메뉴 건너뛰기




Volumn 5 FEB, Issue , 2014, Pages

Connexin and Pannexin hemichannels are regulated by redox potential

Author keywords

Carbon monoxide; Connexin; Nitric oxide; Redox signaling; S Nitrosylation

Indexed keywords

CONNEXIN 43; GAP JUNCTION PROTEIN; MEMBRANE PROTEIN; NITRIC OXIDE; PANNEXIN; UNCLASSIFIED DRUG;

EID: 84895506082     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00080     Document Type: Review
Times cited : (63)

References (101)
  • 1
    • 77955293473 scopus 로고    scopus 로고
    • Pannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other
    • doi: 10.1074/jbc.M110.115444
    • Ambrosi, C., Gassmann, O., Pranskevich, J. N., Boassa, D., Smock, A., Wang, J., et al. (2010). Pannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other. J. Biol. Chem. 285, 24420-24431. doi: 10.1074/jbc.M110.115444.
    • (2010) J. Biol. Chem. , vol.285 , pp. 24420-24431
    • Ambrosi, C.1    Gassmann, O.2    Pranskevich, J.N.3    Boassa, D.4    Smock, A.5    Wang, J.6
  • 2
    • 84862556342 scopus 로고    scopus 로고
    • Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease
    • doi: 10.1007/s00109-012-0878-z
    • Anand, P., and Stamler, J. S. (2012). Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease. J. Mol. Med. (Berl). 90, 233-244. doi: 10.1007/s00109-012-0878-z.
    • (2012) J. Mol. Med. (Berl). , vol.90 , pp. 233-244
    • Anand, P.1    Stamler, J.S.2
  • 3
    • 33846003833 scopus 로고    scopus 로고
    • Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides inryanodine receptor type 1
    • doi: 10.1074/jbc.M600876200
    • Aracena-Parks, P., Goonasekera, S. A., Gilman, C. P., Dirksen, R. T., Hidalgo, C., and Hamilton, S. L. (2006). Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides inryanodine receptor type 1. J. Biol. Chem. 281, 40354-40368. doi: 10.1074/jbc.M600876200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 40354-40368
    • Aracena-Parks, P.1    Goonasekera, S.A.2    Gilman, C.P.3    Dirksen, R.T.4    Hidalgo, C.5    Hamilton, S.L.6
  • 4
    • 79958798010 scopus 로고    scopus 로고
    • A potential therapeutic role for P2X7 receptor (P2X7R) antagonists in the treatment of inflammatory diseases
    • doi: 10.1517/13543784.2011.578068
    • Arulkumaran, N., Unwin, R. J., and Tam, F. W. (2011). A potential therapeutic role for P2X7 receptor (P2X7R) antagonists in the treatment of inflammatory diseases. Expert Opin. Investig. Drugs 20, 897-915. doi: 10.1517/13543784.2011.578068.
    • (2011) Expert Opin. Investig. Drugs , vol.20 , pp. 897-915
    • Arulkumaran, N.1    Unwin, R.J.2    Tam, F.W.3
  • 5
    • 84866740851 scopus 로고    scopus 로고
    • Regulation of Cx45 hemichannels mediated by extracellular and intracellular calcium
    • doi: 10.1007/s00424-012-1133-8
    • Bader, P., Weingart, R., and Egger, M. (2012). Regulation of Cx45 hemichannels mediated by extracellular and intracellular calcium. Pflugers Arch. 464, 249-259. doi: 10.1007/s00424-012-1133-8.
    • (2012) Pflugers Arch. , vol.464 , pp. 249-259
    • Bader, P.1    Weingart, R.2    Egger, M.3
  • 6
    • 4143127920 scopus 로고    scopus 로고
    • Pannexin membrane channels are mechanosensitive conduits for ATP
    • doi: 10.1016/j.febslet.2004.07.009
    • Bao, L., Locovei, S., and Dahl, G. (2004). Pannexin membrane channels are mechanosensitive conduits for ATP. FEBS Lett. 572, 65-68. doi: 10.1016/j.febslet.2004.07.009.
    • (2004) FEBS Lett. , vol.572 , pp. 65-68
    • Bao, L.1    Locovei, S.2    Dahl, G.3
  • 7
    • 34247644332 scopus 로고    scopus 로고
    • Change in permeant size selectivity by phosphorylation of connexin 43 gap-junctional hemichannels by PKC
    • doi: 10.1073/pnas.0603154104
    • Bao, X., Lee, S. C., Reuss, L., and Altenberg, G. A. (2007). Change in permeant size selectivity by phosphorylation of connexin 43 gap-junctional hemichannels by PKC. Proc. Natl. Acad. Sci. U.S.A. 104, 4919-4924. doi: 10.1073/pnas.0603154104.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 4919-4924
    • Bao, X.1    Lee, S.C.2    Reuss, L.3    Altenberg, G.A.4
  • 9
    • 84869500645 scopus 로고    scopus 로고
    • Connexin and pannexin hemichannels in inflammatory responses of glia and neurons
    • doi: 10.1016/j.brainres.2012.08.042
    • Bennett, M. V., Garré, J. M., Orellana, J. A., Bukauskas, F. F., Nedergaard, M., and Sáez, J. C. (2012). Connexin and pannexin hemichannels in inflammatory responses of glia and neurons. Brain Res. 1487, 3-15. doi: 10.1016/j.brainres.2012.08.042.
    • (2012) Brain Res. , vol.1487 , pp. 3-15
    • Bennett, M.V.1    Garré, J.M.2    Orellana, J.A.3    Bukauskas, F.F.4    Nedergaard, M.5    Sáez, J.C.6
  • 10
    • 84886897722 scopus 로고    scopus 로고
    • Ca2+dependent nitric oxide release in the injured endothelium of excised rat aorta: a promising mechanism applying in vascular prosthetic devices in aging patients
    • doi: 10.1186/1471-2482-13-S2-S40
    • Berra-Romani, R., Avelino-Cruz, J. E., Raqeeb, A., Della Corte, A., Cinelli, M., Montagnani, S., et al. (2013). Ca2+dependent nitric oxide release in the injured endothelium of excised rat aorta: a promising mechanism applying in vascular prosthetic devices in aging patients. BMC Surg. 13(Suppl. 2), S40. doi: 10.1186/1471-2482-13-S2-S40.
    • (2013) BMC Surg. , vol.13 , Issue.SUPPL. 2
    • Berra-Romani, R.1    Avelino-Cruz, J.E.2    Raqeeb, A.3    Della Corte, A.4    Cinelli, M.5    Montagnani, S.6
  • 11
    • 58149091691 scopus 로고    scopus 로고
    • Oxidative stress, lens gap junctions, and cataracts
    • doi: 10.1089/ars.2008.2119
    • Berthoud, V. M., and Beyer, E. C. (2009). Oxidative stress, lens gap junctions, and cataracts. Antioxid. Redox Signal. 11, 339-353. doi: 10.1089/ars.2008.2119.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 339-353
    • Berthoud, V.M.1    Beyer, E.C.2
  • 12
    • 1642273067 scopus 로고    scopus 로고
    • Gap junction channel gating
    • doi: 10.1016/j.bbamem.2004.01.008
    • Bukauskas, F. F., and Verselis, V. K. (2004). Gap junction channel gating. Biochim. Biophys. Acta. 1662, 42-60. doi: 10.1016/j.bbamem.2004.01.008.
    • (2004) Biochim. Biophys. Acta. , vol.1662 , pp. 42-60
    • Bukauskas, F.F.1    Verselis, V.K.2
  • 13
    • 0035235938 scopus 로고    scopus 로고
    • Connexin 43 hemichannels mediate Ca2+-regulated transmembrane NAD+ fluxes in intact cells
    • doi: 10.1096/fj.00-0566fje
    • Bruzzone, S., Guida, L., Zocchi, E., Franco, L., and De Flora, A. (2001). Connexin 43 hemichannels mediate Ca2+-regulated transmembrane NAD+ fluxes in intact cells. FASEB J. 15, 10-12. doi: 10.1096/fj.00-0566fje.
    • (2001) FASEB J. , vol.15 , pp. 10-12
    • Bruzzone, S.1    Guida, L.2    Zocchi, E.3    Franco, L.4    De Flora, A.5
  • 14
    • 0345255097 scopus 로고    scopus 로고
    • Pannexins, a family of gap junction proteins expressed in brain
    • doi: 10.1073/pnas.2233464100
    • Bruzzone, R., Hormuzdi, S. G., Barbe, M. T., Herb, A., and Monyer, H. (2003). Pannexins, a family of gap junction proteins expressed in brain. Proc. Natl. Acad. Sci. U.S.A. 100, 13644-13649. doi: 10.1073/pnas.2233464100.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13644-13649
    • Bruzzone, R.1    Hormuzdi, S.G.2    Barbe, M.T.3    Herb, A.4    Monyer, H.5
  • 15
    • 70349948843 scopus 로고    scopus 로고
    • The potassium channel subunit Kvbeta3 interacts with pannexin 1 and attenuates its sensitivity to changes in redox potentials
    • doi: 10.1111/j.1742-4658.2009.07334.x
    • Bunse, S., Locovei, S., Schmidt, M., Qiu, F., Zoidl, G., Dahl, G., et al. (2009). The potassium channel subunit Kvbeta3 interacts with pannexin 1 and attenuates its sensitivity to changes in redox potentials. FEBS J. 276, 6258-6270. doi: 10.1111/j.1742-4658.2009.07334.x.
    • (2009) FEBS J. , vol.276 , pp. 6258-6270
    • Bunse, S.1    Locovei, S.2    Schmidt, M.3    Qiu, F.4    Zoidl, G.5    Dahl, G.6
  • 16
    • 78649684422 scopus 로고    scopus 로고
    • Intracellular cysteine 346 is essentially involved in regulating Panx1 channel activity
    • doi: 10.1074/jbc.M110.101014
    • Bunse, S., Schmidt, M., Prochnow, N., Zoidl, G., and Dermietzel, R. (2010). Intracellular cysteine 346 is essentially involved in regulating Panx1 channel activity. J. Biol. Chem. 285, 38444-38452. doi: 10.1074/jbc.M110.101014.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38444-38452
    • Bunse, S.1    Schmidt, M.2    Prochnow, N.3    Zoidl, G.4    Dermietzel, R.5
  • 17
    • 84867997135 scopus 로고    scopus 로고
    • Modulation of the carotid body sensory discharge by NO: an up-dated hypothesis
    • doi: 10.1016/j.resp.2012.04.005
    • Campanucci, V. A., Dookhoo, L., Vollmer, C., and Nurse, C. A. (2012). Modulation of the carotid body sensory discharge by NO: an up-dated hypothesis. Respir. Physiol. Neurobiol. 184, 149-157. doi: 10.1016/j.resp.2012.04.005.
    • (2012) Respir. Physiol. Neurobiol. , vol.184 , pp. 149-157
    • Campanucci, V.A.1    Dookhoo, L.2    Vollmer, C.3    Nurse, C.A.4
  • 18
    • 84863285065 scopus 로고    scopus 로고
    • Pathogenic connexin-31 forms constitutively active hemichannels to promote necrotic cell death
    • doi: 10.1371/journal.pone.0032531
    • Chi, J., Li, L., Liu, M., Tan, J., Tang, C., Pan, Q., et al. (2012). Pathogenic connexin-31 forms constitutively active hemichannels to promote necrotic cell death. PLoS ONE. 7:e32531. doi: 10.1371/journal.pone.0032531.
    • (2012) PLoS ONE. , vol.7
    • Chi, J.1    Li, L.2    Liu, M.3    Tan, J.4    Tang, C.5    Pan, Q.6
  • 19
    • 0037039391 scopus 로고    scopus 로고
    • Metabolic inhibition induces opening of unapposed connexin 43 gap junction hemichannels and reduces gap junctional communication in cortical astrocytes in culture
    • doi: 10.1073/pnas.012589799
    • Contreras, J. E., Sánchez, H. A., Eugenin, E. A., Speidel, D., Theis, M., Willecke, K., et al. (2002). Metabolic inhibition induces opening of unapposed connexin 43 gap junction hemichannels and reduces gap junctional communication in cortical astrocytes in culture. Proc. Natl. Acad. Sci. U.S.A. 99, 495-500. doi: 10.1073/pnas.012589799.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 495-500
    • Contreras, J.E.1    Sánchez, H.A.2    Eugenin, E.A.3    Speidel, D.4    Theis, M.5    Willecke, K.6
  • 20
    • 0141705404 scopus 로고    scopus 로고
    • Gating and regulation of connexin 43 (Cx43) hemichannels
    • doi: 10.1073/pnas.1434298100
    • Contreras, J. E., Sáez, J. C., Bukauskas, F. F., and Bennett, M. V. (2003). Gating and regulation of connexin 43 (Cx43) hemichannels. Proc. Natl. Acad. Sci. U.S.A. 100, 11388-11393. doi: 10.1073/pnas.1434298100.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11388-11393
    • Contreras, J.E.1    Sáez, J.C.2    Bukauskas, F.F.3    Bennett, M.V.4
  • 22
    • 60149097598 scopus 로고    scopus 로고
    • Adhesive properties of connexin hemichannels
    • doi: 10.1002/glia.20728
    • Cotrina, M. L., Lin, J. H., and Nedergaard, M. (2008). Adhesive properties of connexin hemichannels. Glia 56, 1791-1798. doi: 10.1002/glia.20728.
    • (2008) Glia , vol.56 , pp. 1791-1798
    • Cotrina, M.L.1    Lin, J.H.2    Nedergaard, M.3
  • 23
    • 84883551785 scopus 로고    scopus 로고
    • Regulation of connexin-and pannexin-based channels by post-translational modifications
    • doi: 10.1111/boc.201200096
    • D'Hondt, C., Iyyathurai, J., Vinken, M., Rogiers, V., Leybaert, L., Himpens, B., et al. (2013). Regulation of connexin-and pannexin-based channels by post-translational modifications. Biol. Cell 105, 373-398. doi: 10.1111/boc.201200096.
    • (2013) Biol. Cell , vol.105 , pp. 373-398
    • D'Hondt, C.1    Iyyathurai, J.2    Vinken, M.3    Rogiers, V.4    Leybaert, L.5    Himpens, B.6
  • 24
    • 69249213411 scopus 로고    scopus 로고
    • Ca(2+) regulation of connexin 43 hemichannels in C6 glioma and glial cells
    • doi: 10.1016/j.ceca.2009.07.002
    • De Vuyst, E., Wang, N., Decrock, E., De Bock, M., Vinken, M., Van Moorhem, M., et al. (2009). Ca(2+) regulation of connexin 43 hemichannels in C6 glioma and glial cells. Cell Calcium 46, 176-187. doi: 10.1016/j.ceca.2009.07.002.
    • (2009) Cell Calcium , vol.46 , pp. 176-187
    • De Vuyst, E.1    Wang, N.2    Decrock, E.3    De Bock, M.4    Vinken, M.5    Van Moorhem, M.6
  • 25
    • 77950889709 scopus 로고    scopus 로고
    • P2X7 receptors mediate ischemic damage to oligodendrocytes
    • doi: 10.1002/glia.20958
    • Domercq, M., Perez-Samartin, A., Aparicio, D., Alberdi, E., Pampliega, O., and Matute, C. (2010). P2X7 receptors mediate ischemic damage to oligodendrocytes. Glia 58, 730-740. doi: 10.1002/glia.20958.
    • (2010) Glia , vol.58 , pp. 730-740
    • Domercq, M.1    Perez-Samartin, A.2    Aparicio, D.3    Alberdi, E.4    Pampliega, O.5    Matute, C.6
  • 26
    • 0042833257 scopus 로고    scopus 로고
    • Physiology and biophysics of hemi-gap-junctional channels expressed in Xenopus oocytes
    • doi: 10.1046/j.1365-201X.2003.01195.x
    • Ebihara, L. (2003). Physiology and biophysics of hemi-gap-junctional channels expressed in Xenopus oocytes. Acta Physiol. Scand. 179, 5-8. doi: 10.1046/j.1365-201X.2003.01195.x.
    • (2003) Acta Physiol. Scand. , vol.179 , pp. 5-8
    • Ebihara, L.1
  • 27
    • 84871048026 scopus 로고    scopus 로고
    • Purinergic signaling during inflammation
    • doi: 10.1056/NEJMra1205750
    • Eltzschig, H. K., Sitkovsky, M. V., and Robson, S. C. (2012). Purinergic signaling during inflammation. N. Engl. J. Med. 367, 2322-2333. doi: 10.1056/NEJMra1205750.
    • (2012) N. Engl. J. Med. , vol.367 , pp. 2322-2333
    • Eltzschig, H.K.1    Sitkovsky, M.V.2    Robson, S.C.3
  • 28
    • 4444379731 scopus 로고    scopus 로고
    • Connexin30 mutations responsible for hidrotic ectodermal dysplasia cause abnormal hemichannel activity
    • doi: 10.1093/hmg/ddh191
    • Essenfelder, G. M., Bruzzone, R., Lamartine, J., Charollais, A., Blanchet-Bardon, C., Barbe, M. T., et al. (2004). Connexin30 mutations responsible for hidrotic ectodermal dysplasia cause abnormal hemichannel activity. Hum. Mol. Genet. 13, 1703-1714. doi: 10.1093/hmg/ddh191.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1703-1714
    • Essenfelder, G.M.1    Bruzzone, R.2    Lamartine, J.3    Charollais, A.4    Blanchet-Bardon, C.5    Barbe, M.T.6
  • 29
    • 79957480883 scopus 로고    scopus 로고
    • Connexin43 hemichannels contribute to cadmium-induced oxidative stress and cell injury
    • doi: 10.1089/ars.2010.3150
    • Fang, X., Huang, T., Zhu, Y., Yan, Q., Chi, Y., Jiang, J. X., et al. (2011). Connexin43 hemichannels contribute to cadmium-induced oxidative stress and cell injury. Antioxid. Redox Signal. 14, 2427-2439. doi: 10.1089/ars.2010.3150.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 2427-2439
    • Fang, X.1    Huang, T.2    Zhu, Y.3    Yan, Q.4    Chi, Y.5    Jiang, J.X.6
  • 30
    • 84890426600 scopus 로고    scopus 로고
    • Diffusion of nitric oxide across cell membranes of the vascular wall requires specific connexin-based channels
    • doi: 10.1016/j.neuropharm.2013.02.022
    • Figueroa, X. F., Lillo, M. A., Gaete, P. S., Riquelme, M. A., and Sáez, J. C. (2013). Diffusion of nitric oxide across cell membranes of the vascular wall requires specific connexin-based channels. Neuropharmacology 75, 471-478. doi: 10.1016/j.neuropharm.2013.02.022.
    • (2013) Neuropharmacology , vol.75 , pp. 471-478
    • Figueroa, X.F.1    Lillo, M.A.2    Gaete, P.S.3    Riquelme, M.A.4    Sáez, J.C.5
  • 31
    • 84870014750 scopus 로고    scopus 로고
    • Permeation of calcium through purified connexin 26 hemichannels
    • doi: 10.1074/jbc.M112.383281
    • Fiori, M. C., Figueroa, V., Zoghbi, M. E., Saéz, J. C., Reuss, L., and Altenberg, G. A. (2012). Permeation of calcium through purified connexin 26 hemichannels. J. Biol. Chem. 287, 40826-40834. doi: 10.1074/jbc.M112.383281.
    • (2012) J. Biol. Chem. , vol.287 , pp. 40826-40834
    • Fiori, M.C.1    Figueroa, V.2    Zoghbi, M.E.3    Saéz, J.C.4    Reuss, L.5    Altenberg, G.A.6
  • 32
    • 77955091332 scopus 로고    scopus 로고
    • Inhibition of cytokine-induced connexin43 hemichannel activity in astrocytes is neuroprotective
    • doi: 10.1016/j.mcn.2010.05.007
    • Froger, N., Orellana, J. A., Calvo, C. F., Amigou, E., Kozoriz, M. G., Naus, C. C., et al. (2010). Inhibition of cytokine-induced connexin43 hemichannel activity in astrocytes is neuroprotective. Mol. Cell. Neurosci. 45, 37-46. doi: 10.1016/j.mcn.2010.05.007.
    • (2010) Mol. Cell. Neurosci. , vol.45 , pp. 37-46
    • Froger, N.1    Orellana, J.A.2    Calvo, C.F.3    Amigou, E.4    Kozoriz, M.G.5    Naus, C.C.6
  • 33
    • 2942675392 scopus 로고    scopus 로고
    • S-nitrosylation signaling in cell biology
    • doi: 10.1124/mi.3.5.253
    • Gaston, B. M., Carver, J., Doctor, A., and Palmer, L. A. (2003). S-nitrosylation signaling in cell biology. Mol. Interv. 3, 253-263. doi: 10.1124/mi.3.5.253.
    • (2003) Mol. Interv. , vol.3 , pp. 253-263
    • Gaston, B.M.1    Carver, J.2    Doctor, A.3    Palmer, L.A.4
  • 34
    • 34250807258 scopus 로고    scopus 로고
    • Aberrant hemichannel properties of Cx26 mutations causing skin disease and deafness
    • doi: 10.1152/ajpcell.00626.2006
    • Gerido, D. A., DeRosa, A. M., Richard, G., and White, T. W. (2007). Aberrant hemichannel properties of Cx26 mutations causing skin disease and deafness. Am. J. Physiol. Cell Physiol. 293, C337-C345. doi: 10.1152/ajpcell.00626.2006.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Gerido, D.A.1    DeRosa, A.M.2    Richard, G.3    White, T.W.4
  • 35
    • 0033224243 scopus 로고    scopus 로고
    • Selective transfer of endogenous metabolites through gap junctions composed of different connexins
    • doi: 10.1038/15693
    • Goldberg, G. S., Lampe, P. D., and Nicholson, B. J. (1999). Selective transfer of endogenous metabolites through gap junctions composed of different connexins. Nat. Cell Biol. 1, 457-459. doi: 10.1038/15693.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 457-459
    • Goldberg, G.S.1    Lampe, P.D.2    Nicholson, B.J.3
  • 37
    • 0019781741 scopus 로고
    • Calcium-dependent proteolysis in living cells
    • doi: 10.1016/0024-3205(81)90194-6
    • Ishiura, S. (1981). Calcium-dependent proteolysis in living cells. Life Sci. 29, 1079-1087. doi: 10.1016/0024-3205(81)90194-6.
    • (1981) Life Sci. , vol.29 , pp. 1079-1087
    • Ishiura, S.1
  • 38
    • 84864358695 scopus 로고    scopus 로고
    • Posttranslational modifications in connexins and pannexins
    • doi: 10.1007/s00232-012-9453-3
    • Johnstone, S. R., Billaud, M., Lohman, A. W., Taddeo, E. P., and Isakson, B. E. (2012). Posttranslational modifications in connexins and pannexins. J. Membr. Biol. 245, 319-332. doi: 10.1007/s00232-012-9453-3.
    • (2012) J. Membr. Biol. , vol.245 , pp. 319-332
    • Johnstone, S.R.1    Billaud, M.2    Lohman, A.W.3    Taddeo, E.P.4    Isakson, B.E.5
  • 39
    • 84873605124 scopus 로고    scopus 로고
    • H(2)S signaling in redox regulation of cellular functions
    • doi: 10.1139/cjpp-2012-0293
    • Ju, Y., Zhang, W., Pei, Y., and Yang, G. (2013). H(2)S signaling in redox regulation of cellular functions. Can. J. Physiol. Pharmacol. 91, 8-14. doi: 10.1139/cjpp-2012-0293.
    • (2013) Can. J. Physiol. Pharmacol. , vol.91 , pp. 8-14
    • Ju, Y.1    Zhang, W.2    Pei, Y.3    Yang, G.4
  • 40
    • 0031710971 scopus 로고    scopus 로고
    • Transfer of second messengers through gap junction connexin 43 channels reconstituted in liposomes
    • doi: 10.1016/S0005-2736(98)00075-3
    • Kam, Y., Kim, D. Y., Koo, S. K., and Joe, C. O. (1998). Transfer of second messengers through gap junction connexin 43 channels reconstituted in liposomes. Biochim. Biophys. Acta 1372, 384-388. doi: 10.1016/S0005-2736(98)00075-3.
    • (1998) Biochim. Biophys. Acta , vol.1372 , pp. 384-388
    • Kam, Y.1    Kim, D.Y.2    Koo, S.K.3    Joe, C.O.4
  • 42
    • 84862166302 scopus 로고    scopus 로고
    • Biological role of connexin intercellular channels and hemichannels
    • doi: 10.1016/j.abb.2012.03.008
    • Kar, R., Batra, N., Riquelme, M. A., and Jiang, J. X. (2012). Biological role of connexin intercellular channels and hemichannels. Arch. Biochem. Biophys. 524, 2-15. doi: 10.1016/j.abb.2012.03.008.
    • (2012) Arch. Biochem. Biophys. , vol.524 , pp. 2-15
    • Kar, R.1    Batra, N.2    Riquelme, M.A.3    Jiang, J.X.4
  • 43
    • 84879584067 scopus 로고    scopus 로고
    • A tale of two gases: NO and H2S, foes or friends for life?
    • doi: 10.1016/j.redox.2013.05.001
    • Kolluru, G. K., Shen, X., and Kevil, C. G. (2013). A tale of two gases: NO and H2S, foes or friends for life? Redox Biol. 1, 313-318. doi: 10.1016/j.redox.2013.05.001.
    • (2013) Redox Biol. , vol.1 , pp. 313-318
    • Kolluru, G.K.1    Shen, X.2    Kevil, C.G.3
  • 44
    • 84866742557 scopus 로고    scopus 로고
    • The N-terminal half of the connexin protein contains the core elements of the pore and voltage gates
    • doi: 10.1007/s00232-012-9457-z
    • Kronengold, J., Srinivas, M., and Verselis, V. K. (2012). The N-terminal half of the connexin protein contains the core elements of the pore and voltage gates. J. Membr. Biol. 245, 453-463. doi: 10.1007/s00232-012-9457-z.
    • (2012) J. Membr. Biol. , vol.245 , pp. 453-463
    • Kronengold, J.1    Srinivas, M.2    Verselis, V.K.3
  • 45
    • 77949400181 scopus 로고    scopus 로고
    • Comprehensive identification and modified-site mapping of S-nitrosylated targets in prostate epithelial cells
    • doi: 10.1371/journal.pone.0009075
    • Lam, Y. W., Yuan, Y., Isaac, J., Babu, C. V., Meller, J., and Ho, S. M. (2010). Comprehensive identification and modified-site mapping of S-nitrosylated targets in prostate epithelial cells. PLoS ONE. 5:e9075. doi: 10.1371/journal.pone.0009075.
    • (2010) PLoS ONE. , vol.5
    • Lam, Y.W.1    Yuan, Y.2    Isaac, J.3    Babu, C.V.4    Meller, J.5    Ho, S.M.6
  • 46
    • 0034671950 scopus 로고    scopus 로고
    • Regulation of gap junctions by phosphorylation of connexins
    • doi: 10.1006/abbi.2000.2131
    • Lampe, P. D., and Lau, A. F. (2000). Regulation of gap junctions by phosphorylation of connexins. Arch. Biochem. Biophys. 384, 205-215. doi: 10.1006/abbi.2000.2131.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 205-215
    • Lampe, P.D.1    Lau, A.F.2
  • 47
    • 33744479681 scopus 로고    scopus 로고
    • S-nitrosylation of cysteine 289 of the AT1 receptor decreases its affinity for angiotensin II
    • doi: 10.1038/sj.bjp.0706725
    • Leclerc, P. C., Lanctot, P. M., Auger-Messier, M., Escher, E., Leduc, R., and Guillemette, G. (2006) S-nitrosylation of cysteine 289 of the AT1 receptor decreases its affinity for angiotensin II. Br. J. Pharmacol. 148, 306-313. doi: 10.1038/sj.bjp.0706725.
    • (2006) Br. J. Pharmacol. , vol.148 , pp. 306-313
    • Leclerc, P.C.1    Lanctot, P.M.2    Auger-Messier, M.3    Escher, E.4    Leduc, R.5    Guillemette, G.6
  • 48
    • 84055168825 scopus 로고    scopus 로고
    • Pathological hemichannels associated with human Cx26 mutations causing Keratitis-Ichthyosis-Deafness syndrome
    • doi: 10.1016/j.bbamem.2011.09.003
    • Levit, N. A., Mese, G., Basaly, M. G., and White, T. W. (2012). Pathological hemichannels associated with human Cx26 mutations causing Keratitis-Ichthyosis-Deafness syndrome. Biochim. Biophys. Acta 1818, 2014-2019. doi: 10.1016/j.bbamem.2011.09.003.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2014-2019
    • Levit, N.A.1    Mese, G.2    Basaly, M.G.3    White, T.W.4
  • 50
    • 29344452180 scopus 로고    scopus 로고
    • Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium
    • doi: 10.1016/j.febslet.2005.12.004
    • Locovei, S., Wang, J., and Dahl, G. (2006). Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium. FEBS Lett. 580, 239-244. doi: 10.1016/j.febslet.2005.12.004.
    • (2006) FEBS Lett. , vol.580 , pp. 239-244
    • Locovei, S.1    Wang, J.2    Dahl, G.3
  • 51
    • 84869234325 scopus 로고    scopus 로고
    • S-nitrosylation inhibits pannexin 1 channel function
    • doi: 10.1074/jbc.M112.397976
    • Lohman, A. W., Weaver, J. L., Billaud, M., Sandilos, J. K., Griffiths, R., Straub, A. C., et al. (2012). S-nitrosylation inhibits pannexin 1 channel function. J. Biol. Chem. 287, 39602-39612. doi: 10.1074/jbc.M112.397976.
    • (2012) J. Biol. Chem. , vol.287 , pp. 39602-39612
    • Lohman, A.W.1    Weaver, J.L.2    Billaud, M.3    Sandilos, J.K.4    Griffiths, R.5    Straub, A.C.6
  • 52
    • 0024095587 scopus 로고
    • Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations
    • Milks, L. C., Kumar, N. M., Houghten, R., Unwin, N., and Gilula, N. B. (1988). Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations. EMBO J. 7, 2967-2975.
    • (1988) EMBO J. , vol.7 , pp. 2967-2975
    • Milks, L.C.1    Kumar, N.M.2    Houghten, R.3    Unwin, N.4    Gilula, N.B.5
  • 53
    • 20444404602 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to channel gating
    • doi: 10.1016/j.bbamem.2005.02.016
    • Moreno, A. P. (2005). Connexin phosphorylation as a regulatory event linked to channel gating. Biochim. Biophys. Acta 1711, 164-171. doi: 10.1016/j.bbamem.2005.02.016.
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 164-171
    • Moreno, A.P.1
  • 54
    • 0034075770 scopus 로고    scopus 로고
    • A novel C202F mutation in the connexin 26 gene (GJB2) associated with autosomal dominant isolated hearing loss
    • doi: 10.1136/jmg.37.5.368
    • Morlé, L., Bozon, M., Alloisio, N., Latour, P., Vandenberghe, A., Plauchu, H., et al. (2000). A novel C202F mutation in the connexin 26 gene (GJB2) associated with autosomal dominant isolated hearing loss. Med. Genet. 37, 368-370. doi: 10.1136/jmg.37.5.368.
    • (2000) Med. Genet. , vol.37 , pp. 368-370
    • Morlé, L.1    Bozon, M.2    Alloisio, N.3    Latour, P.4    Vandenberghe, A.5    Plauchu, H.6
  • 55
    • 84878443676 scopus 로고    scopus 로고
    • Aberrant protein s-nitrosylation in neurodegenerative diseases
    • doi: 10.1016/j.neuron.2013.05.005
    • Nakamura, T., Tu, S., Akhtar, M. W., Sunico, C. R., Okamoto, S., and Lipton, S. A. (2013). Aberrant protein s-nitrosylation in neurodegenerative diseases. Neuron 78, 596-614. doi: 10.1016/j.neuron.2013.05.005.
    • (2013) Neuron , vol.78 , pp. 596-614
    • Nakamura, T.1    Tu, S.2    Akhtar, M.W.3    Sunico, C.R.4    Okamoto, S.5    Lipton, S.A.6
  • 56
    • 0034106797 scopus 로고    scopus 로고
    • Selective permeability of different connexin channels to the second messenger inositol 1,4,5-trisphosphate
    • Niessen, H., Harz, H., Bedner, P., Krämer, K., and Willecke, K. (2000). Selective permeability of different connexin channels to the second messenger inositol 1,4,5-trisphosphate. J. Cell Sci. 113, 1365-1372.
    • (2000) J. Cell Sci. , vol.113 , pp. 1365-1372
    • Niessen, H.1    Harz, H.2    Bedner, P.3    Krämer, K.4    Willecke, K.5
  • 57
    • 80051759671 scopus 로고    scopus 로고
    • ATP and glutamate released via astroglialconnexin 43 hemichannels mediate neuronal death through activation of pannexin 1 hemichannels
    • doi: 10.1111/j.1471-4159.2011.07210.x
    • Orellana, J. A., Froger, N., Ezan, P., Jiang, J. X., Bennett, M. V., Naus, C. C., et al. (2011). ATP and glutamate released via astroglialconnexin 43 hemichannels mediate neuronal death through activation of pannexin 1 hemichannels. J. Neurochem. 118, 826-840. doi: 10.1111/j.1471-4159.2011.07210.x.
    • (2011) J. Neurochem. , vol.118 , pp. 826-840
    • Orellana, J.A.1    Froger, N.2    Ezan, P.3    Jiang, J.X.4    Bennett, M.V.5    Naus, C.C.6
  • 58
    • 84895457787 scopus 로고    scopus 로고
    • Role of connexins and pannexins in ischemic stroke
    • [Epub ahead of print].
    • Orellana, J. A., Avendaño, B. C., and Montero, T. D. (2013). Role of connexins and pannexins in ischemic stroke. Curr. Med. Chem. [Epub ahead of print].
    • (2013) Curr. Med. Chem.
    • Orellana, J.A.1    Avendaño, B.C.2    Montero, T.D.3
  • 59
    • 33750473352 scopus 로고    scopus 로고
    • Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
    • doi: 10.1038/sj.emboj.7601378
    • Pelegrin, P., and Surprenant, A. (2006). Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor. EMBO J. 25, 5071-5082. doi: 10.1038/sj.emboj.7601378.
    • (2006) EMBO J. , vol.25 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 60
    • 36549084087 scopus 로고    scopus 로고
    • Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins
    • doi: 10.1242/jcs.009514
    • Penuela, S., Bhalla, R., Gong, X. Q., Cowan, K. N., Celetti, S. J., Cowan, B. J., et al. (2007). Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins. J. Cell Sci. 120, 3772-3783. doi: 10.1242/jcs.009514.
    • (2007) J. Cell Sci. , vol.120 , pp. 3772-3783
    • Penuela, S.1    Bhalla, R.2    Gong, X.Q.3    Cowan, K.N.4    Celetti, S.J.5    Cowan, B.J.6
  • 61
    • 84870054442 scopus 로고    scopus 로고
    • The biochemistry and function of pannexin channels
    • doi: 10.1016/j.bbamem.2012.01.017
    • Penuela, S., Gehi, R., and Laird, D. W. (2013). The biochemistry and function of pannexin channels. Biochim. Biophys. Acta 1828, 15-22. doi: 10.1016/j.bbamem.2012.01.017.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 15-22
    • Penuela, S.1    Gehi, R.2    Laird, D.W.3
  • 62
    • 1642385314 scopus 로고    scopus 로고
    • Chemical gating of gap junction channels; roles of calcium, pH and calmodulin
    • doi: 10.1016/j.bbamem.2003.10.020
    • Peracchia, C. (2004). Chemical gating of gap junction channels; roles of calcium, pH and calmodulin. Biochim. Biophys. Acta. 1662, 61-80. doi: 10.1016/j.bbamem.2003.10.020.
