메뉴 건너뛰기




Volumn 5 JUN, Issue , 2014, Pages

Possible role of hemichannels in cancer

Author keywords

Cancer; Connexins; Hemichannels; Pannexins

Indexed keywords

5' NUCLEOTIDASE; ADENOSINE TRIPHOSPHATE; CALCIUM; CD38 ANTIGEN; CD39 ANTIGEN; CONNEXIN 26; CONNEXIN 30; CONNEXIN 32; CONNEXIN 36; CONNEXIN 37; CONNEXIN 40; CONNEXIN 43; DARATUMUMAB; GAP JUNCTION PROTEIN; HEMICHANNEL; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; MOR 03087; NICOTINAMIDE ADENINE DINUCLEOTIDE; PANNEXIN; PANNEXIN 1; PLATINUM COMPLEX; PURINERGIC P2X RECEPTOR; PURINERGIC P2Y RECEPTOR; SAR 650984; UNCLASSIFIED DRUG;

EID: 84904383737     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00237     Document Type: Article
Times cited : (35)

References (210)
  • 1
    • 39049102137 scopus 로고    scopus 로고
    • Nerve growth factor is a potential therapeutic target in breast cancer
    • doi: 10.1158/0008-5472.CAN-07-1183
    • Adriaenssens, E., Vanhecke, E., Saule, P., Mougel, A., Page, A., Romon, R., et al. (2008). Nerve growth factor is a potential therapeutic target in breast cancer. Cancer Res. 68, 346-351. doi: 10.1158/0008-5472.CAN-07-1183
    • (2008) Cancer Res , vol.68 , pp. 346-351
    • Adriaenssens, E.1    Vanhecke, E.2    Saule, P.3    Mougel, A.4    Page, A.5    Romon, R.6
  • 2
    • 84855943692 scopus 로고    scopus 로고
    • Quantitative validation of GJC1 promoter hypermethylation in benign and malignant colorectal tumors
    • doi: 10.1530/ERC-11-0204
    • Ahmed, D., Lothe, R. A., Rivedal, E., and Lind, G. E. (2011). Quantitative validation of GJC1 promoter hypermethylation in benign and malignant colorectal tumors. Endocr. Relat. Cancer 18, C31-C34. doi: 10.1530/ERC-11-0204
    • (2011) Endocr. Relat. Cancer , vol.18
    • Ahmed, D.1    Lothe, R.A.2    Rivedal, E.3    Lind, G.E.4
  • 3
    • 79952751773 scopus 로고    scopus 로고
    • MiR-218 suppresses nasopharyngeal cancer progression through downregulation of survivin and the SLIT2-ROBO1 pathway
    • doi: 10.1158/0008-5472.CAN-10-2754
    • Alajez, N. M., Lenarduzzi, M., Ito, E., Hui, A. B., Shi, W., Bruce, J., et al. (2011). MiR-218 suppresses nasopharyngeal cancer progression through downregulation of survivin and the SLIT2-ROBO1 pathway. Cancer Res. 71, 2381-2391. doi: 10.1158/0008-5472.CAN-10-2754
    • (2011) Cancer Res , vol.71 , pp. 2381-2391
    • Alajez, N.M.1    Lenarduzzi, M.2    Ito, E.3    Hui, A.B.4    Shi, W.5    Bruce, J.6
  • 4
    • 84878614399 scopus 로고    scopus 로고
    • CD39 and CD73 in immunity and inflammation
    • doi: 10.1016/j.molmed.2013.03.005
    • Antonioli, L., Pacher, P., Vizi, E. S., and Haskó, G. (2013). CD39 and CD73 in immunity and inflammation. Trends Mol. Med. 19, 355-367. doi: 10.1016/j.molmed.2013.03.005
    • (2013) Trends Mol. Med. , vol.19 , pp. 355-367
    • Antonioli, L.1    Pacher, P.2    Vizi, E.S.3    Haskó, G.4
  • 5
    • 0037162496 scopus 로고    scopus 로고
    • Intercellular calcium signaling mediated by point-source burst release of ATP. Proc. Natl
    • doi: 10.1073/pnas.152588599
    • Arcuino, G., Lin, J. H., Takano, T., Liu, C., Jiang, L., Gao, Q., et al. (2002). Intercellular calcium signaling mediated by point-source burst release of ATP. Proc. Natl. Acad. Sci. U.S.A. 99, 9840-9845. doi: 10.1073/pnas.152588599
    • (2002) Acad. Sci. U.S.A. , vol.99 , pp. 9840-9845
    • Arcuino, G.1    Lin, J.H.2    Takano, T.3    Liu, C.4    Jiang, L.5    Gao, Q.6
  • 6
    • 84890313522 scopus 로고    scopus 로고
    • Exosomes in cancer development, metastasis, and drug resistance: a comprehensive review
    • doi: 10.1007/s10555-013-9441-9
    • Azmi, A. S., Bao, B., and Sarkar, F. H. (2013). Exosomes in cancer development, metastasis, and drug resistance: a comprehensive review. Cancer Metastasis Rev. 32, 623-642. doi: 10.1007/s10555-013-9441-9
    • (2013) Cancer Metastasis Rev , vol.32 , pp. 623-642
    • Azmi, A.S.1    Bao, B.2    Sarkar, F.H.3
  • 7
    • 28444432330 scopus 로고    scopus 로고
    • Endogenous hemichannels play a role in the release of ATP from Xenopus oocytes
    • doi: 10.1002/jcp.20440
    • Bahima, L., Aleu, J., Elias, M., Martín-Satué, M., Muhaisen, A., Blasi, J., et al. (2006). Endogenous hemichannels play a role in the release of ATP from Xenopus oocytes. J. Cell. Physiol. 206, 95-102. doi: 10.1002/jcp.20440
    • (2006) J. Cell. Physiol. , vol.206 , pp. 95-102
    • Bahima, L.1    Aleu, J.2    Elias, M.3    Martín-Satué, M.4    Muhaisen, A.5    Blasi, J.6
  • 8
    • 84858049750 scopus 로고    scopus 로고
    • Pannexin1 drives multicellular aggregate compaction via a signaling cascade that remodels the actin cytoskeleton
    • doi: 10.1074/jbc.M111.306522
    • Bao, B. A., Lai, C. P., Naus, C. C., and Morgan, J. R. (2012). Pannexin1 drives multicellular aggregate compaction via a signaling cascade that remodels the actin cytoskeleton. J. Biol. Chem. 287, 8407-8016. doi: 10.1074/jbc.M111.306522
    • (2012) J. Biol. Chem. , vol.287 , pp. 8016-8407
    • Bao, B.A.1    Lai, C.P.2    Naus, C.C.3    Morgan, J.R.4
  • 9
    • 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
  • 10
    • 12144288999 scopus 로고    scopus 로고
    • The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins
    • doi: 10.1016/j.ygeno.2003.09.025
    • Baranova, A., Ivanov, D., Petrash, N., Pestova, A., Skoblov, M., Kelmanson, I., et al. (2004). The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins. Genomics 83, 706-716. doi: 10.1016/j.ygeno.2003.09.025
    • (2004) Genomics , vol.83 , pp. 706-716
    • Baranova, A.1    Ivanov, D.2    Petrash, N.3    Pestova, A.4    Skoblov, M.5    Kelmanson, I.6
  • 11
    • 84870055576 scopus 로고    scopus 로고
    • The participation of plasma membrane hemichannels to purinergic signaling
    • doi: 10.1016/j.bbamem.2012.01.002
    • Baroja-Mazo, A., Barberà-Cremades, M., and Pelegrín, P. (2013). The participation of plasma membrane hemichannels to purinergic signaling. Biochim. Biophys. Acta 1828, 79-93. doi: 10.1016/j.bbamem.2012.01.002
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 79-93
    • Baroja-Mazo, A.1    Barberà-Cremades, M.2    Pelegrín, P.3
  • 13
    • 33746358536 scopus 로고    scopus 로고
    • Enhanced neurite outgrowth in PC12 cells mediated by connexin hemichannels and ATP
    • doi: 10.1074/jbc.M600026200
    • Belliveau, D. J., Bani-Yaghoub, M., McGirr, B., Naus, C. C., and Rushlow, W. J. (2006). Enhanced neurite outgrowth in PC12 cells mediated by connexin hemichannels and ATP. J. Biol. Chem. 281, 20920-20931. doi: 10.1074/jbc.M600026200
    • (2006) J. Biol. Chem. , vol.281 , pp. 20920-20931
    • Belliveau, D.J.1    Bani-Yaghoub, M.2    McGirr, B.3    Naus, C.C.4    Rushlow, W.J.5
  • 14
    • 0038125598 scopus 로고    scopus 로고
    • Calcium signalling: dynamics, homeostasis and remodelling
    • doi: 10.1038/nrm1155
    • Berridge, M. J., Bootman, M. D., and Roderick, H. L. (2003). Calcium signalling: dynamics, homeostasis and remodelling. Nat. Rev. Mol. Cell Biol. 4, 517-529. doi: 10.1038/nrm1155
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 517-529
    • Berridge, M.J.1    Bootman, M.D.2    Roderick, H.L.3
  • 15
    • 42649085323 scopus 로고    scopus 로고
    • Trafficking dynamics of glycosylated pannexin 1 proteins. Cell Commun
    • doi: 10.1080/15419060802013885
    • Boassa, D., Qiu, F., Dahl, G., and Sosinsky, G. (2008). Trafficking dynamics of glycosylated pannexin 1 proteins. Cell Commun. Adhes. 15, 119-132. doi: 10.1080/15419060802013885
    • (2008) Adhes , vol.15 , pp. 119-132
    • Boassa, D.1    Qiu, F.2    Dahl, G.3    Sosinsky, G.4
  • 18
    • 0037285683 scopus 로고    scopus 로고
    • Photoliberating inositol-1,4,5-trisphosphate triggers ATP release that is blocked by the connexin mimetic peptide gap 26
    • doi:10.1016/S0143-4160(02)
    • Braet, K., Vandamme, W., Martin, P. E., Evans, W. H., and Leybaert, L. (2003b). Photoliberating inositol-1,4,5-trisphosphate triggers ATP release that is blocked by the connexin mimetic peptide gap 26. Cell Calcium 33, 37-48. doi: 10.1016/S0143-4160(02)00180-X
    • (2003) Cell Calcium , vol.33 , pp. 37-48
    • Braet, K.1    Vandamme, W.2    Martin, P.E.3    Evans, W.H.4    Leybaert, L.5
  • 19
    • 58149099301 scopus 로고    scopus 로고
    • Connexins in vascular physiology and pathology
    • doi: 10.1089/ars.2008.2115
    • Brisset, A. C., Isakson, B. E., and Kwak, B. R. (2009). Connexins in vascular physiology and pathology. Antioxid. Redox Signal. 11, 267-282. doi: 10.1089/ars.2008.2115
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 267-282
    • Brisset, A.C.1    Isakson, B.E.2    Kwak, B.R.3
  • 20
    • 0345255097 scopus 로고    scopus 로고
    • Pannexins, a family of gap junction proteins expressed in brain. Proc
    • 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) 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
  • 21
    • 0035235938 scopus 로고    scopus 로고
    • Connexin 43 hemi channels 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 hemi channels 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
  • 22
    • 79959191760 scopus 로고    scopus 로고
    • Connexin 43 is a potential prognostic biomarker for ewing sarcoma/primitive neuroectodermal tumor
    • doi: 10.1155/2011/971050 2011
    • Bui, M. M., Han, G., Acs, G., Reed, D., Gonzalez, R. J., Pasha, T. L., et al. (2011). Connexin 43 is a potential prognostic biomarker for ewing sarcoma/primitive neuroectodermal tumor. Sarcoma 2011:971050. doi: 10.1155/2011/971050
    • (2011) Sarcoma , pp. 971050
    • Bui, M.M.1    Han, G.2    Acs, G.3    Reed, D.4    Gonzalez, R.J.5    Pasha, T.L.6
  • 23
    • 84888377850 scopus 로고    scopus 로고
    • Purinergic signalling and cancer
    • doi: 10.1007/s11302-013-9372-5
    • Burnstock, G., and Di Virgilio, F. (2013). Purinergic signalling and cancer. Purinergic Signal. 9, 491-540. doi: 10.1007/s11302-013-9372-5
    • (2013) Purinergic Signal , vol.9 , pp. 491-540
    • Burnstock, G.1    Di Virgilio, F.2
  • 24
    • 57349120207 scopus 로고    scopus 로고
    • Connexin 37 profoundly slows cell cycle progression in rat insulinoma cells. Am. J. Physiol
    • doi: 10.1152/ajpcell.299.2008
    • Burt, J. M., Nelson, T. K., Simon, A. M., and Fang, J. S. (2008). Connexin 37 profoundly slows cell cycle progression in rat insulinoma cells. Am. J. Physiol. Cell Physiol. 295, C1103-C1112. doi: 10.1152/ajpcell.299.2008
    • (2008) Cell Physiol , vol.295
    • Burt, J.M.1    Nelson, T.K.2    Simon, A.M.3    Fang, J.S.4
  • 25
    • 71749095578 scopus 로고    scopus 로고
    • ATP released by electrical stimuli elicits calcium transients and gene expression in skeletal muscle
    • doi: 10.1074/jbc.M109.057315
    • Buvinic, S., Almarza, G., Bustamante, M., Casas, M., López, J., Riquelme, M., et al. (2009). ATP released by electrical stimuli elicits calcium transients and gene expression in skeletal muscle. J. Biol. Chem. 284, 34490-34505. doi: 10.1074/jbc.M109.057315
    • (2009) J. Biol. Chem. , vol.284 , pp. 34490-34505
    • Buvinic, S.1    Almarza, G.2    Bustamante, M.3    Casas, M.4    López, J.5    Riquelme, M.6
  • 26
    • 84899423972 scopus 로고    scopus 로고
    • Connexin a check-point component of cell apoptosis in normal and physiopathological conditions
    • doi: 10.1016/j.biochi.2013.11.015
    • Carette, D., Gilleron, J., Chevallier, D., Segretain, D., and Pointis, G. (2014). Connexin a check-point component of cell apoptosis in normal and physiopathological conditions. Biochimie 101, 1-9. doi: 10.1016/j.biochi.2013.11.015
    • (2014) Biochimie , vol.101 , pp. 1-9
    • Carette, D.1    Gilleron, J.2    Chevallier, D.3    Segretain, D.4    Pointis, G.5
  • 27
    • 77951148608 scopus 로고    scopus 로고
    • Implications of pannexin 1 and pannexin 3 for keratinocyte differentiation
    • doi: 10.1242/jcs.056093
    • Celetti, S. J., Cowan, K. N., Penuela, S., Shao, Q., Churko, J., and Laird, D. W. (2010). Implications of pannexin 1 and pannexin 3 for keratinocyte differentiation. J. Cell Sci. 123(Pt 8), 1363-1372. doi: 10.1242/jcs.056093
    • (2010) J. Cell Sci. , vol.123 , Issue.PART 8 , pp. 1363-1372
    • Celetti, S.J.1    Cowan, K.N.2    Penuela, S.3    Shao, Q.4    Churko, J.5    Laird, D.W.6
  • 28
    • 77957942834 scopus 로고    scopus 로고
    • Pannexin 1 channels mediate "find-me" signal release and membrane permeability during apoptosis
    • doi:10.1038/nature09413
    • Chekeni, F. B., Elliott, M. R., Sandilos, J. K., Walk, S. F., Kinchen, J. M., Lazarowski, E. R., et al. (2010). Pannexin 1 channels mediate "find-me" signal release and membrane permeability during apoptosis. Nature 467, 863-867. doi: 10.1038/nature09413
    • (2010) Nature , vol.467 , pp. 863-867
    • Chekeni, F.B.1    Elliott, M.R.2    Sandilos, J.K.3    Walk, S.F.4    Kinchen, J.M.5    Lazarowski, E.R.6
  • 29
    • 0141566688 scopus 로고    scopus 로고
    • The correlation between aberrant connexin 43 mRNA expression induced by promoter methylation and nodal micrometastasis in non-small cell lung cancer
    • Chen, J. T., Cheng, Y. W., Chou, M. C., Sen-Lin, T., Lai, W. W., Ho, W. L., et al. (2003). The correlation between aberrant connexin 43 mRNA expression induced by promoter methylation and nodal micrometastasis in non-small cell lung cancer. Clin. Cancer Res. 9, 4200-4204.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 4200-4204
    • Chen, J.T.1    Cheng, Y.W.2    Chou, M.C.3    Sen-Lin, T.4    Lai, W.W.5    Ho, W.L.6
  • 30
    • 8644227780 scopus 로고    scopus 로고
    • Downregulation of connexin 26 in human lung cancer is related to promoter methylation
    • doi: 10.1002/ijc.20498
    • Chen, Y., Hühn, D., Knösel, T., Pacyna-Gengelbach, M., Deutschmann, N., and Petersen, I. (2005). Downregulation of connexin 26 in human lung cancer is related to promoter methylation. Int. J. Cancer 113, 14-21. doi: 10.1002/ijc.20498
    • (2005) Int. J. Cancer , vol.3 , pp. 14-21
    • Chen, Y.1    Hühn, D.2    Knösel, T.3    Pacyna-Gengelbach, M.4    Deutschmann, N.5    Petersen, I.6
  • 31
    • 84876098016 scopus 로고    scopus 로고
    • Remodeling of calcium signaling in tumor progression
    • doi: 10.1186/1423-0127-20-23
    • Chen, Y. F., Chen, Y. T., Chiu, W. T., and Shen, M. R. (2013). Remodeling of calcium signaling in tumor progression. J. Biomed. Sci. 20:23. doi: 10.1186/1423-0127-20-23
    • (2013) J. Biomed. Sci. , vol.20 , pp. 23
    • Chen, Y.F.1    Chen, Y.T.2    Chiu, W.T.3    Shen, M.R.4
  • 32
    • 84867877340 scopus 로고    scopus 로고
    • The NAD metabolome-a key determinant of cancer cell biology
    • doi: 10.1038/nrc3340
    • Chiarugi, A., Dölle, C., Felici, R., and Ziegler, M. (2012). The NAD metabolome-a key determinant of cancer cell biology. Nat. Rev. Cancer 12, 741-752. doi: 10.1038/nrc3340
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 741-752
    • Chiarugi, A.1    Dölle, C.2    Felici, R.3    Ziegler, M.4
  • 33
    • 60349100794 scopus 로고    scopus 로고
    • ATP release by cardiac myocytes in a simulated ischaemia model: inhibition by a connexin mimetic and enhancement by an antiarrhythmic peptide
    • doi: 10.1016/j.ejphar.2008.12.005
    • Clarke, T. C., Williams, O. J., Martin, P. E., and Evans, W. H. (2009). ATP release by cardiac myocytes in a simulated ischaemia model: inhibition by a connexin mimetic and enhancement by an antiarrhythmic peptide. Eur. J. Pharmacol. 605, 9-14. doi: 10.1016/j.ejphar.2008.12.005
    • (2009) Eur. J. Pharmacol. , vol.605 , pp. 9-14
    • Clarke, T.C.1    Williams, O.J.2    Martin, P.E.3    Evans, W.H.4
  • 34
    • 84879258844 scopus 로고    scopus 로고
    • A comparative antibody analysis of pannexin1 expression in four rat brain regions reveals varying subcellular localizations
    • doi: 10.3389/fphar.2013.00006
    • Cone, A. C., Ambrosi, C., Scemes, E., Martone, M. E., and Sosinsky, G. E. (2013). A comparative antibody analysis of pannexin1 expression in four rat brain regions reveals varying subcellular localizations. Front. Pharmacol. 4:6. doi: 10.3389/fphar.2013.00006
    • (2013) Front. Pharmacol. , vol.4 , pp. 6
    • Cone, A.C.1    Ambrosi, C.2    Scemes, E.3    Martone, M.E.4    Sosinsky, G.E.5
  • 35
    • 9644302728 scopus 로고    scopus 로고
    • Role of connexin-based gap junction channels and hemichannels in ischemia-induced cell death in nervous tissue
    • doi: 10.1016/j.brainresrev.2004.08.002
    • Contreras, J. E., Sánchez, H. A., Véliz, L. P., Bukauskas, F. F., Bennett, M. V., and Sáez, J. C. (2004). Role of connexin-based gap junction channels and hemichannels in ischemia-induced cell death in nervous tissue. Brain Res. Brain Res. Rev. 47, 290-303. doi: 10.1016/j.brainresrev.2004.08.002
    • (2004) Brain Res. Brain Res. Rev. , vol.47 , pp. 290-303
    • Contreras, J.E.1    Sánchez, H.A.2    Véliz, L.P.3    Bukauskas, F.F.4    Bennett, M.V.5    Sáez, J.C.6
  • 36
    • 0036193874 scopus 로고    scopus 로고
    • Re: the sinoatrial node, connexin distribution patterns and specific immunodetection of connexin45
    • author reply 1046. doi: 10.1016/S0008-6363(01)00564-8
    • Coppen, S. R., Dupont, E., and Severs, N. J. (2002). Re: the sinoatrial node, connexin distribution patterns and specific immunodetection of connexin45. Cardiovasc. Res. 53, 1043-1045; author reply 1046. doi: 10.1016/S0008-6363(01)00564-8
    • (2002) Cardiovasc. Res. , vol.53 , pp. 1043-1045
    • Coppen, S.R.1    Dupont, E.2    Severs, N.J.3
  • 38
    • 58149104029 scopus 로고    scopus 로고
    • Gap junctions and cancer: new functions for an old story
    • doi: 10.1089/ars.2008.2153
    • Cronier, L., Crespin, S., Strale, P. O., Defamie, N., and Mesnil, M. (2009). Gap junctions and cancer: new functions for an old story. Antioxid. Redox Signal. 11, 323-338. doi: 10.1089/ars.2008.2153
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 323-338
    • Cronier, L.1    Crespin, S.2    Strale, P.O.3    Defamie, N.4    Mesnil, M.5
  • 39
    • 42749090959 scopus 로고    scopus 로고
    • CD38 at the junction between prognostic marker and therapeutic target
    • doi: 10.1016/j.molmed.2008.02.005
    • Deaglio, S., Aydin, S., Vaisitti, T., Bergui, L., and Malavasi, F. (2008). CD38 at the junction between prognostic marker and therapeutic target. Trends Mol. Med. 14, 210-218. doi: 10.1016/j.molmed.2008.02.005
    • (2008) Trends Mol. Med. , vol.14 , pp. 210-218
    • Deaglio, S.1    Aydin, S.2    Vaisitti, T.3    Bergui, L.4    Malavasi, F.5
  • 40
    • 80052640514 scopus 로고    scopus 로고
    • Calcium and connexin-based intercellular communication, a deadly catch?
    • doi: 10.1016/j.ceca.2011.05.007
    • Decrock, E., Vinken, M., Bol, M., D'Herde, K., Rogiers, V., Vandenabeele, P., et al. (2011). Calcium and connexin-based intercellular communication, a deadly catch? Cell Calcium 50, 310-321. doi: 10.1016/j.ceca.2011.05.007
    • (2011) Cell Calcium , vol.50 , pp. 310-321
    • Decrock, E.1    Vinken, M.2    Bol, M.3    D'Herde, K.4    Rogiers, V.5    Vandenabeele, P.6
  • 41
    • 14944349319 scopus 로고    scopus 로고
    • Autocrine and paracrine calcium signaling by the CD38/NAD+/cyclic ADP-ribose system
    • doi: 10.1196/annals.1322.021
    • De Flora, A., Zocchi, E., Guida, L., Franco, L., and Bruzzone, S. (2004). Autocrine and paracrine calcium signaling by the CD38/NAD+/cyclic ADP-ribose system. Ann. N.Y. Acad. Sci. 1028, 176-191. doi: 10.1196/annals.1322.021
    • (2004) Ann. N. Y. Acad. Sci. , vol.1028 , pp. 176-191
    • De Flora, A.1    Zocchi, E.2    Guida, L.3    Franco, L.4    Bruzzone, S.5
  • 42
    • 30444459027 scopus 로고    scopus 로고
    • Intracellular calcium changes trigger connexin 32 hemichannel opening
    • doi: 10.1038/sj.emboj.7600908
    • De Vuyst, E., Decrock, E., Cabooter, L., Dubyak, G. R., Naus, C. C., Evans, W. H., et al. (2006). Intracellular calcium changes trigger connexin 32 hemichannel opening. EMBO J. 25, 34-44. doi: 10.1038/sj.emboj.7600908
    • (2006) EMBO J , vol.25 , pp. 34-44
    • De Vuyst, E.1    Decrock, E.2    Cabooter, L.3    Dubyak, G.R.4    Naus, C.C.5    Evans, W.H.6
  • 43
    • 33846100604 scopus 로고    scopus 로고
    • Connexin hemichannels and gap junction channels are differentially influenced by lipopolysaccharide and basic fibroblast growth factor
    • doi: 10.1091/mbc.E06-03-0182
    • De Vuyst, E., Decrock, E., De Bock, M., Yamasaki, H., Naus, C. C., Evans, W. H., et al. (2007). Connexin hemichannels and gap junction channels are differentially influenced by lipopolysaccharide and basic fibroblast growth factor. Mol. Biol. Cell. 18, 34-46. doi: 10.1091/mbc.E06-03-0182
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 34-46
    • De Vuyst, E.1    Decrock, E.2    De Bock, M.3    Yamasaki, H.4    Naus, C.C.5    Evans, W.H.6
  • 44
    • 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
  • 45
    • 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
  • 46
    • 84876048479 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor inhibitors as a cancer treatment: from a biologic rationale to medical perspectives
    • doi: 10.1158/2159-8290.CD-12-0362
    • Dieci, M. V., Arnedos, M., Andre, F., and Soria, J. C. (2013). Fibroblast growth factor receptor inhibitors as a cancer treatment: from a biologic rationale to medical perspectives. Cancer Discov. 3, 264-279. doi: 10.1158/2159-8290.CD-12-0362
    • (2013) Cancer Discov , vol.3 , pp. 264-279
    • Dieci, M.V.1    Arnedos, M.2    Andre, F.3    Soria, J.C.4
  • 47
    • 84896691579 scopus 로고    scopus 로고
    • Genomic aberrations in the FGFR pathway: opportunities for targeted therapies in solid tumors
    • doi: 10.1093/annonc/mdt419
    • Dienstmann, R., Rodon, J., Prat, A., Perez-Garcia, J., Adamo, B., Felip, E., et al. (2014). Genomic aberrations in the FGFR pathway: opportunities for targeted therapies in solid tumors. Ann. Oncol. 25, 552-563. doi: 10.1093/annonc/mdt419
    • (2014) Ann. Oncol. , vol.25 , pp. 552-563
    • Dienstmann, R.1    Rodon, J.2    Prat, A.3    Perez-Garcia, J.4    Adamo, B.5    Felip, E.6
  • 48
    • 84868248487 scopus 로고    scopus 로고
    • Purines, purinergic receptors, and cancer
    • doi: 10.1158/0008-5472.CAN-12-1600
    • Di Virgilio, F. (2012). Purines, purinergic receptors, and cancer. Cancer Res. 72, 5441-5447. doi: 10.1158/0008-5472.CAN-12-1600
    • (2012) Cancer Res , vol.72 , pp. 5441-5447
    • Di Virgilio, F.1
  • 50
    • 84869179175 scopus 로고    scopus 로고
    • Cardiomyocyte ATP release through pannexin 1 aids in early fibroblast activation
    • doi: 10.1152/ajpheart.00251.2012
    • Dolmatova, E., Spagnol, G., Boassa, D., Baum, J. R., Keith, K., Ambrosi, C., et al. (2012). Cardiomyocyte ATP release through pannexin 1 aids in early fibroblast activation. Am. J. Physiol. Heart Circ. Physiol. 303, H1208-H1218. doi: 10.1152/ajpheart.00251.2012
    • (2012) Am. J. Physiol. Heart Circ. Physiol. , vol.303
    • Dolmatova, E.1    Spagnol, G.2    Boassa, D.3    Baum, J.R.4    Keith, K.5    Ambrosi, C.6
  • 51
    • 84878860621 scopus 로고    scopus 로고
    • Thrombocytosis and immunohistochemical expression of connexin 43 at diagnosis predict survival in advanced non-small-cell lung cancer treated with cisplatin-based chemotherapy
    • doi: 10.1007/s00280-013-2080-6
    • Du, G., Yang, Y., Zhang, Y., Sun, T., Liu, W., Wang, Y., et al. (2013). Thrombocytosis and immunohistochemical expression of connexin 43 at diagnosis predict survival in advanced non-small-cell lung cancer treated with cisplatin-based chemotherapy. Cancer Chemother. Pharmacol. 71, 893-904. doi: 10.1007/s00280-013-2080-6
    • (2013) Cancer Chemother. Pharmacol. , vol.71 , pp. 893-904
    • Du, G.1    Yang, Y.2    Zhang, Y.3    Sun, T.4    Liu, W.5    Wang, Y.6
  • 52
    • 0037173718 scopus 로고    scopus 로고
    • Connexin 43, but not connexin 32, is mutated at advanced stages of human sporadic colon cancer
    • doi: 10.1038/sj.onc.1205630
    • Dubina, M. V., Iatckii, N. A., Popov, D. E., Vasil'ev, S. V., and Krutovskikh, V. A. (2002). Connexin 43, but not connexin 32, is mutated at advanced stages of human sporadic colon cancer. Oncogene 21, 4992-4996. doi: 10.1038/sj.onc.1205630
    • (2002) Oncogene , vol.21 , pp. 4992-4996
    • Dubina, M.V.1    Iatckii, N.A.2    Popov, D.E.3    Vasil'ev, S.V.4    Krutovskikh, V.A.5
  • 53
    • 33750929739 scopus 로고    scopus 로고
    • ATP release from activated neutrophils occurs via connexin 43 and modulates adenosine-dependent endothelial cell function
    • doi: 10.1161/01.RES.0000250174.31269.70
    • Eltzschig, H. K., Eckle, T., Mager, A., Küper, N., Karcher, C., Weissmüller, T., et al. (2006). ATP release from activated neutrophils occurs via connexin 43 and modulates adenosine-dependent endothelial cell function. Circ. Res. 99, 1100-1108. doi: 10.1161/01.RES.0000250174.31269.70
    • (2006) Circ. Res. , vol.99 , pp. 1100-1108
    • Eltzschig, H.K.1    Eckle, T.2    Mager, A.3    Küper, N.4    Karcher, C.5    Weissmüller, T.6
  • 54
    • 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
  • 55
    • 33745528139 scopus 로고    scopus 로고
    • The gap junction cellular internet: connexin hemichannels enter the signalling limelight
    • doi: 10.1042/BJ20060175
    • Evans, W. H., De Vuyst, E., and Leybaert, L. (2006). The gap junction cellular internet: connexin hemichannels enter the signalling limelight. Biochem J. 397, 1-14. doi: 10.1042/BJ20060175
    • (2006) Biochem J , vol.397 , pp. 1-14
    • Evans, W.H.1    De Vuyst, E.2    Leybaert, L.3
  • 56
    • 50949116679 scopus 로고    scopus 로고
    • ATP release from vascular endothelia occurs across Cx43 hemichannels and is attenuated during hypoxia
    • doi: 10.1371/journal.pone.0002801
    • Faigle, M., Seessle, J., Zug, S., El Kasmi, K. C., and Eltzschig, H. K. (2008). ATP release from vascular endothelia occurs across Cx43 hemichannels and is attenuated during hypoxia. PLoS ONE 3:e2801. doi: 10.1371/journal.pone.0002801
    • (2008) PLoS ONE , vol.3
    • Faigle, M.1    Seessle, J.2    Zug, S.3    El Kasmi, K.C.4    Eltzschig, H.K.5
  • 57
    • 84876558170 scopus 로고    scopus 로고
    • Detecting adenosine triphosphate in the pericellular space
    • doi: 10.1098/rsfs.2012.0101
    • Falzoni, S., Donvito, G., and Di Virgilio, F. (2013). Detecting adenosine triphosphate in the pericellular space. Interface Focus 3:20120101. doi: 10.1098/rsfs.2012.0101
    • (2013) Interface Focus , vol.3 , pp. 20120101
    • Falzoni, S.1    Donvito, G.2    Di Virgilio, F.3
  • 58
    • 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
  • 59
    • 0035877808 scopus 로고    scopus 로고
    • Paracrine roles of NAD+ and cyclic ADP-ribose in increasing intracellular calcium and enhancing cell proliferation of 3T3 fibroblasts
    • doi: 10.1074/jbc.M010536200
    • Franco, L., Zocchi, E., Usai, C., Guida, L., Bruzzone, S., Costa, A., et al. (2001). Paracrine roles of NAD+ and cyclic ADP-ribose in increasing intracellular calcium and enhancing cell proliferation of 3T3 fibroblasts. J. Biol. Chem. 276, 21642-21648. doi: 10.1074/jbc.M010536200
    • (2001) J. Biol. Chem. , vol.276 , pp. 21642-21648
    • Franco, L.1    Zocchi, E.2    Usai, C.3    Guida, L.4    Bruzzone, S.5    Costa, A.6
  • 60
    • 0037134035 scopus 로고    scopus 로고
    • Multicolor and electron microscopic imaging of connexin trafficking
    • doi: 10.1126/science.1068793
    • Gaietta, G., Deerinck, T. J., Adams, S. R., Bouwer, J., Tour, O., Laird, D. W., et al. (2002). Multicolor and electron microscopic imaging of connexin trafficking. Science 296, 503-507. doi: 10.1126/science.1068793
    • (2002) Science , vol.296 , pp. 503-507
    • Gaietta, G.1    Deerinck, T.J.2    Adams, S.R.3    Bouwer, J.4    Tour, O.5    Laird, D.W.6
  • 61
    • 78651081496 scopus 로고    scopus 로고
    • FGF-1 induces ATP release from spinal astrocytes in culture and opens pannexin and connexin hemichannels
    • doi: 10.1073/pnas.1013793107
    • Garré, J. M., Retamal, M. A., Cassina, P., Barbeito, L., Bukauskas, F. F., Sáez, J. C., et al. (2010). FGF-1 induces ATP release from spinal astrocytes in culture and opens pannexin and connexin hemichannels. Proc. Natl. Acad. Sci. U.S.A. 107, 22659-22664. doi: 10.1073/pnas.1013793107
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 22659-22664
    • Garré, J.M.1    Retamal, M.A.2    Cassina, P.3    Barbeito, L.4    Bukauskas, F.F.5    Sáez, J.C.6
  • 62
    • 84869078806 scopus 로고    scopus 로고
    • Production of adenosine by ectonucleotidases: a key factor in tumor immunoescape
    • doi: 10.1155/2012/473712
    • Ghiringhelli, F., Bruchard, M., Chalmin, F., and Rébé, C. (2012). Production of adenosine by ectonucleotidases: a key factor in tumor immunoescape. J. Biomed. Biotechnol. 2012:473712. doi: 10.1155/2012/473712
    • (2012) J. Biomed. Biotechnol. , vol.2012 , pp. 473712
    • Ghiringhelli, F.1    Bruchard, M.2    Chalmin, F.3    Rébé, C.4
  • 63
    • 84893411575 scopus 로고    scopus 로고
    • Connexin-43 regulates p38-mediated cell migration and invasion induced selectively in tumour cells by low doses of γ-radiation in an ERK-1/2-independent manner
    • doi: 10.1093/carcin/bgt303
    • Ghosh, S., Kumar, A., Tripathi, R. P., and Chandna, S. (2014). Connexin-43 regulates p38-mediated cell migration and invasion induced selectively in tumour cells by low doses of γ-radiation in an ERK-1/2-independent manner. Carcinogenesis 35, 383-395. doi: 10.1093/carcin/bgt303
    • (2014) Carcinogenesis , vol.35 , pp. 383-395
    • Ghosh, S.1    Kumar, A.2    Tripathi, R.P.3    Chandna, S.4
  • 64
    • 77952426247 scopus 로고    scopus 로고
    • Pharmacological and genetic approaches to study connexin-mediated channels in glial cells of the central nervous system
    • doi: 10.1016/j.brainresrev.2009.11.005
    • Giaume, C., and Theis, M. (2010). Pharmacological and genetic approaches to study connexin-mediated channels in glial cells of the central nervous system. Brain Res. Rev. 63, 160-176. doi: 10.1016/j.brainresrev.2009.11.005
    • (2010) Brain Res. Rev. , vol.63 , pp. 160-176
    • Giaume, C.1    Theis, M.2
  • 65
    • 18244365858 scopus 로고    scopus 로고
    • ATP release through connexin hemichannels in corneal endothelial cells. Invest. Ophthalmol
    • doi: 10.1167/iovs.04-1181
    • Gomes, P., Srinivas, S. P., Van Driessche, W., Vereecke, J., and Himpens, B. (2005). ATP release through connexin hemichannels in corneal endothelial cells. Invest. Ophthalmol. Vis. Sci. 46, 1208-1218. doi: 10.1167/iovs.04-1181
    • (2005) Vis. Sci. , vol.46 , pp. 1208-1218
    • Gomes, P.1    Srinivas, S.P.2    Van Driessche, W.3    Vereecke, J.4    Himpens, B.5
  • 66
    • 84866046899 scopus 로고    scopus 로고
    • Extracellular loop cysteine mutant of cx37 fails to suppress proliferation of rat insulinoma cells
    • doi: 10.1007/s00232-012-9459-x
    • Good, M. E., Ek-Vitorín, J. F., and Burt, J. M. (2012). Extracellular loop cysteine mutant of cx37 fails to suppress proliferation of rat insulinoma cells. J. Membr. Biol. 245, 369-380. doi: 10.1007/s00232-012-9459-x
    • (2012) J. Membr. Biol. , vol.245 , pp. 369-380
    • Good, M.E.1    Ek-Vitorín, J.F.2    Burt, J.M.3
  • 67
    • 79960401710 scopus 로고    scopus 로고
    • A functional channel is necessary for growth suppression by Cx37
    • doi: 10.1242/jcs.081695
    • Good, M. E., Nelson, T. K., Simon, A. M., and Burt, J. M. (2011). A functional channel is necessary for growth suppression by Cx37. J. Cell Sci. 124(Pt 14), 2448-2456. doi: 10.1242/jcs.081695
    • (2011) J. Cell Sci. , vol.124 , Issue.PART 14 , pp. 2448-2456
    • Good, M.E.1    Nelson, T.K.2    Simon, A.M.3    Burt, J.M.4
  • 68
    • 0037382614 scopus 로고    scopus 로고
    • Beyond the gap: functions of unpaired connexon channels
    • doi: 10.1038/nrm1072
    • Goodenough, D. A., and Paul, D. L. (2003). Beyond the gap: functions of unpaired connexon channels. Nat. Rev. Mol. Cell Biol. 4, 285-294. doi: 10.1038/nrm1072
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 285-294
    • Goodenough, D.A.1    Paul, D.L.2
  • 69
    • 58149335240 scopus 로고    scopus 로고
    • Hemichannel-mediated inositol 1,4,5-trisphosphate (IP3) release in the cochlea: a novel mechanism of IP3 intercellular signaling
    • doi: 10.1080/15419060802357217
    • Gossman, D. G., and Zhao, H. B. (2008). Hemichannel-mediated inositol 1,4,5-trisphosphate (IP3) release in the cochlea: a novel mechanism of IP3 intercellular signaling. Cell Commun. Adhes. 15, 305-315. doi: 10.1080/15419060802357217
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 305-315
    • Gossman, D.G.1    Zhao, H.B.2
  • 70
    • 84863287433 scopus 로고    scopus 로고
    • miR-221/222 is the regulator of Cx43 expression in human glioblastoma cells
    • doi: 10.3892/or.2012.1652
    • Hao, J., Zhang, C., Zhang, A., Wang, K., Jia, Z., Wang, G., et al. (2012). miR-221/222 is the regulator of Cx43 expression in human glioblastoma cells. Oncol. Rep. 27, 1504-1510. doi: 10.3892/or.2012.1652
    • (2012) Oncol. Rep. , vol.27 , pp. 1504-1510
    • Hao, J.1    Zhang, C.2    Zhang, A.3    Wang, K.4    Jia, Z.5    Wang, G.6
  • 71
    • 84893769896 scopus 로고    scopus 로고
    • MicroRNAs and long non-coding RNAs: prospects in diagnostics and therapy of cancer
    • doi: 10.2478/raon-2013-0062
    • Hauptman, N., and Glavac, D. (2013). MicroRNAs and long non-coding RNAs: prospects in diagnostics and therapy of cancer. Radiol. Oncol. 47, 311-318. doi: 10.2478/raon-2013-0062
    • (2013) Radiol. Oncol. , vol.47 , pp. 311-318
    • Hauptman, N.1    Glavac, D.2
  • 72
    • 33746794230 scopus 로고    scopus 로고
    • A histone deacetylation-dependent mechanism for transcriptional repression of the gap junction gene cx43 in prostate cancer cells
    • doi: 10.1002/pros.20451
    • Hernandez, M., Shao, Q., Yang, X. J., Luh, S. P., Kandouz, M., Batist, G., et al. (2006). A histone deacetylation-dependent mechanism for transcriptional repression of the gap junction gene cx43 in prostate cancer cells. Prostate 66, 1151-1161. doi: 10.1002/pros.20451
    • (2006) Prostate , vol.66 , pp. 1151-1161
    • Hernandez, M.1    Shao, Q.2    Yang, X.J.3    Luh, S.P.4    Kandouz, M.5    Batist, G.6
  • 73
    • 0038693736 scopus 로고    scopus 로고
    • Down-regulation of connexin 32 gene expression through DNA methylation in a human renal cell carcinoma cell
    • doi: 10.1159/000070653
    • Hirai, A., Yano, T., Nishikawa, K., Suzuki, K., Asano, R., Satoh, H., et al. (2003). Down-regulation of connexin 32 gene expression through DNA methylation in a human renal cell carcinoma cell. Am. J. Nephrol. 23, 172-177. doi: 10.1159/000070653
    • (2003) Am. J. Nephrol. , vol.23 , pp. 172-177
    • Hirai, A.1    Yano, T.2    Nishikawa, K.3    Suzuki, K.4    Asano, R.5    Satoh, H.6
  • 74
    • 84863248130 scopus 로고    scopus 로고
    • Critical role of connexin 43 in secondary expansion of traumatic spinal cord injury
    • doi: 10.1523/JNEUROSCI.1216-11.2012
    • Huang, C., Han, X., Li, X., Lam, E., Peng, W., Lou, N., et al. (2012). Critical role of connexin 43 in secondary expansion of traumatic spinal cord injury. J. Neurosci. 32, 3333-3338. doi: 10.1523/JNEUROSCI.1216-11.2012
    • (2012) J. Neurosci. , vol.32 , pp. 3333-3338
    • Huang, C.1    Han, X.2    Li, X.3    Lam, E.4    Peng, W.5    Lou, N.6
  • 75
    • 34247631845 scopus 로고    scopus 로고
    • The role of pannexin 1 hemichannels in ATP release and cell-cell communication in mouse taste buds. Proc
    • doi: 10.1073/pnas.0611280104
    • Huang, Y. J., Maruyama, Y., Dvoryanchikov, G., Pereira, E., Chaudhari, N., and Roper, S. D. (2007). The role of pannexin 1 hemichannels in ATP release and cell-cell communication in mouse taste buds. Proc. Natl. Acad. Sci. U.S A. 104, 6436-6441. doi: 10.1073/pnas.0611280104
    • (2007) Natl. Acad. Sci. U.S A. , vol.104 , pp. 6436-6441
    • Huang, Y.J.1    Maruyama, Y.2    Dvoryanchikov, G.3    Pereira, E.4    Chaudhari, N.5    Roper, S.D.6
  • 76
    • 78649420520 scopus 로고    scopus 로고
    • Extracellular NAD+ shapes the Foxp3+ regulatory T cell compartment through the ART2-P2X7 pathway
    • doi: 10.1084/jem.20091154
    • Hubert, S., Rissiek, B., Klages, K., Huehn, J., Sparwasser, T., Haag, F., et al. (2010). Extracellular NAD+ shapes the Foxp3+ regulatory T cell compartment through the ART2-P2X7 pathway. J. Exp. Med. 207, 2561-2568. doi: 10.1084/jem.20091154
    • (2010) J. Exp. Med. , vol.207 , pp. 2561-2568
    • Hubert, S.1    Rissiek, B.2    Klages, K.3    Huehn, J.4    Sparwasser, T.5    Haag, F.6
  • 77
    • 84892990284 scopus 로고    scopus 로고
    • Cell-cell communication via extracellular membrane vesicles and its role in the immune response. Mol
    • doi: 10.1007/s10059-013-0154-2
    • Hwang, I. (2013). Cell-cell communication via extracellular membrane vesicles and its role in the immune response. Mol. Cells 36, 105-111. doi: 10.1007/s10059-013-0154-2
    • (2013) Cells , vol.36 , pp. 105-111
    • Hwang, I.1
  • 78
    • 66149173401 scopus 로고    scopus 로고
    • Pannexin 1: the molecular substrate of astrocyte hemichannels
    • doi: 10.1523/JNEUROSCI.6062-08.2009
    • Iglesias, R., Dahl, G., Qiu, F., Spray, D. C., Scemes, E., Iglesias, et al. (2009). Pannexin 1: the molecular substrate of astrocyte hemichannels. J. Neurosci. 29, 7092-7097. doi: 10.1523/JNEUROSCI.6062-08.2009
    • (2009) J. Neurosci. , vol.29 , pp. 7092-7097
    • Iglesias, R.1    Dahl, G.2    Qiu, F.3    Spray, D.C.4    Scemes, E.5    Iglesias, X.6
  • 79
    • 84862861555 scopus 로고    scopus 로고
    • Pannexin1-mediated ATP release provides signal transmission between Neuro2A cells
    • doi: 10.1007/s11064-012-0720-6
    • Iglesias, R. M., and Spray, D. C. (2012). Pannexin1-mediated ATP release provides signal transmission between Neuro2A cells. Neurochem. Res. 37, 1355-1363. doi: 10.1007/s11064-012-0720-6
    • (2012) Neurochem. Res. , vol.37 , pp. 1355-1363
    • Iglesias, R.M.1    Spray, D.C.2
  • 80
    • 77955071131 scopus 로고    scopus 로고
    • Connexin 43, E-cadherin, beta-catenin and ZO-1 expression, and aberrant methylation of the connexin 43 gene in NSCLC
    • Jinn, Y., and Inase, N. (2010). Connexin 43, E-cadherin, beta-catenin and ZO-1 expression, and aberrant methylation of the connexin 43 gene in NSCLC. Anticancer Res. 30, 2271-2278.
    • (2010) Anticancer Res , vol.30 , pp. 2271-2278
    • Jinn, Y.1    Inase, N.2
  • 81
    • 84872681814 scopus 로고    scopus 로고
    • Association between C1019T polymorphism in the connexin 37 gene and Helicobacter pylori infection in patients with gastric cancer
    • doi: 10.7314/APJCP.2012.13.5.2363
    • Jing, Y. M., Guo, S. X., Zhang, X. P., Sun, A. J., Tao, F., and Qian, H. X. (2012). Association between C1019T polymorphism in the connexin 37 gene and Helicobacter pylori infection in patients with gastric cancer. Asian Pac. J. Cancer Prev. 13, 2363-2367. doi: 10.7314/APJCP.2012.13.5.2363
    • (2012) Asian Pac. J. Cancer Prev. , vol.13 , pp. 2363-2367
    • Jing, Y.M.1    Guo, S.X.2    Zhang, X.P.3    Sun, A.J.4    Tao, F.5    Qian, H.X.6
  • 82
    • 84894294740 scopus 로고    scopus 로고
    • Exosomes: mediators of neurodegeneration, neuroprotection and therapeutics
    • doi: 10.1007/s12035-013-8544-1
    • Kalani, A., Tyagi, A., and Tyagi, N. (2014). Exosomes: mediators of neurodegeneration, neuroprotection and therapeutics. Mol. Neurobiol. 49, 590-600. doi: 10.1007/s12035-013-8544-1
    • (2014) Mol. Neurobiol. , vol.49 , pp. 590-600
    • Kalani, A.1    Tyagi, A.2    Tyagi, N.3
  • 83
    • 33645695606 scopus 로고    scopus 로고
    • Increased expression of connexins 26 and 43 in lymph node metastases of breast cancer
    • doi: 10.1136/jcp.2005.029272
    • Kanczuga-Koda, L., Sulkowski, S., Lenczewski, A., Koda, M., Wincewicz, A., Baltaziak, M., et al. (2006). Increased expression of connexins 26 and 43 in lymph node metastases of breast cancer. J. Clin. Pathol. 59, 429-433. doi: 10.1136/jcp.2005.029272
    • (2006) J. Clin. Pathol. , vol.59 , pp. 429-433
    • Kanczuga-Koda, L.1    Sulkowski, S.2    Lenczewski, A.3    Koda, M.4    Wincewicz, A.5    Baltaziak, M.6
  • 84
    • 77953585288 scopus 로고    scopus 로고
    • Gap junctions and connexins as therapeutic targets in cancer
    • doi: 10.1517/14728222.2010.487866
    • Kandouz, M., and Batist, G. (2010). Gap junctions and connexins as therapeutic targets in cancer. Expert Opin. Ther. Targets 14, 681-692. doi: 10.1517/14728222.2010.487866
    • (2010) Expert Opin. Ther. Targets , vol.14 , pp. 681-692
    • Kandouz, M.1    Batist, G.2
  • 85
    • 44649092806 scopus 로고    scopus 로고
    • Connexin 43 hemichannels are permeable to ATP
    • doi: 10.1523/JNEUROSCI.5048-07.2008
    • Kang, J., Kang, N., Lovatt, D., Torres, A., Zhao, Z., Lin, J., et al. (2008). Connexin 43 hemichannels are permeable to ATP. J. Neurosci. 28, 4702-4711. doi: 10.1523/JNEUROSCI.5048-07.2008
    • (2008) J. Neurosci. , vol.28 , pp. 4702-4711
    • Kang, J.1    Kang, N.2    Lovatt, D.3    Torres, A.4    Zhao, Z.5    Lin, J.6
  • 86
    • 0022344076 scopus 로고
    • Modulation of cell communication and carcinogenesis
    • doi: 10.2170/jjphysiol.35.693
    • Kanno, Y. (1985). Modulation of cell communication and carcinogenesis. Jpn. J. Physiol. 35, 693-707. doi: 10.2170/jjphysiol.35.693
    • (1985) Jpn. J. Physiol. , vol.35 , pp. 693-707
    • Kanno, Y.1
  • 87
    • 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
  • 88
    • 0030918234 scopus 로고    scopus 로고
    • Direct cell/cell communication in the lymphoid germinal center: connexin43 gap junctions functionally couple follicular dendritic cells to each other and to B lymphocytes
    • doi: 10.1002/eji.1830270627
    • Krenacs, T., van Dartel, M., Lindhout, E., and Rosendaal, M. (1997). Direct cell/cell communication in the lymphoid germinal center: connexin43 gap junctions functionally couple follicular dendritic cells to each other and to B lymphocytes. Eur. J. Immunol. 27, 1489-1497. doi: 10.1002/eji.1830270627
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1489-1497
    • Krenacs, T.1    van Dartel, M.2    Lindhout, E.3    Rosendaal, M.4
  • 89
    • 40249115335 scopus 로고    scopus 로고
    • Overexpression of connexin 26 in carcinoma of the pancreas
    • doi: 10.3892/or.19.3.627
    • Kyo, N., Yamamoto, H., Takeda, Y., Ezumi, K., Ngan, C. Y., Terayama, M., et al. (2008). Overexpression of connexin 26 in carcinoma of the pancreas. Oncol. Rep. 19, 627-631. doi: 10.3892/or.19.3.627
    • (2008) Oncol. Rep. , vol.19 , pp. 627-631
    • Kyo, N.1    Yamamoto, H.2    Takeda, Y.3    Ezumi, K.4    Ngan, C.Y.5    Terayama, M.6
  • 90
    • 72049084500 scopus 로고    scopus 로고
    • Pannexin2 as a novel growth regulator in C6 glioma cells
    • doi: 10.1038/onc.2009.283
    • Lai, C. P., Bechberger, J. F., and Naus, C. C. (2009). Pannexin2 as a novel growth regulator in C6 glioma cells. Oncogene 28, 4402-4408. doi: 10.1038/onc.2009.283
    • (2009) Oncogene , vol.28 , pp. 4402-4408
    • Lai, C.P.1    Bechberger, J.F.2    Naus, C.C.3
  • 91
    • 33847745727 scopus 로고    scopus 로고
    • Tumor-suppressive effects of pannexin 1 in C6 glioma cells
    • doi: 10.1158/0008-5472.CAN-06-1396
    • Lai, C. P., Bechberger, J. F., Thompson, R. J., MacVicar, B. A., Bruzzone, R., and Naus, C. C. (2007). Tumor-suppressive effects of pannexin 1 in C6 glioma cells. Cancer Res. 67, 1545-1554. doi: 10.1158/0008-5472.CAN-06-1396
    • (2007) Cancer Res , vol.67 , pp. 1545-1554
    • Lai, C.P.1    Bechberger, J.F.2    Thompson, R.J.3    MacVicar, B.A.4    Bruzzone, R.5    Naus, C.C.6
  • 92
    • 84857159720 scopus 로고    scopus 로고
    • The gap junction protein Cx43 is involved in the bone-targeted metastatic behaviour of human prostate cancer cells
    • doi: 10.1007/s10585-011-9434-4
    • Lamiche, C., Clarhaut, J., Strale, P. O., Crespin, S., Pedretti, N., Bernard, F. X., et al. (2012). The gap junction protein Cx43 is involved in the bone-targeted metastatic behaviour of human prostate cancer cells. Clin. Exp. Metastas. 29, 111-122. doi: 10.1007/s10585-011-9434-4
    • (2012) Clin. Exp. Metastas. , vol.29 , pp. 111-122
    • Lamiche, C.1    Clarhaut, J.2    Strale, P.O.3    Crespin, S.4    Pedretti, N.5    Bernard, F.X.6
  • 93
    • 80054887592 scopus 로고    scopus 로고
    • Ion channels and transporters in cancer. 4. Remodeling of Ca(2+) signaling in tumorigenesis: role of Ca(2+) transport
    • doi: 10.1152/ajpcell.00136.2011
    • Lee, J. M., Davis, F. M., Roberts-Thomson, S. J., and Monteith, G. R. (2011). Ion channels and transporters in cancer. 4. Remodeling of Ca(2+) signaling in tumorigenesis: role of Ca(2+) transport. Am. J. Physiol. Cell Physiol. 301, C969-C976. doi: 10.1152/ajpcell.00136.2011
    • (2011) Am. J. Physiol. Cell Physiol. , vol.301
    • Lee, J.M.1    Davis, F.M.2    Roberts-Thomson, S.J.3    Monteith, G.R.4
  • 94
    • 0025877670 scopus 로고
    • Positive selection of candidate tumor-suppressor genes by subtractive hybridization. Proc
    • doi: 10.1073/pnas.88.7.2825
    • Lee, S. W., Tomasetto, C., and Sager, R. (1991). Positive selection of candidate tumor-suppressor genes by subtractive hybridization. Proc. Natl. Acad. Sci. U.S.A. 88, 2825-2829. doi: 10.1073/pnas.88.7.2825
    • (1991) Natl. Acad. Sci. U.S.A. , vol.88 , pp. 2825-2829
    • Lee, S.W.1    Tomasetto, C.2    Sager, R.3
  • 95
    • 80054954153 scopus 로고    scopus 로고
    • Mechanisms of ATP release by human trabecular meshwork cells, the enabling step in purinergic regulation of aqueous humor outflow
    • doi: 10.1002/jcp.22715
    • Li, A., Leung, C. T., Peterson-Yantorno, K., Stamer, W. D., Mitchell, C. H., and Civan, M. M. (2012a). Mechanisms of ATP release by human trabecular meshwork cells, the enabling step in purinergic regulation of aqueous humor outflow. J. Cell Physiol. 227, 172-182. doi: 10.1002/jcp.22715
    • (2012) J. Cell Physiol. , vol.227 , pp. 172-182
    • Li, A.1    Leung, C.T.2    Peterson-Yantorno, K.3    Stamer, W.D.4    Mitchell, C.H.5    Civan, M.M.6
  • 96
    • 0035693047 scopus 로고    scopus 로고
    • Activation of connexin-43 hemichannels can elevate [Ca(2+)]i and [Na(+)]i in rabbit ventricular myocytes during metabolic inhibition
    • doi: 10.1006/jmcc.2001.1477
    • Li, F., Sugishita, K., Su, Z., Ueda, I., and Barry, W. H. (2001). Activation of connexin-43 hemichannels can elevate [Ca(2+)]i and [Na(+)]i in rabbit ventricular myocytes during metabolic inhibition. J. Mol. Cell Cardiol. 33, 2145-2155. doi: 10.1006/jmcc.2001.1477
    • (2001) J. Mol. Cell Cardiol. , vol.33 , pp. 2145-2155
    • Li, F.1    Sugishita, K.2    Su, Z.3    Ueda, I.4    Barry, W.H.5
  • 97
    • 84864550842 scopus 로고    scopus 로고
    • Suppression of CX43 expression by miR-20a in the progression of human prostate cancer
    • doi: 10.4161/cbt.20841
    • Li, X., Pan, J. H., Song, B., Xiong, E. Q., Chen, Z. W., Zhou, Z. S., et al. (2012b). Suppression of CX43 expression by miR-20a in the progression of human prostate cancer. Cancer Biol. Ther. 13, 890-898. doi: 10.4161/cbt.20841
    • (2012) Cancer Biol. Ther. , vol.13 , pp. 890-898
    • Li, X.1    Pan, J.H.2    Song, B.3    Xiong, E.Q.4    Chen, Z.W.5    Zhou, Z.S.6
  • 98
    • 84876313103 scopus 로고    scopus 로고
    • Connexin 26 is down-regulated by KDM5B in the progression of bladder cancer
    • doi: 10.3390/ijms14047866
    • Li, X., Su, Y., Pan, J., Zhou, Z., Song, B., Xiong, E., et al. (2013). Connexin 26 is down-regulated by KDM5B in the progression of bladder cancer. Int. J. Mol. Sci. 14, 7866-7879. doi: 10.3390/ijms14047866
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 7866-7879
    • Li, X.1    Su, Y.2    Pan, J.3    Zhou, Z.4    Song, B.5    Xiong, E.6
  • 99
    • 34548832771 scopus 로고    scopus 로고
    • Deletion of a small consensus region at 6q15, including the MAP3K7 gene, is significantly associated with high-grade prostate cancers
    • doi: 10.1158/1078-0432.CCR-07-0300
    • Liu, W., Chang, B. L., Cramer, S., Koty, P. P., Li, T., Sun, J., et al. (2007). Deletion of a small consensus region at 6q15, including the MAP3K7 gene, is significantly associated with high-grade prostate cancers. Clin. Cancer Res. 13, 5028-5033. doi: 10.1158/1078-0432.CCR-07-0300
    • (2007) Clin. Cancer Res. , vol.13 , pp. 5028-5033
    • Liu, W.1    Chang, B.L.2    Cramer, S.3    Koty, P.P.4    Li, T.5    Sun, J.6
  • 100
    • 33646748700 scopus 로고    scopus 로고
    • Pannexin 1 in erythrocytes: function without a gap
    • doi: 10.1073/pnas.0601037103
    • Locovei, S., Bao, L., and Dahl, G. (2006). Pannexin 1 in erythrocytes: function without a gap. Proc. Natl. Acad. Sci. U.S.A. 103, 7655-7659. doi: 10.1073/pnas.0601037103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7655-7659
    • Locovei, S.1    Bao, L.2    Dahl, G.3
  • 101
    • 0018877971 scopus 로고
    • Junctional cell-to-cell communication and growth control
    • doi: 10.1111/j.1749-6632.1980.tb15966.x
    • Loewenstein, W. R. (1980). Junctional cell-to-cell communication and growth control. Ann. N.Y. Acad. Sci. 339, 39-45. doi: 10.1111/j.1749-6632.1980.tb15966.x
    • (1980) Ann. N.Y. Acad. Sci. , vol.339 , pp. 39-45
    • Loewenstein, W.R.1
  • 102
    • 0014021760 scopus 로고
    • Intercellular communication and the control of tissue growth: lack of communication between cancer cells
    • doi: 10.1038/2091248a0
    • Loewenstein, W. R., and Kanno, Y. (1966). Intercellular communication and the control of tissue growth: lack of communication between cancer cells. Nature 209, 1248-1249. doi: 10.1038/2091248a0
    • (1966) Nature , vol.209 , pp. 1248-1249
    • Loewenstein, W.R.1    Kanno, Y.2
  • 103
    • 0014089460 scopus 로고
    • Intercellular communication and tissue growth
    • doi: 10.1083/jcb.33.2.225
    • Loewenstein, W. R., and Kanno, Y. (1967). Intercellular communication and tissue growth. I. Cancerous growth. J. Cell Biol. 33, 225-234. doi: 10.1083/jcb.33.2.225
    • (1967) I. Cancerous growth. J. Cell Biol. , vol.33 , pp. 225-234
    • Loewenstein, W.R.1    Kanno, Y.2
  • 104
    • 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
  • 105
    • 0037311770 scopus 로고    scopus 로고
    • The expression of the tumor suppressor gene connexin 26 is not mediated by methylation in human esophageal cancer cells
    • doi: 10.1002/mc.10102
    • Loncarek, J., Yamasaki, H., Levillain, P., Milinkevitch, S., and Mesnil, M. (2003). The expression of the tumor suppressor gene connexin 26 is not mediated by methylation in human esophageal cancer cells. Mol. Carcinog. 36, 74-81. doi: 10.1002/mc.10102
    • (2003) Mol. Carcinog. , vol.36 , pp. 74-81
    • Loncarek, J.1    Yamasaki, H.2    Levillain, P.3    Milinkevitch, S.4    Mesnil, M.5
  • 106
    • 84861765275 scopus 로고    scopus 로고
    • ATP released from cardiac fibroblasts via connexin hemichannels activates profibrotic P2Y2 receptors
    • doi: 10.1096/fj.12-204677
    • Lu, D., Soleymani, S., Madakshire, R., and Insel, P. A. (2012). ATP released from cardiac fibroblasts via connexin hemichannels activates profibrotic P2Y2 receptors. FASEB J. 26, 2580-2591. doi: 10.1096/fj.12-204677
    • (2012) FASEB J , vol.26 , pp. 2580-2591
    • Lu, D.1    Soleymani, S.2    Madakshire, R.3    Insel, P.A.4
  • 107
    • 79961160915 scopus 로고    scopus 로고
    • The gap junction protein Cx43 regulates B-lymphocyte spreading and adhesion
    • doi: 10.1242/jcs.089532
    • Machtaler, S., Dang-Lawson, M., Choi, K., Jang, C., Naus, C. C., and Matsuuchi, L. (2011). The gap junction protein Cx43 regulates B-lymphocyte spreading and adhesion. J. Cell Sci. 124(Pt 15), 2611-2621. doi: 10.1242/jcs.089532
    • (2011) J. Cell Sci. , vol.124 , Issue.PART 15 , pp. 2611-2621
    • Machtaler, S.1    Dang-Lawson, M.2    Choi, K.3    Jang, C.4    Naus, C.C.5    Matsuuchi, L.6
  • 108
    • 84055176143 scopus 로고    scopus 로고
    • The Cx26-G45E mutation displays increased hemichannel activity in a mouse model of the lethal form of keratitis-ichthyosis-deafness syndrome
    • doi: 10.1091/mbc.E11-09-0778
    • Mese, G., Sellitto, C., Li, L., Wang, H. Z., Valiunas, V., Richard, G., et al. (2011). The Cx26-G45E mutation displays increased hemichannel activity in a mouse model of the lethal form of keratitis-ichthyosis-deafness syndrome. Mol. Biol. Cell. 22, 4776-4786. doi: 10.1091/mbc.E11-09-0778
    • (2011) Mol. Biol. Cell. , vol.22 , pp. 4776-4786
    • Mese, G.1    Sellitto, C.2    Li, L.3    Wang, H.Z.4    Valiunas, V.5    Richard, G.6
  • 109
    • 0036873006 scopus 로고    scopus 로고
    • Connexins and cancer
    • doi:10.1016/S0248-4900(02)00025-4
    • Mesnil, M. (2002). Connexins and cancer. Biol. Cell 94, 493-500. doi: 10.1016/S0248-4900(02)00025-4
    • (2002) Biol. Cell , vol.94 , pp. 493-500
    • Mesnil, M.1
  • 110
    • 28944441155 scopus 로고    scopus 로고
    • Defective gap junctional intercellular communication in the carcinogenic process
    • doi: 10.1016/j.bbamem.2005.11.004
    • Mesnil, M., Crespin, S., Avanzo, J. L., and Zaidan-Dagli, M. L. (2005). Defective gap junctional intercellular communication in the carcinogenic process. Biochim. Biophys. Acta 1719, 125-145. doi: 10.1016/j.bbamem.2005.11.004
    • (2005) Biochim. Biophys. Acta , vol.1719 , pp. 125-145
    • Mesnil, M.1    Crespin, S.2    Avanzo, J.L.3    Zaidan-Dagli, M.L.4
  • 111
    • 0029557038 scopus 로고
    • Role of blocked gap junctional intercellular communication in non-genotoxic carcinogenesis
    • doi:10.1016/0378-4274(95)03588-5 701-706
    • Mesnil, M., Krutovskikh, V., Omori, Y., and Yamasaki, H. (1995). Role of blocked gap junctional intercellular communication in non-genotoxic carcinogenesis. Toxicol. Lett. 82-83, 701-706. doi: 10.1016/0378-4274(95)03588-5
    • (1995) Toxicol. Lett , pp. 82-83
    • Mesnil, M.1    Krutovskikh, V.2    Omori, Y.3    Yamasaki, H.4
  • 112
    • 0027411956 scopus 로고
    • Cell-cell communication and growth control of normal and cancer cells: evidence and hypothesis
    • doi: 10.1002/mc.2940070103
    • Mesnil, M., and Yamasaki, H. (1993). Cell-cell communication and growth control of normal and cancer cells: evidence and hypothesis. Mol. Carcinog. 7, 14-17. doi: 10.1002/mc.2940070103
    • (1993) Mol. Carcinog. , vol.7 , pp. 14-17
    • Mesnil, M.1    Yamasaki, H.2
  • 113
    • 33646061996 scopus 로고    scopus 로고
    • The action of prostaglandins on ion channels
    • doi: 10.2174/157015906775203048
    • Meves, H. (2006). The action of prostaglandins on ion channels. Curr. Neuropharmacol. 4, 41-57. doi: 10.2174/157015906775203048
    • (2006) Curr. Neuropharmacol. , vol.4 , pp. 41-57
    • Meves, H.1
  • 114
    • 79953721970 scopus 로고    scopus 로고
    • Nerve growth factor in cancer cell death and survival
    • doi: 10.3390/cancers3010510
    • Molloy, N. H., Read, D. E., and Gorman, A. M. (2011). Nerve growth factor in cancer cell death and survival. Cancers 3, 510-530. doi: 10.3390/cancers3010510
    • (2011) Cancers , vol.3 , pp. 510-530
    • Molloy, N.H.1    Read, D.E.2    Gorman, A.M.3
  • 115
    • 0034847403 scopus 로고    scopus 로고
    • Regulation of hematopoiesis by gap junction-mediated intercellular communication
    • Montecino-Rodriguez, E., and Dorshkind, K. (2001). Regulation of hematopoiesis by gap junction-mediated intercellular communication. J. Leukoc. Biol. 70, 341-347.
