene functions as a negative regulatory element in HeLa cells.”. Mol. Cells 13 (2): 341–6. PMID 12018859. 
  • Calabrese B, Tabarean IV, Juranka P, Morris CE (2002). „Mechanosensitivity of N-type calcium channel currents.”. Biophys. J. 83 (5): 2560–74. DOI:10.1016/S0006-3495(02)75267-3. PMC 1302342. PMID 12414690. 
  • Moskvina V, Craddock N, Holmans P, et al. (2009). „Gene-wide analyses of genome-wide association data sets: evidence for multiple common risk alleles for schizophrenia and bipolar disorder and for overlap in genetic risk.”. Mol. Psychiatry 14 (3): 252–60. DOI:10.1038/mp.2008.133. PMID 19065143. 
  • Castiglioni AJ, Raingo J, Lipscombe D (2006). „Alternative splicing in the C-terminus of CaV2.2 controls expression and gating of N-type calcium channels.”. J. Physiol. (Lond.) 576 (Pt 1): 119–34. DOI:10.1113/jphysiol.2006.115030. PMC 1995641. PMID 16857708. 
  • Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J (2005). „International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels.”. Pharmacol. Rev. 57 (4): 411–25. DOI:10.1124/pr.57.4.5. PMID 16382099. 
  • Yokoyama CT, Myers SJ, Fu J, et al. (2005). „Mechanism of SNARE protein binding and regulation of Cav2 channels by phosphorylation of the synaptic protein interaction site.”. Mol. Cell. Neurosci. 28 (1): 1–17. DOI:10.1016/j.mcn.2004.08.019. PMID 15607937. 
  • Maeno-Hikichi Y, Chang S, Matsumura K, et al. (2003). „A PKC epsilon-ENH-channel complex specifically modulates N-type Ca2+ channels.”. Nat. Neurosci. 6 (5): 468–75. DOI:10.1038/nn1041. PMID 12665800. 
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). „Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”. Cell 127 (3): 635–48. DOI:10.1016/j.cell.2006.09.026. PMID 17081983. 
  • Li D, Wang F, Lai M, et al. (2005). „A protein phosphatase 2calpha-Ca2+ channel complex for dephosphorylation of neuronal Ca2+ channels phosphorylated by protein kinase C.”. J. Neurosci. 25 (8): 1914–23. DOI:10.1523/JNEUROSCI.4790-04.2005. PMID 15728831. 
  • Butcher AJ, Leroy J, Richards MW, et al. (2006). „The importance of occupancy rather than affinity of CaV(beta) subunits for the calcium channel I-II linker in relation to calcium channel function.”. J. Physiol. (Lond.) 574 (Pt 2): 387–98. DOI:10.1113/jphysiol.2006.109744. PMC 1817768. PMID 16627564. 
  • Stotz SC, Barr W, McRory JE, et al. (2004). „Several structural domains contribute to the regulation of N-type calcium channel inactivation by the beta 3 subunit.”. J. Biol. Chem. 279 (5): 3793–800. DOI:10.1074/jbc.M308991200. PMID 14602720. 
  • Maximov A, Bezprozvanny I (2002). „Synaptic targeting of N-type calcium channels in hippocampal neurons.”. J. Neurosci. 22 (16): 6939–52. PMID 12177192. 
  • Peng S, Hajela RK, Atchison WD (2002). „Characteristics of block by Pb2+ of function of human neuronal L-, N-, and R-type Ca2+ channels transiently expressed in human embryonic kidney 293 cells.”. Mol. Pharmacol. 62 (6): 1418–30. DOI:10.1124/mol.62.6.1418. PMID 12435810. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). „Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
  • Murakami M, Fleischmann B, De Felipe C, et al. (2002). „Pain perception in mice lacking the beta3 subunit of voltage-activated calcium channels.”. J. Biol. Chem. 277 (43): 40342–51. DOI:10.1074/jbc.M203425200. PMID 12161429. 
  • Vitko I, Shcheglovitov A, Baumgart JP, et al. (2008). „Orientation of the calcium channel beta relative to the alpha(1)2.2 subunit is critical for its regulation of channel activity.”. PLoS ONE 3 (10): e3560. DOI:10.1371/journal.pone.0003560. PMC 2570331. PMID 18958281. 