    • (2004) Biochim. Biophys. Acta. , vol.1662 , pp. 61-80
    • Peracchia, C.1
  • 63
    • 78649894823 scopus 로고    scopus 로고
    • Intramolecular loop/tail interactions are essential for connexin 43-hemichannel activity
    • doi: 10.1096/fj.09-153007
    • Ponsaerts, R., De Vuyst, E., Retamal, M., D'Hondt, C., Vermeire, D., Wang, N., et al. (2010). Intramolecular loop/tail interactions are essential for connexin 43-hemichannel activity. FASEB J. 24, 4378-4395. doi: 10.1096/fj.09-153007.
    • (2010) FASEB J. , vol.24 , pp. 4378-4395
    • Ponsaerts, R.1    De Vuyst, E.2    Retamal, M.3    D'Hondt, C.4    Vermeire, D.5    Wang, N.6
  • 64
    • 73349131079 scopus 로고    scopus 로고
    • Replacement of a single cysteine in the fourth transmembrane region of zebrafish pannexin 1 alters hemichannel gating behavior
    • doi: 10.1007/s00221-009-1957-4
    • Prochnow, N., Hoffmann, S., Dermietzel, R., and Zoidl, G. (2009). Replacement of a single cysteine in the fourth transmembrane region of zebrafish pannexin 1 alters hemichannel gating behavior. Exp. Brain Res. 199, 255-264. doi: 10.1007/s00221-009-1957-4.
    • (2009) Exp. Brain Res. , vol.199 , pp. 255-264
    • Prochnow, N.1    Hoffmann, S.2    Dermietzel, R.3    Zoidl, G.4
  • 65
    • 77953058721 scopus 로고    scopus 로고
    • Diversity and properties of connexin gap junction channels
    • Rackauskas, M., Neverauskas, V., and Skeberdis, V. A.(2010). Diversity and properties of connexin gap junction channels. Medicina (Kaunas). 46, 1-12.
    • (2010) Medicina (Kaunas) , vol.46 , pp. 1-12
    • Rackauskas, M.1    Neverauskas, V.2    Skeberdis, V.A.3
  • 66
    • 40249103337 scopus 로고    scopus 로고
    • A novel role for connexin hemichannel in oxidative stress and smoking-induced cell injury
    • doi: 10.1371/journal.pone.0000712
    • Ramachandran, S., Xie, L. H., John, S. A., Subramaniam, S., and Lal, R. (2007). A novel role for connexin hemichannel in oxidative stress and smoking-induced cell injury. PLoS ONE. 2:e712. doi: 10.1371/journal.pone.0000712.
    • (2007) PLoS ONE. , vol.2
    • Ramachandran, S.1    Xie, L.H.2    John, S.A.3    Subramaniam, S.4    Lal, R.5
  • 68
    • 33645238079 scopus 로고    scopus 로고
    • S-nitrosylation and permeation through connexin 43 hemichannels in astrocytes: induction by oxidant stress and reversal by reducing agents
    • doi: 10.1073/pnas.0511118103
    • Retamal, M. A., Cortés, C. J., Reuss, L., Bennett, M. V., and Sáez, J. C. (2006). S-nitrosylation and permeation through connexin 43 hemichannels in astrocytes: induction by oxidant stress and reversal by reducing agents. Proc. Natl. Acad. Sci. U.S.A. 103, 4475-4480. doi: 10.1073/pnas.0511118103.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4475-4480
    • Retamal, M.A.1    Cortés, C.J.2    Reuss, L.3    Bennett, M.V.4    Sáez, J.C.5
  • 69
    • 37249015389 scopus 로고    scopus 로고
    • Cx43 hemichannels and gap junction channels in astrocytes are regulated oppositely by proinflammatory cytokines released from activated microglia
    • doi: 10.1523/JNEUROSCI.2042-07.2007
    • Retamal, M. A., Froger, N., Palacios-Prado, N., Ezan, P., Sáez, P. J., Sáez, J. C., et al. (2007a). Cx43 hemichannels and gap junction channels in astrocytes are regulated oppositely by proinflammatory cytokines released from activated microglia. J. Neurosci. 27, 13781-13792. doi: 10.1523/JNEUROSCI.2042-07.2007.
    • (2007) J. Neurosci. , vol.27 , pp. 13781-13792
    • Retamal, M.A.1    Froger, N.2    Palacios-Prado, N.3    Ezan, P.4    Sáez, P.J.5    Sáez, J.C.6
  • 70
    • 34347261750 scopus 로고    scopus 로고
    • Opening of connexin 43 hemichannels is increased by lowering intracellular redox potential
    • doi: 10.1073/pnas.0702456104
    • Retamal, M. A., Schalper, K. A., Shoji, K. F., Bennett, M. V., and Sáez, J. C. (2007b). Opening of connexin 43 hemichannels is increased by lowering intracellular redox potential. Proc. Natl. Acad. Sci. U.S.A. 104, 8322-8327. doi: 10.1073/pnas.0702456104.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 8322-8327
    • Retamal, M.A.1    Schalper, K.A.2    Shoji, K.F.3    Bennett, M.V.4    Sáez, J.C.5
  • 71
    • 66749132787 scopus 로고    scopus 로고
    • Modulation of Cx46 hemichannels by nitric oxide
    • doi: 10.1152/ajpcell.00054.2009
    • Retamal, M. A., Yin, S., Altenberg, G. A., and Reuss, L. (2009). Modulation of Cx46 hemichannels by nitric oxide. Am. J. Physiol. Cell Physiol. 296, C1356-C1363. doi: 10.1152/ajpcell.00054.2009.
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296
    • Retamal, M.A.1    Yin, S.2    Altenberg, G.A.3    Reuss, L.4
  • 73
    • 77957101431 scopus 로고    scopus 로고
    • Extracellular ATP is a danger signal activating P2X7 receptor in lung inflammation and fibrosis
    • doi: 10.1164/rccm.201003-0359OC
    • Riteau, N., Gasse, P., Fauconnier, L., Gombault, A., Couegnat, M., Fick, L., et al. (2010). Extracellular ATP is a danger signal activating P2X7 receptor in lung inflammation and fibrosis. Am. J. Respir. Crit. Care Med. 182, 774-783. doi: 10.1164/rccm.201003-0359OC.
    • (2010) Am. J. Respir. Crit. Care Med. , vol.182 , pp. 774-783
    • Riteau, N.1    Gasse, P.2    Fauconnier, L.3    Gombault, A.4    Couegnat, M.5    Fick, L.6
  • 74
    • 0034918779 scopus 로고    scopus 로고
    • Dual mechanism of intercellular communication in HOBIT osteoblastic cells: a role for gap-junctional hemichannels
    • doi: 10.1359/jbmr.2001.16.8.1465
    • Romanello, M., and D'Andrea, P. (2001). Dual mechanism of intercellular communication in HOBIT osteoblastic cells: a role for gap-junctional hemichannels. J. Bone Miner. Res. 16, 1465-1476. doi: 10.1359/jbmr.2001.16.8.1465.
    • (2001) J. Bone Miner. Res. , vol.16 , pp. 1465-1476
    • Romanello, M.1    D'Andrea, P.2
  • 75
    • 0343058567 scopus 로고
    • Hepatocyte gap junctions are permeable to the second messenger, inositol 1,4,5-trisphosphate, and to calcium ions
    • doi: 10.1073/pnas.86.8.2708
    • Sáez, J. C., Connor, J. A., Spray, D. C., and Bennett, M. V. (1989). Hepatocyte gap junctions are permeable to the second messenger, inositol 1,4,5-trisphosphate, and to calcium ions. Proc. Natl. Acad. Sci. U.S.A. 86, 2708-2712. doi: 10.1073/pnas.86.8.2708.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 2708-2712
    • Sáez, J.C.1    Connor, J.A.2    Spray, D.C.3    Bennett, M.V.4
  • 77
    • 77955087401 scopus 로고    scopus 로고
    • Cell membrane permeabilization via connexin hemichannels in living and dying cells
    • doi: 10.1016/j.yexcr.2010.05.026
    • Sáez, J. C., Schalper, K. A., Retamal, M. A., Orellana, J. A., Shoji, K. F., and Bennett, M. V. (2010). Cell membrane permeabilization via connexin hemichannels in living and dying cells. Exp. Cell Res. 316, 2377-2389. doi: 10.1016/j.yexcr.2010.05.026.
    • (2010) Exp. Cell Res. , vol.316 , pp. 2377-2389
    • Sáez, J.C.1    Schalper, K.A.2    Retamal, M.A.3    Orellana, J.A.4    Shoji, K.F.5    Bennett, M.V.6
  • 78
    • 77954320871 scopus 로고    scopus 로고
    • 2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome
    • doi: 10.1085/jgp.201010433
    • 2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome. J. Gen. Physiol. 136, 47-62. doi: 10.1085/jgp.201010433.
    • (2010) J. Gen. Physiol. , vol.136 , pp. 47-62
    • Sánchez, H.A.1    Mese, G.2    Srinivas, M.3    White, T.W.4    Verselis, V.K.5
  • 80
    • 0026611599 scopus 로고
    • Ca2+/calmodulin-regulated nitric oxide synthases
    • doi: 10.1016/0143-4160(92)90055-W
    • Schmidt, H. H., Pollock, J. S., Nakane, M., Förstermann, U., and Murad, F. (1992). Ca2+/calmodulin-regulated nitric oxide synthases. Cell Calcium 13, 427-434. doi: 10.1016/0143-4160(92)90055-W.
    • (1992) Cell Calcium , vol.13 , pp. 427-434
    • Schmidt, H.H.1    Pollock, J.S.2    Nakane, M.3    Förstermann, U.4    Murad, F.5
  • 81
    • 42649102649 scopus 로고    scopus 로고
    • Connexin and pannexin mediated cell-cell communication
    • doi: 10.1017/S1740925X08000069
    • Scemes, E., Suadicani, S. O., Dahl, G., and Spray, D. C. (2007). Connexin and pannexin mediated cell-cell communication. Neuron Glia Biol. 2007, 199-208. doi: 10.1017/S1740925X08000069.
    • (2007) Neuron Glia Biol. , vol.2007 , pp. 199-208
    • Scemes, E.1    Suadicani, S.O.2    Dahl, G.3    Spray, D.C.4
  • 83
    • 0031984904 scopus 로고    scopus 로고
    • A novel mutation (C201R) in the transmembrane domain of connexin 32 in severe X-linked Charcot-Marie-Tooth disease
    • doi: 10.1002/humu.1380110104
    • Sillén, A., Annerén, G., and Dahl, N. (1998). A novel mutation (C201R) in the transmembrane domain of connexin 32 in severe X-linked Charcot-Marie-Tooth disease. Hum. Mutat. 1998(Suppl. 1), S8-S9. doi: 10.1002/humu.1380110104.
    • (1998) Hum. Mutat. , vol.1998 , Issue.SUPPL. 1
    • Sillén, A.1    Annerén, G.2    Dahl, N.3
  • 86
    • 84865765992 scopus 로고    scopus 로고
    • Release of gliotransmitters through astroglialconnexin 43 hemichannels is necessary for fear memory consolidation in the basolateral amygdala
    • doi: 10.1096/fj.11-198416
    • Stehberg, J., Moraga-Amaro, R., Salazar, C., Becerra, A., Echeverría, C., Orellana, J. A., et al. (2012). Release of gliotransmitters through astroglialconnexin 43 hemichannels is necessary for fear memory consolidation in the basolateral amygdala. FASEB J. 26, 3649-3657. doi: 10.1096/fj.11-198416.
    • (2012) FASEB J. , vol.26 , pp. 3649-3657
    • Stehberg, J.1    Moraga-Amaro, R.2    Salazar, C.3    Becerra, A.4    Echeverría, C.5    Orellana, J.A.6
  • 87
    • 33845505914 scopus 로고    scopus 로고
    • A novel mechanism for connexin 26 mutation linked deafness: cell death caused by leaky gap junction hemichannels
    • doi: 10.1097/01.mlg.0000241944.77192.d2
    • Stong, B. C., Chang, Q., Ahmad, S., and Lin, X. (2006). A novel mechanism for connexin 26 mutation linked deafness: cell death caused by leaky gap junction hemichannels. Laryngoscope 116, 2205-2210. doi: 10.1097/01.mlg.0000241944.77192.d2.
    • (2006) Laryngoscope , vol.116 , pp. 2205-2210
    • Stong, B.C.1    Chang, Q.2    Ahmad, S.3    Lin, X.4
  • 88
    • 0037155841 scopus 로고    scopus 로고
    • Intercellular calcium signaling in astrocytes via ATP release through connexin hemichannels
    • doi: 10.1074/jbc.M109902200
    • Stout, C. E., Costantin, J. L., Naus, C. C., and Charles, A. C. (2002). Intercellular calcium signaling in astrocytes via ATP release through connexin hemichannels. J. Biol. Chem. 277, 10482-10488. doi: 10.1074/jbc.M109902200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10482-10488
    • Stout, C.E.1    Costantin, J.L.2    Naus, C.C.3    Charles, A.C.4
  • 89
    • 79551497451 scopus 로고    scopus 로고
    • Compartmentalized connexin 43s-nitrosylation/denitrosylation regulates heterocellular communication in the vessel wall
    • doi: 10.1161/ATVBAHA.110.215939
    • Straub, A. C., Billaud, M., Johnstone, S. R., Best, A. K., Yemen, S., Dwyer, S. T., et al. (2011). Compartmentalized connexin 43s-nitrosylation/denitrosylation regulates heterocellular communication in the vessel wall. Arterioscler. Thromb. Vasc. Biol. 31, 399-407. doi: 10.1161/ATVBAHA.110.215939.
    • (2011) Arterioscler. Thromb. Vasc. Biol. , vol.31 , pp. 399-407
    • Straub, A.C.1    Billaud, M.2    Johnstone, S.R.3    Best, A.K.4    Yemen, S.5    Dwyer, S.T.6
  • 90
    • 33646584876 scopus 로고    scopus 로고
    • Ischemia opens neuronal gap junction hemichannels
    • doi: 10.1126/science.1126241
    • Thompson, R. J., Zhou, N., and MacVicar, B. A. (2006). Ischemia opens neuronal gap junction hemichannels. Science 312, 924-927. doi: 10.1126/science.1126241.
    • (2006) Science , vol.312 , pp. 924-927
    • Thompson, R.J.1    Zhou, N.2    MacVicar, B.A.3
  • 91
    • 79955557177 scopus 로고    scopus 로고
    • Different consequences of cataract-associated mutations at adjacent positions in the first extracellular boundary of connexin50
    • doi: 10.1152/ajpcell.00384.2010
    • Tong, J. J., Minogue, P. J., Guo, W., Chen, T. L., Beyer, E. C., Berthoud, V. M., et al. (2011) Different consequences of cataract-associated mutations at adjacent positions in the first extracellular boundary of connexin50. Am. J. Physiol. Cell Physiol. 300, C1055-C1064. doi: 10.1152/ajpcell.00384.2010.
    • (2011) Am. J. Physiol. Cell Physiol. , vol.300
    • Tong, J.J.1    Minogue, P.J.2    Guo, W.3    Chen, T.L.4    Beyer, E.C.5    Berthoud, V.M.6
  • 92
    • 84881582031 scopus 로고    scopus 로고
    • Cyclic nucleotide permeability through unopposed connexin hemichannels
    • doi: 10.3389/fphar.2013.00075
    • Valiunas, V. (2013). Cyclic nucleotide permeability through unopposed connexin hemichannels. Front. Pharmacol. 4:75. doi: 10.3389/fphar.2013.00075.
    • (2013) Front. Pharmacol. , vol.4 , pp. 75
    • Valiunas, V.1
  • 93
    • 50449110491 scopus 로고    scopus 로고
    • Divalent cations regulate connexin hemichannels by modulating intrinsic voltage-dependent gating
    • doi: 10.1085/jgp.200810029
    • Verselis, V. K., and Srinivas, M. (2008). Divalent cations regulate connexin hemichannels by modulating intrinsic voltage-dependent gating. J. Gen. Physiol. 132, 315-327. doi: 10.1085/jgp.200810029.
    • (2008) J. Gen. Physiol. , vol.132 , pp. 315-327
    • Verselis, V.K.1    Srinivas, M.2
  • 94
    • 84884690783 scopus 로고    scopus 로고
    • Ephaptic communication in the vertebrate retina
    • doi: 10.3389/fnhum.2013.00612
    • Vroman, R., Klaassen, L. J., and Kamermans, M. (2013). Ephaptic communication in the vertebrate retina. Front. Hum. Neurosci. 7:612. doi: 10.3389/fnhum.2013.00612.
    • (2013) Front. Hum. Neurosci. , vol.7 , pp. 612
    • Vroman, R.1    Klaassen, L.J.2    Kamermans, M.3
  • 95
    • 79953154392 scopus 로고    scopus 로고
    • Nitric oxide: promoter or suppressor of programmed cell death?
    • doi: 10.1007/s13238-010-0018-x
    • Wang, Y., Chen, C., Loake, G. J., and Chu, C. (2010). Nitric oxide: promoter or suppressor of programmed cell death? Protein Cell 1, 133-142. doi: 10.1007/s13238-010-0018-x.
    • (2010) Protein Cell , vol.1 , pp. 133-142
    • Wang, Y.1    Chen, C.2    Loake, G.J.3    Chu, C.4
  • 96
    • 78649480274 scopus 로고    scopus 로고
    • SCAM analysis of Panx1 suggests a peculiar pore structure
    • doi: 10.1085/jgp.201010440
    • Wang, J., and Dahl, G. (2010). SCAM analysis of Panx1 suggests a peculiar pore structure. J. Gen. Physiol. 136, 515-527. doi: 10.1085/jgp.201010440.
    • (2010) J. Gen. Physiol. , vol.136 , pp. 515-527
    • Wang, J.1    Dahl, G.2
  • 97
    • 84865708285 scopus 로고    scopus 로고
    • Anoxia-induced NMDA receptor activation opens pannexin channels via Src family kinases
    • doi: 10.1523/JNEUROSCI.1267-12.2012
    • Weilinger, N. L., Tang, P. L., and Thompson, R. J. (2012). Anoxia-induced NMDA receptor activation opens pannexin channels via Src family kinases. J. Neurosci. 32, 12579-12588. doi: 10.1523/JNEUROSCI.1267-12.2012.
    • (2012) J. Neurosci. , vol.32 , pp. 12579-12588
    • Weilinger, N.L.1    Tang, P.L.2    Thompson, R.J.3
  • 98
    • 79959710752 scopus 로고    scopus 로고
    • Carbon monoxide: an emerging regulator of ion channels
    • doi: 10.1113/J Physiol.2011.206706
    • Wilkinson, W. J., and Kemp, P. J. (2011). Carbon monoxide: an emerging regulator of ion channels. J. Physiol. 589, 3055-3062. doi: 10.1113/J Physiol.2011.206706.
    • (2011) J. Physiol. , vol.589 , pp. 3055-3062
    • Wilkinson, W.J.1    Kemp, P.J.2
  • 99
    • 0037531231 scopus 로고    scopus 로고
    • Functional hemichannels in astrocytes: a novel mechanism of glutamate release
    • Ye, Z. C., Wyeth, M. S., Baltan-Tekkok, S., and Ransom, B. R. (2003). Functional hemichannels in astrocytes: a novel mechanism of glutamate release. J. Neurosci. 23, 3588-3596.
    • (2003) J. Neurosci. , vol.23 , pp. 3588-3596
    • Ye, Z.C.1    Wyeth, M.S.2    Baltan-Tekkok, S.3    Ransom, B.R.4
  • 100
    • 0026515179 scopus 로고
    • Membrane topology and quaternary structure of cardiac gap junction ion channels
    • doi: 10.1016/0022-2836(92)90253-G
    • Yeager, M., and Gilula, N. B.(1992). Membrane topology and quaternary structure of cardiac gap junction ion channels. J. Mol. Biol. 223, 929-948. doi: 10.1016/0022-2836(92)90253-G.
    • (1992) J. Mol. Biol. , vol.223 , pp. 929-948
    • Yeager, M.1    Gilula, N.B.2
  • 101
    • 48249095934 scopus 로고    scopus 로고
    • Role for nitric oxide in permeability of hippocampal neuronal hemichannels during oxygen glucose deprivation
    • doi: 10.1002/jnr.21675
    • Zhang, L., Deng, T., Sun, Y., Liu, K., Yang, Y., and Zheng, X. (2008). Role for nitric oxide in permeability of hippocampal neuronal hemichannels during oxygen glucose deprivation. J. Neurosci. Res. 86, 2281-2291. doi: 10.1002/jnr.21675.
    • (2008) J. Neurosci. Res. , vol.86 , pp. 2281-2291
    • Zhang, L.1    Deng, T.2    Sun, Y.3    Liu, K.4    Yang, Y.5    Zheng, X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.