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 341-347
    • Montecino-Rodriguez, E.1    Dorshkind, K.2
  • 116
    • 84866367672 scopus 로고    scopus 로고
    • Calcium channels and pumps in cancer: changes and consequences
    • doi: 10.1074/jbc.R112.343061
    • Monteith, G. R., Davis, F. M., and Roberts-Thomson, S. J. (2012). Calcium channels and pumps in cancer: changes and consequences. J. Biol. Chem. 287, 31666-31673. doi: 10.1074/jbc.R112.343061
    • (2012) J. Biol. Chem. , vol.287 , pp. 31666-31673
    • Monteith, G.R.1    Davis, F.M.2    Roberts-Thomson, S.J.3
  • 117
    • 34250893780 scopus 로고    scopus 로고
    • Calcium and cancer: targeting Ca2+ transport. Nat. Rev
    • doi: 10.1038/nrc2171
    • Monteith, G. R., McAndrew, D., Faddy, H. M., and Roberts-Thomson, S. J. (2007). Calcium and cancer: targeting Ca2+ transport. Nat. Rev. Cancer 7, 519-530. doi: 10.1038/nrc2171
    • (2007) Cancer , vol.7 , pp. 519-530
    • Monteith, G.R.1    McAndrew, D.2    Faddy, H.M.3    Roberts-Thomson, S.J.4
  • 118
    • 77955929155 scopus 로고    scopus 로고
    • Action potential-enhanced ATP release from taste cells through hemichannels
    • doi: 10.1152/jn.00414.2010
    • Murata, Y., Yasuo, T., Yoshida, R., Obata, K., Yanagawa, Y., Margolskee, R. F., et al. (2010). Action potential-enhanced ATP release from taste cells through hemichannels. J. Neurophysiol. 104, 896-901. doi: 10.1152/jn.00414.2010
    • (2010) J. Neurophysiol. , vol.104 , pp. 896-901
    • Murata, Y.1    Yasuo, T.2    Yoshida, R.3    Obata, K.4    Yanagawa, Y.5    Margolskee, R.F.6
  • 119
    • 34848858289 scopus 로고    scopus 로고
    • Connexin26 expression is associated with lymphatic vessel invasion and poor prognosis in human breast cancer
    • doi: 10.1007/s10549-006-9465-8
    • Naoi, Y., Miyoshi, Y., Taguchi, T., Kim, S. J., Arai, T., Tamaki, Y., et al. (2007). Connexin26 expression is associated with lymphatic vessel invasion and poor prognosis in human breast cancer. Breast Cancer Res. Treat. 106, 11-17. doi: 10.1007/s10549-006-9465-8
    • (2007) Breast Cancer Res. Treat. , vol.106 , pp. 11-17
    • Naoi, Y.1    Miyoshi, Y.2    Taguchi, T.3    Kim, S.J.4    Arai, T.5    Tamaki, Y.6
  • 120
    • 0036203586 scopus 로고    scopus 로고
    • Gap junctions and tumour progression. Can
    • doi: 10.1139/y02-009
    • Naus, C. C. (2002). Gap junctions and tumour progression. Can. J. Physiol. Pharmacol. 80, 136-141. doi: 10.1139/y02-009
    • (2002) J. Physiol. Pharmacol. , vol.80 , pp. 136-141
    • Naus, C.C.1
  • 121
    • 77952929243 scopus 로고    scopus 로고
    • Implications and challenges of connexin connections to cancer
    • doi: 10.1038/nrc2841
    • Naus, C. C., and Laird, D. W. (2010). Implications and challenges of connexin connections to cancer. Nat. Rev. Cancer 10, 435-441. doi: 10.1038/nrc2841
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 435-441
    • Naus, C.C.1    Laird, D.W.2
  • 122
    • 84886745789 scopus 로고    scopus 로고
    • Expression of nerve growth factor and heme oxygenase-1 predict poor survival of breast carcinoma patients
    • doi: 10.1186/1471-2407-13-516
    • Noh, S. J., Bae, J. S., Jamiyandorj, U., Park, H. S., Kwon, K. S., Jung, S. H., et al. (2013). Expression of nerve growth factor and heme oxygenase-1 predict poor survival of breast carcinoma patients. BMC Cancer 13:516. doi: 10.1186/1471-2407-13-516
    • (2013) BMC Cancer , vol.13 , pp. 516
    • Noh, S.J.1    Bae, J.S.2    Jamiyandorj, U.3    Park, H.S.4    Kwon, K.S.5    Jung, S.H.6
  • 123
    • 84886639238 scopus 로고    scopus 로고
    • Role of connexin 32 hemichannels in the release of ATP from peripheral nerves
    • doi: 10.1002/glia.22568
    • Nualart-Marti, A., del Molino, E. M., Grandes, X., Bahima, L., Martin-Satué, M., Puchal, R., et al. (2013). Role of connexin 32 hemichannels in the release of ATP from peripheral nerves. Glia 61, 1976-1989. doi: 10.1002/glia.22568
    • (2013) Glia , vol.61 , pp. 1976-1989
    • Nualart-Marti, A.1    del Molino, E.M.2    Grandes, X.3    Bahima, L.4    Martin-Satué, M.5    Puchal, R.6
  • 124
    • 27544458943 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid enhances gap junctional intercellular communication via acetylation of histone containing connexin 43 gene locus
    • doi: 10.1158/0008-5472.CAN-05-0227
    • Ogawa, T., Hayashi, T., Tokunou, M., Nakachi, K., Trosko, J. E., Chang, C. C., et al. (2005). Suberoylanilide hydroxamic acid enhances gap junctional intercellular communication via acetylation of histone containing connexin 43 gene locus. Cancer Res. 65, 9771-9778. doi: 10.1158/0008-5472.CAN-05-0227
    • (2005) Cancer Res , vol.65 , pp. 9771-9778
    • Ogawa, T.1    Hayashi, T.2    Tokunou, M.3    Nakachi, K.4    Trosko, J.E.5    Chang, C.C.6
  • 125
    • 84872102097 scopus 로고    scopus 로고
    • Involvement of connexin43 hemichannel in ATP release after γ-irradiation
    • doi: 10.1093/jrr/rrs014
    • Ohshima, Y., Tsukimoto, M., Harada, H., and Kojima, S. (2012). Involvement of connexin43 hemichannel in ATP release after γ-irradiation. J. Radiat. Res. 53, 551-557. doi: 10.1093/jrr/rrs014
    • (2012) J. Radiat. Res. , vol.53 , pp. 551-557
    • Ohshima, Y.1    Tsukimoto, M.2    Harada, H.3    Kojima, S.4
  • 126
    • 84890425994 scopus 로고    scopus 로고
    • Gap junction channels and hemichannels in the CNS: regulation by signaling molecules
    • doi: 10.1016/j.neuropharm.2013.02.020
    • Orellana, J. A., Martinez, A. D., and Retamal, M. A. (2013). Gap junction channels and hemichannels in the CNS: regulation by signaling molecules. Neuropharmacology 75, 567-582. doi: 10.1016/j.neuropharm.2013.02.020
    • (2013) Neuropharmacology , vol.75 , pp. 567-582
    • Orellana, J.A.1    Martinez, A.D.2    Retamal, M.A.3
  • 127
    • 84859884278 scopus 로고    scopus 로고
    • Regulation of intercellular calcium signaling through calcium interactions with connexin-based channels
    • doi: 10.1007/978-94-007-2888-2_34
    • Orellana, J. A., Sánchez, H. A., Schalper, K. A., Figueroa, V., and Sáez, J. C. (2012). Regulation of intercellular calcium signaling through calcium interactions with connexin-based channels. Adv. Exp. Med. Biol. 740, 777-794. doi: 10.1007/978-94-007-2888-2_34
    • (2012) Adv. Exp. Med. Biol. , vol.740 , pp. 777-794
    • Orellana, J.A.1    Sánchez, H.A.2    Schalper, K.A.3    Figueroa, V.4    Sáez, J.C.5
  • 128
    • 79955739803 scopus 로고    scopus 로고
    • Amyloid β-induced death in neurons involves glial and neuronal hemichannels
    • doi: 10.1523/JNEUROSCI.6417-10.2011
    • Orellana, J. A., Shoji, K. F., Abudara, V., Ezan, P., Amigou, E., Sáez, P. J., et al. (2011). Amyloid β-induced death in neurons involves glial and neuronal hemichannels. J. Neurosci. 31, 4962-4977. doi: 10.1523/JNEUROSCI.6417-10.2011
    • (2011) J. Neurosci. , vol.31 , pp. 4962-4977
    • Orellana, J.A.1    Shoji, K.F.2    Abudara, V.3    Ezan, P.4    Amigou, E.5    Sáez, P.J.6
  • 129
    • 0035082041 scopus 로고    scopus 로고
    • Immunoglobulin and cytokine expression in mixed lymphocyte cultures is reduced by disruption of gap junction intercellular communication
    • doi: 10.1096/fj.00-0288com
    • Oviedo-Orta, E., Gasque, P., and Evans, W. H. (2001). Immunoglobulin and cytokine expression in mixed lymphocyte cultures is reduced by disruption of gap junction intercellular communication. FASEB J. 15, 768-774. doi: 10.1096/fj.00-0288com
    • (2001) FASEB J , vol.15 , pp. 768-774
    • Oviedo-Orta, E.1    Gasque, P.2    Evans, W.H.3
  • 130
    • 0034129005 scopus 로고    scopus 로고
    • Intercellular communication in the immune system: differential expression of connexin40 and 43, and perturbation of gap junction channel functions in peripheral blood and tonsil human lymphocyte subpopulations
    • doi: 10.1046/j.1365-2567.2000.00991.x
    • Oviedo-Orta, E., Hoy, T., and Evans, W. H. (2000). Intercellular communication in the immune system: differential expression of connexin40 and 43, and perturbation of gap junction channel functions in peripheral blood and tonsil human lymphocyte subpopulations. Immunology 99, 578-590. doi: 10.1046/j.1365-2567.2000.00991.x
    • (2000) Immunology , vol.99 , pp. 578-590
    • Oviedo-Orta, E.1    Hoy, T.2    Evans, W.H.3
  • 131
    • 84870057902 scopus 로고    scopus 로고
    • Regulation of connexin expression by transcription factors and epigenetic mechanisms
    • doi: 10.1016/j.bbamem.2011.12.031
    • Oyamada, M., Takebe, K., and Oyamada, Y. (2013). Regulation of connexin expression by transcription factors and epigenetic mechanisms. Biochim. Biophys. Acta 1828, 118-133. doi: 10.1016/j.bbamem.2011.12.031
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 118-133
    • Oyamada, M.1    Takebe, K.2    Oyamada, Y.3
  • 132
    • 18944394972 scopus 로고    scopus 로고
    • Evolution of gap junction proteins-the pannexin alternative
    • doi: 10.1242/jeb.01547
    • Panchin, Y. V. (2005). Evolution of gap junction proteins-the pannexin alternative. J. Exp. Biol. 208(Pt 8), 1415-1419. doi: 10.1242/jeb.01547
    • (2005) J. Exp. Biol. , vol.208 , Issue.PART 8 , pp. 1415-1419
    • Panchin, Y.V.1
  • 133
    • 78049464333 scopus 로고    scopus 로고
    • Calcium wave signaling in cancer cells
    • doi: 10.1016/j.lfs.2010.09.013
    • Parkash, J., and Asotra, K. (2010). Calcium wave signaling in cancer cells. Life Sci. 87, 587-595. doi: 10.1016/j.lfs.2010.09.013
    • (2010) Life Sci , vol.87 , pp. 587-595
    • Parkash, J.1    Asotra, K.2
  • 134
    • 19544379905 scopus 로고    scopus 로고
    • ATP released via gap junction hemichannels from the pigment epithelium regulates neural retinal progenitor proliferation
    • doi: 10.1016/j.neuron.2005.04.024
    • Pearson, R. A., Dale, N., Llaudet, E., and Mobbs, P. (2005). ATP released via gap junction hemichannels from the pigment epithelium regulates neural retinal progenitor proliferation. Neuron 46, 731-744. doi: 10.1016/j.neuron.2005.04.024
    • (2005) Neuron , vol.46 , pp. 731-744
    • Pearson, R.A.1    Dale, N.2    Llaudet, E.3    Mobbs, P.4
  • 135
    • 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
  • 136
    • 84870054442 scopus 로고    scopus 로고
    • The biochemistry and function of pannexin channels
    • doi: 10.1016/j.bbamem.2012.01.017
    • Peñuela, 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
    • Peñuela, S.1    Gehi, R.2    Laird, D.W.3
  • 137
    • 84865220396 scopus 로고    scopus 로고
    • Loss of pannexin 1 attenuates melanoma progression by reversion to a melanocytic phenotype
    • doi: 10. 1074/jbc. M112. 377176
    • Peñuela, S., Gyenis, L., Ablack, A., Churko, J. M., Berger, A. C., Litchfield, D. W., et al. (2012). Loss of pannexin 1 attenuates melanoma progression by reversion to a melanocytic phenotype. J. Biol. Chem. 287, 29184-29193. doi: 10.1074/jbc.M112.377176
    • (2012) J. Biol. Chem. , vol.287 , pp. 29184-29193
    • Peñuela, S.1    Gyenis, L.2    Ablack, A.3    Churko, J.M.4    Berger, A.C.5    Litchfield, D.W.6
  • 138
    • 78650037681 scopus 로고    scopus 로고
    • Mutations in connexin genes and disease
    • doi: 10.1111/j.1365-2362.2010.02378.x
    • Pfenniger, A., Wohlwend, A., and Kwak, B. R. (2011). Mutations in connexin genes and disease. Eur. J. Clin. Invest. 41, 103-116. doi: 10.1111/j.1365-2362.2010.02378.x
    • (2011) Eur. J. Clin. Invest. , vol.41 , pp. 103-116
    • Pfenniger, A.1    Wohlwend, A.2    Kwak, B.R.3
  • 139
    • 84884575578 scopus 로고    scopus 로고
    • Histamine induces ATP release from human subcutaneous fibroblasts, via pannexin-1 hemichannels, leading to Ca2+ mobilization and cell proliferation
    • doi: 10.1074/jbc.M113.460865
    • Pinheiro, A. R., Paramos-de-Carvalho, D., Certal, M., Costa, M. A., Costa, C., Magalhães-Cardoso, M. T., et al. (2013). Histamine induces ATP release from human subcutaneous fibroblasts, via pannexin-1 hemichannels, leading to Ca2+ mobilization and cell proliferation. J. Biol. Chem. 288, 27571-27583. doi: 10.1074/jbc.M113.460865
    • (2013) J. Biol. Chem. , vol.288 , pp. 27571-27583
    • Pinheiro, A.R.1    Paramos-de-Carvalho, D.2    Certal, M.3    Costa, M.A.4    Costa, C.5    Magalhães-Cardoso, M.T.6
  • 140
    • 0037040922 scopus 로고    scopus 로고
    • Transduction of cell survival signals by connexin-43 hemichannels
    • doi: 10.1074/jbc.M108625200
    • Plotkin, L. I., Manolagas, S. C., and Bellido, T. (2002). Transduction of cell survival signals by connexin-43 hemichannels. J. Biol. Chem. 277, 8648-8657. doi: 10.1074/jbc.M108625200
    • (2002) J. Biol. Chem. , vol.277 , pp. 8648-8657
    • Plotkin, L.I.1    Manolagas, S.C.2    Bellido, T.3
  • 141
    • 60849084461 scopus 로고    scopus 로고
    • A permeant regulating its permeation pore: inhibition of pannexin 1 channels by ATP
    • doi: 10.1152/ajpcell.00433.2008
    • Qiu, F., and Dahl, G. (2009). A permeant regulating its permeation pore: inhibition of pannexin 1 channels by ATP. Am. J. Physiol. Cell Physiol. 296, C250-C255. doi: 10.1152/ajpcell.00433.2008