  • Coppola T, Magnin-Luthi S, Perret-Menoud V, et al. (2001). „Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin.”. J. Biol. Chem. 276 (35): 32756–62. DOI:10.1074/jbc.M100929200. PMID 11438518. 
  • Johnson JM, Castle J, Garrett-Engele P, et al. (2003). „Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays.”. Science 302 (5653): 2141–4. DOI:10.1126/science.1090100. PMID 14684825. 
  • Agler HL, Evans J, Tay LH, et al. (2005). „G protein-gated inhibitory module of N-type (ca(v)2.2) ca2+ channels.”. Neuron 46 (6): 891–904. DOI:10.1016/j.neuron.2005.05.011. PMID 15953418. 

Spoljašnje veze

  • MeSH CACNA1B+protein,+human
  • MeSH N-Type+Calcium+Channel
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Ca2+: Kalcijumski kanal
L-tip/Cavα (1.1, 1.2, 1.3, 1.4) • N-tip/Cavα2.2 • P-tip/Cavα(2.1) • Q-tip/Cavα2.1 • R-tip/Cavα2.3 • T-tip/Cavα(3.1, 3.2, 3.3)
α2δ-podjedinice (1, 2) • β-podjedinice (β1, β2, β3, β4) • γ-podjedinice (γ1, γ2, γ3, γ4)
[Katjonski kanali sperme]] (1, 2, 3, 4) •Dvoporni kanal (1, 2)
Ligand-kontrolisani
Inozitol trisfosfatni receptor (1, 2, 3) • Rianodinski receptor (1, 2, 3)
  • p
  • r
  • u
Na+: Natrijumski kanal
Naponom-kontrolisani
Navα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) • Navβ (1, 2, 3, 4)
Konstitutivno aktivni
Epitelni Natrijumski kanal (α, β, γ, δ)
  • p
  • r
  • u
K+: Kalijumski kanal
Naponom-kontrolisani
Kvα1-6 (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8) • (2.1, 2.2) • (3.1, 3.2, 3.3, 3.4) • (4.1, 4.2, 4.3) • (5.1) • (6.1, 6.2, 6.3, 6.4)
Kvα7-12 (7.1, 7.2, 7.3, 7.4, 7.5) • (8.1, 8.2) • (9.1, 9.2, 9.3) • (10.1, 10.2) • (11.1/hERG, 11.2, 11.3) • (12.1, 12.2, 12.3)
Kvβ (1, 2, 3) • KCNIP (1, 2, 3, 4) • minK/ISK • minK/ISK-sličan • MiRP (1, 2, 3) • Shaker gen
Kalcijumom-aktivirani
BK kanal (α1, β1, β2, β3, β4) • SK kanal (SK1, SK2, SK3, SK4) • KCa (1.1, 2.1, 2.2, 2.3, 3.1, 4.1, 4.2, 5.1)
Unutrašnje-ispravljajući
KATP • Kir (1.1, 2.1, 2.2, 2.3, 2.4, 2.6) • GIRK/Kir (3.1, 3.2, 3.3, 3.4) • Kir (4.1, 4.2, 5.1, 6.1, 6.2, 7.1)
Tandem pora domen
K2P (1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)
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  • r
  • u
Drugi
M+: TRP katjonski kanal
TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (1, 2, 3) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)
Cl-: Hloridni kanal
ANO1 • Bestrofin (1, 2) • CFTR • CLCA (1, 2, 3, 4) • CLCN (1, 2, 3, 4, 5, 6, 7, KA, KB) • CLIC (1, 2, 3, 4, 5, 6, L1) • CLNS (1A, 1B)
α (1, 2, 3, 4) • β (1, 2, 3) • HCN (1, 2, 3, 4)
Porin
Akvaporin (1, 2, 3, 4, 5, 7, 8, 9) • Napon-zavisni anjonski kanal (1, 2, 3) • Generalna bakterijska porinska familija
Propusna veza
Koneksin: A (GJA1, GJA3, GJA4, GJA5, GJA8, GJA9, GJA10) • B (GJB1, GJB2, GJB3, GJB4, GJB5, GJB6, GJB7) • C (GJC1, GJC2, GJC3) • D (GJD2, GJD3, GJD4) • E (GJE1)
Ineksin
Generalno
Ligandom-kontrolisani jonski kanal • Naponom-kontrolisani jonski kanal • Rastezanjem-aktivirani jonski kanal
vidi isto poremećaji
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr