N-tip kalcijumski kanal

Kalcijumski kanal, od napona zavisna, N tip, alfa 1B podjedinica
Kalcijumski kanal, od napona zavisna, N tip, alfa 1B podjedinica
Identifikatori
Simboli	CACNA1B; CACNN; CACNL1A5; BIII
Vanjski ID	OMIM: 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
Vrsta	Čovek
Entrez	774
Ensembl	ENSG00000148408
UniProt	Q00975
RefSeq (mRNA)	NM_000718
RefSeq (protein)	NP_000709
Lokacija (UCSC)	Chr 9:; 139.89 - 140.14 Mb
PubMed pretraga	[1]

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 Cav_2.2^[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

^ ^а ^б Williams ME, Brust PF, Feldman DH, Patthi S, Simerson S, Maroufi A, McCue AF, Veliçelebi G, Ellis SB, Harpold MM (1992). „Structure and functional expression of an omega-conotoxin-sensitive human N-type calcium channel”. Science (journal). 257 (5068): 389—95. PMID 1321501. doi:10.1126/science.1321501.
^ „Entrez Gene: CACNA1B calcium channel, voltage-dependent, N type, alpha 1B subunit”.
^ Diriong S, Lory P, Williams ME, Ellis SB, Harpold MM, Taviaux S (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. PMID 8825650. doi:10.1006/geno.1995.1284.
^ 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. PMID 16382099. doi:10.1124/pr.57.4.5.
^ Kurihara T, Tanabe T (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. PMID 15166237. doi:10.1074/jbc.M310848200.
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. PMC 1302342  . PMID 12414690. doi:10.1016/S0006-3495(02)75267-3.
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. PMID 19065143. doi:10.1038/mp.2008.133.
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. PMC 1995641  . PMID 16857708. doi:10.1113/jphysiol.2006.115030.
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. PMID 16382099. doi:10.1124/pr.57.4.5.
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. PMID 15607937. doi:10.1016/j.mcn.2004.08.019.
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. PMID 12665800. doi:10.1038/nn1041.
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. PMID 17081983. doi:10.1016/j.cell.2006.09.026.
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. PMID 15728831. doi:10.1523/JNEUROSCI.4790-04.2005.
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. PMC 1817768  . PMID 16627564. doi:10.1113/jphysiol.2006.109744.
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. PMID 14602720. doi:10.1074/jbc.M308991200.
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. PMID 12435810. doi:10.1124/mol.62.6.1418.
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. PMC 139241  . PMID 12477932. doi:10.1073/pnas.242603899.
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. PMID 12161429. doi:10.1074/jbc.M203425200.
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. PMC 2570331  . PMID 18958281. doi:10.1371/journal.pone.0003560.
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. PMID 11438518. doi:10.1074/jbc.M100929200.
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. PMID 14684825. doi:10.1126/science.1090100.
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. PMID 15953418. doi:10.1016/j.neuron.2005.05.011.

Spoljašnje veze

CACNA1B+protein,+human на US National Library of Medicine Medical Subject Headings (MeSH)
N-Type+Calcium+Channel на US National Library of Medicine Medical Subject Headings (MeSH)

[pmid1321501-1] а ^б Williams ME, Brust PF, Feldman DH, Patthi S, Simerson S, Maroufi A, McCue AF, Veliçelebi G, Ellis SB, Harpold MM (1992). „Structure and functional expression of an omega-conotoxin-sensitive human N-type calcium channel”. Science (journal). 257 (5068): 389—95. PMID 1321501. doi:10.1126/science.1321501.

[entrez-2] „Entrez Gene: CACNA1B calcium channel, voltage-dependent, N type, alpha 1B subunit”.

[pmid8825650-3] Diriong S, Lory P, Williams ME, Ellis SB, Harpold MM, Taviaux S (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. PMID 8825650. doi:10.1006/geno.1995.1284.

[pmid16382099-4] 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. PMID 16382099. doi:10.1124/pr.57.4.5.

[pmid12777840-5] Kurihara T, Tanabe T (2003). „N-type Ca2+ channel”. Nippon Yakurigaku Zasshi. Folia Pharmacologica Japonica. 121 (4): 211—22. PMID 12777840.

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