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296
    • Qiu, F.1    Dahl, G.2
  • 142
    • 84877022722 scopus 로고    scopus 로고
    • Exploiting CTLA-4, PD-1 and PD-L1 to reactivate the host immune response against cancer
    • doi: 10.1038/bjc.2013.117
    • Quezada, S. A., and Peggs, K. S. (2013). Exploiting CTLA-4, PD-1 and PD-L1 to reactivate the host immune response against cancer. Br. J. Cancer 108, 1560-1565. doi: 10.1038/bjc.2013.117
    • (2013) Br. J. Cancer , vol.108 , pp. 1560-1565
    • Quezada, S.A.1    Peggs, K.S.2
  • 144
    • 79959823841 scopus 로고    scopus 로고
    • Metastatic squamous cell carcinoma of the oropharynx in a child with a mutation in the Connexin 26 gene
    • doi: 10.1097/MPH.0b013e3181e65c1c
    • Rednam, S., Hicks, J., Levy, M. L., and Pappo, A. S. (2011). Metastatic squamous cell carcinoma of the oropharynx in a child with a mutation in the Connexin 26 gene. J. Pediatr. Hematol. Oncol. 33, 387-389. doi: 10.1097/MPH.0b013e3181e65c1c
    • (2011) J. Pediatr. Hematol. Oncol. , vol.33 , pp. 387-389
    • Rednam, S.1    Hicks, J.2    Levy, M.L.3    Pappo, A.S.4
  • 145
    • 55949109095 scopus 로고    scopus 로고
    • Elevated pressure triggers a physiological release of ATP from the retina: possible role for pannexin hemichannels
    • doi: 10.1016/j.neuroscience.2008.08.036
    • Reigada, D., Lu, W., Zhang, M., and Mitchell, C. H. (2008). Elevated pressure triggers a physiological release of ATP from the retina: possible role for pannexin hemichannels. Neuroscience 157, 396-404. doi: 10.1016/j.neuroscience.2008.08.036
    • (2008) Neuroscience , vol.157 , pp. 396-404
    • Reigada, D.1    Lu, W.2    Zhang, M.3    Mitchell, C.H.4
  • 146
    • 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
  • 147
    • 36248931499 scopus 로고    scopus 로고
    • Possible involvement of different connexin43 domains in plasma membrane permeabilization induced by ischemia-reperfusion
    • doi: 10.1007/s00232-007-9043-y
    • Retamal, M. A., Schalper, K. A., Shoji, K. F., Orellana, J. A., Bennett, M. V., and Sáez, JC. (2007b). Possible involvement of different connexin43 domains in plasma membrane permeabilization induced by ischemia-reperfusion. J. Membr. Biol. 218, 49-63. doi: 10.1007/s00232-007-9043-y
    • (2007) J. Membr. Biol. , vol.218 , pp. 49-63
    • Retamal, M.A.1    Schalper, K.A.2    Shoji, K.F.3    Orellana, J.A.4    Bennett, M.V.5    Sáez, J.C.6
  • 148
    • 84893513483 scopus 로고    scopus 로고
    • Hydrostatic pressure activates ATP-sensitive K+ channels in lung epithelium by ATP release through pannexin and connexin hemichannels
    • doi: 10.1096/fj.13-229252
    • Richter, K., Kiefer, K. P., Grzesik, B. A., Clauss, W. G., and Fronius, M. (2014). Hydrostatic pressure activates ATP-sensitive K+ channels in lung epithelium by ATP release through pannexin and connexin hemichannels. FASEB J. 28, 45-55. doi: 10.1096/fj.13-229252
    • (2014) FASEB J , vol.28 , pp. 45-55
    • Richter, K.1    Kiefer, K.P.2    Grzesik, B.A.3    Clauss, W.G.4    Fronius, M.5
  • 149
    • 84890426112 scopus 로고    scopus 로고
    • The ATP required for potentiation of skeletal muscle contraction is released via pannexin hemichannels
    • doi: 10.1016/j.neuropharm.2013.03.022
    • Riquelme, M. A., Cea, L. A., Vega, J. L., Boric, M. P., Monyer, H., Bennett, M. V., et al. (2013b). The ATP required for potentiation of skeletal muscle contraction is released via pannexin hemichannels. Neuropharmacology 75, 594-603. doi: 10.1016/j.neuropharm.2013.03.022
    • (2013) Neuropharmacology , vol.75 , pp. 594-603
    • Riquelme, M.A.1    Cea, L.A.2    Vega, J.L.3    Boric, M.P.4    Monyer, H.5    Bennett, M.V.6
  • 150
    • 84890441402 scopus 로고    scopus 로고
    • Antibodies targeting extracellular domain of connexins for studies of hemichannels
    • doi: 10.1016/j.neuropharm.2013.02.021
    • Riquelme, M. A., Kar, R., Gu, S., and Jiang, J. X. (2013a). Antibodies targeting extracellular domain of connexins for studies of hemichannels. Neuropharmacology 75, 525-532. doi: 10.1016/j.neuropharm.2013.02.021
    • (2013) Neuropharmacology , vol.75 , pp. 525-532
    • Riquelme, M.A.1    Kar, R.2    Gu, S.3    Jiang, J.X.4
  • 151
    • 42549164808 scopus 로고    scopus 로고
    • Ca2+ signalling checkpoints in cancer: remodelling Ca2+ for cancer cell proliferation and survival
    • doi: 10.1038/nrc2374
    • Roderick, H. L., and Cook, S. J. (2008). Ca2+ signalling checkpoints in cancer: remodelling Ca2+ for cancer cell proliferation and survival. Nat. Rev. Cancer 8, 361-375. doi: 10.1038/nrc2374
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 361-375
    • Roderick, H.L.1    Cook, S.J.2
  • 152
    • 79958798578 scopus 로고    scopus 로고
    • P2X7 receptor antagonism in the treatment of cancers
    • doi: 10.1517/13543784.2011.583918
    • Roger, S., and Pelegrin, P. (2011). P2X7 receptor antagonism in the treatment of cancers. Expert Opin. Invest. Drugs 20, 875-880. doi: 10.1517/13543784.2011.583918
    • (2011) Expert Opin. Invest. Drugs 20, 875-880.
    • Roger, S.1    Pelegrin, P.2
  • 153
    • 17344390158 scopus 로고    scopus 로고
    • Plasma membrane channels formed by connexins: their regulation and functions
    • doi: 10.1152/physrev.00007.2003
    • Sáez, J. C., Berthoud, V. M., Brañes, M. C., Martinez, A. D., and Beyer, E. C. (2003). Plasma membrane channels formed by connexins: their regulation and functions. Physiol. Rev. 83, 1359-1400. doi: 10.1152/physrev.00007.2003
    • (2003) Physiol. Rev. , vol.83 , pp. 1359-1400
    • Sáez, J.C.1    Berthoud, V.M.2    Brañes, M.C.3    Martinez, A.D.4    Beyer, E.C.5
  • 154
    • 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
  • 155
    • 84901049274 scopus 로고    scopus 로고
    • Pannexins form gap junctions with electrophysiological and pharmacological properties distinct from connexins
    • doi: 10.1038/srep04955
    • Sahu, G., Sukumaran, S., and Bera, A. K. (2014). Pannexins form gap junctions with electrophysiological and pharmacological properties distinct from connexins. Sci. Rep. 4:4955. doi: 10.1038/srep04955
    • (2014) Sci. Rep. , vol.4 , pp. 4955
    • Sahu, G.1    Sukumaran, S.2    Bera, A.K.3
  • 156
    • 0034007959 scopus 로고    scopus 로고
    • Human hemangiosarcomas have a common polymorphism but no mutations in the connexin37 gene
    • doi:10.1002/(SICI)1097-0215(20000401)86:1%3C67::AID-IJC10%3E3.0.CO;
    • Saito, T., Krutovskikh, V., Marion, M. J., Ishak, K. G., Bennett, W. P., and Yamasaki, H. (2000). Human hemangiosarcomas have a common polymorphism but no mutations in the connexin37 gene. Int. J. Cancer 86, 67-70. doi: 10.1002/(SICI)1097-0215(20000401)86:1%3C67::AID-IJC10%3E3.0.CO;2-1
    • (2000) Int. J. Cancer , vol.86 , pp. 67-70
    • Saito, T.1    Krutovskikh, V.2    Marion, M.J.3    Ishak, K.G.4    Bennett, W.P.5    Yamasaki, H.6
  • 157
    • 77954320871 scopus 로고    scopus 로고
    • Differentially altered Ca2+ regulation and Ca2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome
    • doi: 10.1085/jgp.201010433
    • Sánchez, H. A., Mese, G., Srinivas, M., White, T. W., and Verselis, V. K. (2010). Differentially altered Ca2+ regulation and Ca2+ 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
  • 158
    • 70349253972 scopus 로고    scopus 로고
    • Metabolic inhibition increases activity of connexin-32 hemichannels permeable to Ca2+ in transfected HeLa cells
    • doi: 10.1152/ajpcell.00200.2009
    • Sánchez, H. A., Orellana, J. A., Verselis, V. K., and Sáez, J. C. (2009). Metabolic inhibition increases activity of connexin-32 hemichannels permeable to Ca2+ in transfected HeLa cells. Am. J. Physiol. Cell Physiol. 297, C665-C678. doi: 10.1152/ajpcell.00200.2009
    • (2009) Am. J. Physiol. Cell Physiol. , vol.297
    • Sánchez, H.A.1    Orellana, J.A.2    Verselis, V.K.3    Sáez, J.C.4
  • 159
    • 84859514212 scopus 로고    scopus 로고
    • Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region
    • doi: 10.1074/jbc.M111.323378
    • Sandilos, J. K., Chiu, Y. H., Chekeni, F. B., Armstrong, A. J., Walk, S. F., Ravichandran, K. S., et al. (2012). Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region. J. Biol. Chem. 287, 11303-11311. doi: 10.1074/jbc.M111.323378
    • (2012) J. Biol. Chem. , vol.287 , pp. 11303-11311
    • Sandilos, J.K.1    Chiu, Y.H.2    Chekeni, F.B.3    Armstrong, A.J.4    Walk, S.F.5    Ravichandran, K.S.6
  • 160
    • 70349659631 scopus 로고    scopus 로고
    • Dysfunctions of the diffusional membrane pathways mediated by hemichannels in inherited and acquired human diseases
    • doi: 10.2174/157016109789043937
    • Schalper, K. A., Orellana, J. A., Berthoud, V. M., and Sáez, J. C. (2009). Dysfunctions of the diffusional membrane pathways mediated by hemichannels in inherited and acquired human diseases. Curr. Vasc. Pharmacol. 7, 486-505. doi: 10.2174/157016109789043937
    • (2009) Curr. Vasc. Pharmacol. , vol.7 , pp. 486-505
    • Schalper, K.A.1    Orellana, J.A.2    Berthoud, V.M.3    Sáez, J.C.4
  • 161
    • 48449088317 scopus 로고    scopus 로고
    • Currently used methods for identification and characterization of hemichannels. Cell Commun
    • doi: 10.1080/15419060802014198
    • Schalper, K. A., Palacios-Prado, N., Orellana, J. A., and Sáez, J. C. (2008b). Currently used methods for identification and characterization of hemichannels. Cell Commun. Adhes. 15, 207-218. doi: 10.1080/15419060802014198
    • (2008) Adhes , vol.15 , pp. 207-218
    • Schalper, K.A.1    Palacios-Prado, N.2    Orellana, J.A.3    Sáez, J.C.4
  • 162
    • 54249087709 scopus 로고    scopus 로고
    • Connexin hemichannel composition determines the FGF-1-induced membrane permeability and free [Ca2+]i responses
    • doi: 10.1091/mbc.E07-12-1240
    • Schalper, K. A., Palacios-Prado, N., Retamal, M. A., Shoji, K. F., Martínez, A. D., and Sáez, J. C. (2008a). Connexin hemichannel composition determines the FGF-1-induced membrane permeability and free [Ca2+]i responses. Mol. Biol. Cell 19, 3501-3513. doi: 10.1091/mbc.E07-12-1240
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3501-3513
    • Schalper, K.A.1    Palacios-Prado, N.2    Retamal, M.A.3    Shoji, K.F.4    Martínez, A.D.5    Sáez, J.C.6
  • 163
    • 84857198309 scopus 로고    scopus 로고
    • Modulation of gap junction channels and hemichannels by growth factors
    • doi: 10.1039/c1mb05294b
    • Schalper, K. A., Riquelme, M. A., Brañes, M. C., Martínez, A. D., Vega, J. L., Berthoud, V. M., et al. (2014). Modulation of gap junction channels and hemichannels by growth factors. Mol. Biosyst. 8, 685-698. doi: 10.1039/c1mb05294b
    • (2014) Mol. Biosyst. , vol.8 , pp. 685-698
    • Schalper, K.A.1    Riquelme, M.A.2    Brañes, M.C.3    Martínez, A.D.4    Vega, J.L.5    Berthoud, V.M.6
  • 164
    • 78649653091 scopus 로고    scopus 로고
    • Connexin 43 hemichannels mediate the Ca2+ influx induced by extracellular alkalinization. Am
    • doi: 10.1152/ajpcell.00015.2010
    • Schalper, K. A., Sánchez, H. A., Lee, S. C., Altenberg, G. A., Nathanson, M. H., and Sáez, J. C. (2010). Connexin 43 hemichannels mediate the Ca2+ influx induced by extracellular alkalinization. Am. J. Physiol. Cell Physiol. 299, C1504-C1515. doi: 10.1152/ajpcell.00015.2010
    • (2010) J. Physiol. Cell Physiol. , vol.299
    • Schalper, K.A.1    Sánchez, H.A.2    Lee, S.C.3    Altenberg, G.A.4    Nathanson, M.H.5    Sáez, J.C.6
  • 165
    • 55649113607 scopus 로고    scopus 로고
    • Purinergic control of T cell activation by ATP released through pannexin-1 hemichannels
    • doi: 10.1126/scisignal.1160583 ra6
    • Schenk, U., Westendorf, A. M., Radaelli, E., Casati, A., Ferro, M., Fumagalli, M., et al. (2008). Purinergic control of T cell activation by ATP released through pannexin-1 hemichannels. Sci. Signal. 1:ra6. doi: 10.1126/scisignal.1160583
    • (2008) Sci. Signal. , vol.1
    • Schenk, U.1    Westendorf, A.M.2    Radaelli, E.3    Casati, A.4    Ferro, M.5    Fumagalli, M.6
  • 166
    • 64849095102 scopus 로고    scopus 로고
    • NAD+ and ATP released from injured cells induce P2X7-dependent shedding of CD62L and externalization of phosphatidylserine by murine T cells
    • doi: 10.4049/jimmunol.0801711
    • Scheuplein, F., Schwarz, N., Adriouch, S., Krebs, C., Bannas, P., Rissiek, B., et al. (2009). NAD+ and ATP released from injured cells induce P2X7-dependent shedding of CD62L and externalization of phosphatidylserine by murine T cells. J. Immunol. 182, 2898-2908. doi: 10.4049/jimmunol.0801711
    • (2009) J. Immunol. , vol.182 , pp. 2898-2908
    • Scheuplein, F.1    Schwarz, N.2    Adriouch, S.3    Krebs, C.4    Bannas, P.5    Rissiek, B.6
  • 167
    • 0033925821 scopus 로고    scopus 로고
    • Physiological activation of presynaptic metabotropic glutamate receptors increases intracellular calcium and glutamate release
    • Schwartz, N. E., and Alford, S. (2000). Physiological activation of presynaptic metabotropic glutamate receptors increases intracellular calcium and glutamate release. J. Neurophysiol. 84, 415-427.
    • (2000) J. Neurophysiol. , vol.84 , pp. 415-427
    • Schwartz, N.E.1    Alford, S.2
  • 168
    • 79960694399 scopus 로고    scopus 로고
    • Rho signaling regulates pannexin 1-mediated ATP release from airway epithelia
    • doi: 10.1074/jbc.M111.260562
    • Seminario-Vidal, L., Okada, S. F., Sesma, J. I., Kreda, S. M., van Heusden, C. A., Zhu, Y., et al. (2011). Rho signaling regulates pannexin 1-mediated ATP release from airway epithelia. J. Biol. Chem. 286, 26277-26286. doi: 10.1074/jbc.M111.260562
    • (2011) J. Biol. Chem. , vol.286 , pp. 26277-26286
    • Seminario-Vidal, L.1    Okada, S.F.2    Sesma, J.I.3    Kreda, S.M.4    van Heusden, C.A.5    Zhu, Y.6
  • 169
    • 33846695393 scopus 로고    scopus 로고
    • Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions
    • doi: 10.1016/j.cell.2006.12.037
    • Shaw, R. M., Fay, A. J., Puthenveedu, M. A., von Zastrow, M., Jan, Y. N., and Jan, L. Y. (2007). Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions. Cell 128, 547-560. doi: 10.1016/j.cell.2006.12.037
    • (2007) Cell , vol.128 , pp. 547-560
    • Shaw, R.M.1    Fay, A.J.2    Puthenveedu, M.A.3    von Zastrow, M.4    Jan, Y.N.5    Jan, L.Y.6
  • 170
    • 84876581650 scopus 로고    scopus 로고
    • Long-distance relationships: do membrane nanotubes regulate cell-cell communication and disease progression?
    • doi: 10.1091/mbc.E12-08-0622
    • Sherer, N. M. (2013). Long-distance relationships: do membrane nanotubes regulate cell-cell communication and disease progression? Mol. Biol. Cell 24, 1095-1098. doi: 10.1091/mbc.E12-08-0622
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1095-1098
    • Sherer, N.M.1
  • 171
    • 22144495802 scopus 로고    scopus 로고
    • In vivo and in vitro expression of connexins in the human corneal epithelium
    • doi: 10.1167/iovs.04-1364
    • Shurman, D. L., Glazewski, L., Gumpert, A., Zieske, J. D., and Richard, G. (2005). In vivo and in vitro expression of connexins in the human corneal epithelium. Invest. Ophthalmol. Vis. Sci. 46, 1957-1965. doi: 10.1167/iovs.04-1364
    • (2005) Invest. Ophthalmol. Vis. Sci. , vol.46 , pp. 1957-1965
    • Shurman, D.L.1    Glazewski, L.2    Gumpert, A.3    Zieske, J.D.4    Richard, G.5
  • 172
    • 79957575641 scopus 로고    scopus 로고
    • DNA methylation analyses of the connexin gene family reveal silencing of GJC1 (Connexin45) by promoter hypermethylation in colorectal cancer
    • doi: 10.4161/epi.6.5.15237
    • Sirnes, S., Honne, H., Ahmed, D., Danielsen, S. A., Rognum, T. O., Meling, G. I., et al. (2011). DNA methylation analyses of the connexin gene family reveal silencing of GJC1 (Connexin45) by promoter hypermethylation in colorectal cancer. Epigenetics 6, 602-609. doi: 10.4161/epi.6.5.15237
    • (2011) Epigenetics , vol.6 , pp. 602-609
    • Sirnes, S.1    Honne, H.2    Ahmed, D.3    Danielsen, S.A.4    Rognum, T.O.5    Meling, G.I.6
  • 173
    • 1942438964 scopus 로고    scopus 로고
    • Gap junctions and the connexin protein family
    • doi: 10.1016/j.cardiores.2003.11.013
    • Söhl, G., and Willecke, K. (2004). Gap junctions and the connexin protein family. Cardiovasc. Res. 62, 228-232. doi: 10.1016/j.cardiores.2003.11.013
    • (2004) Cardiovasc. Res. , vol.62 , pp. 228-232
    • Söhl, G.1    Willecke, K.2
  • 174
    • 84455170170 scopus 로고    scopus 로고
    • Connexin-43 hemichannels mediate cyclic ADP-ribose generation and its Ca2+-mobilizing activity by NAD+/cyclic ADP-ribose transport
    • doi: 10.1074/jbc.M111.307645
    • Song, E. K., Rah, S. Y., Lee, Y. R., Yoo, C. H., Kim, Y. R., Yeom, J. H., et al. (2011). Connexin-43 hemichannels mediate cyclic ADP-ribose generation and its Ca2+-mobilizing activity by NAD+/cyclic ADP-ribose transport. J. Biol. Chem. 286, 44480-44490. doi: 10.1074/jbc.M111.307645
    • (2011) J. Biol. Chem. , vol.286 , pp. 44480-44490
    • Song, E.K.1    Rah, S.Y.2    Lee, Y.R.3    Yoo, C.H.4    Kim, Y.R.5    Yeom, J.H.6
  • 175
    • 70349660081 scopus 로고    scopus 로고
    • Blockade of connexin 43 hemichannels reduces neointima formation after vascular injury by inhibiting proliferation and phenotypic modulation of smooth muscle cells
    • doi: 10.3181/0902-RM-80
    • Song, M., Yu, X., Cui, X., Zhu, G., Zhao, G., Chen, J., et al. (2009). Blockade of connexin 43 hemichannels reduces neointima formation after vascular injury by inhibiting proliferation and phenotypic modulation of smooth muscle cells. Exp. Biol. Med. (Maywood) 234, 1192-1200. doi: 10.3181/0902-RM-80
    • (2009) Exp. Biol. Med. (Maywood) , vol.234 , pp. 1192-1200
    • Song, M.1    Yu, X.2    Cui, X.3    Zhu, G.4    Zhao, G.5    Chen, J.6
  • 177
    • 33750300467 scopus 로고    scopus 로고
    • Functional connexin hemichannels: a critical appraisal
    • doi: 10.1002/glia.20429
    • Spray, D. C., Ye, Z. C., and Ransom, B. R. (2006). Functional connexin hemichannels: a critical appraisal. Glia 54, 758-773. doi: 10.1002/glia.20429
    • (2006) Glia , vol.54 , pp. 758-777
    • Spray, D.C.1    Ye, Z.C.2    Ransom, B.R.3
  • 179
    • 77957564570 scopus 로고    scopus 로고
    • Extracellular adenosine triphosphate and adenosine in cancer
    • doi: 10.1038/onc.2010.292
    • Stagg, J., and Smyth, M. J. (2010). Extracellular adenosine triphosphate and adenosine in cancer. Oncogene 29, 5346-5358. doi: 10.1038/onc.2010.292
    • (2010) Oncogene , vol.29 , pp. 53465358
    • Stagg, J.1    Smyth, M.J.2
  • 180
    • 84876333409 scopus 로고    scopus 로고
    • Role of connexins in metastatic breast cancer and melanoma brain colonization
    • doi: 10.1242/jcs.112748
    • Stoletov, K., Strnadel, J., Zardouzian, E., Momiyama, M., Park, F. D., Kelber, J. A., et al. (2013). Role of connexins in metastatic breast cancer and melanoma brain colonization. J. Cell Sci. 126(Pt 4), 904-913. doi: 10.1242/jcs.112748
    • (2013) J. Cell Sci. , vol.126 , Issue.PART 4 , pp. 904-913
    • Stoletov, K.1    Strnadel, J.2    Zardouzian, E.3    Momiyama, M.4    Park, F.D.5    Kelber, J.A.6
  • 181
    • 0042364995 scopus 로고    scopus 로고
    • Modulation of intercellular calcium signaling in astrocytes by extracellular calcium and magnesium
    • doi: 10.1002/glia.10257
    • Stout, C., and Charles, A. (2003). Modulation of intercellular calcium signaling in astrocytes by extracellular calcium and magnesium. Glia 43, 265-273. doi: 10.1002/glia.10257
    • (2003) Glia , vol.43 , pp. 265-273
    • Stout, C.1    Charles, A.2
  • 182
    • 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
  • 183
    • 77955285320 scopus 로고    scopus 로고
    • Pannexin 2 is expressed by postnatal hippocampal neural progenitors and modulates neuronal commitment\
    • doi: 10.1074/jbc.M110.130054
    • Swayne, L. A., Sorbara, C. D., and Bennett, S. A. (2010). Pannexin 2 is expressed by postnatal hippocampal neural progenitors and modulates neuronal commitment. J. Biol. Chem. 285, 24977-24986. doi: 10.1074/jbc.M110.130054
    • (2010) J. Biol. Chem. , vol.285 , pp. 24977-24986
    • Swayne, L.A.1    Sorbara, C.D.2    Bennett, S.A.3
  • 184
    • 0036119604 scopus 로고    scopus 로고
    • Variable promoter region CpG island methylation of the putative tumor suppressor gene Connexin 26 in breast cancer
    • doi: 10.1093/carcin/23.2.231
    • Tan, L. W., Bianco, T., and Dobrovic, A. (2002). Variable promoter region CpG island methylation of the putative tumor suppressor gene Connexin 26 in breast cancer. Carcinogenesis 23, 231-236. doi: 10.1093/carcin/23.2.231
    • (2002) Carcinogenesis , vol.23 , pp. 231-236
    • Tan, L.W.1    Bianco, T.2    Dobrovic, A.3
  • 185
    • 84890854892 scopus 로고    scopus 로고
    • Aberrant expression of cx43 is associated with the peritoneal metastasis of gastric cancer and cx43-mediated gap junction enhances gastric cancer cell diapedesis from peritoneal mesothelium
    • doi: 10.1371/journal.pone.0074527
    • Tang, B., Peng, Z. H., Yu, P. W., Yu, G., Qian, F., Zeng, D. Z., et al. (2013). Aberrant expression of cx43 is associated with the peritoneal metastasis of gastric cancer and cx43-mediated gap junction enhances gastric cancer cell diapedesis from peritoneal mesothelium. PLoS ONE 8:e74527. doi: 10.1371/journal.pone.0074527
    • (2013) PLoS ONE , vol.8
    • Tang, B.1    Peng, Z.H.2    Yu, P.W.3    Yu, G.4    Qian, F.5    Zeng, D.Z.6
  • 186
    • 29344472071 scopus 로고    scopus 로고
    • Changes in gap junctional connexin isoforms during prostate cancer progression
    • doi: 10.1002/pros.20317
    • Tate, A. W., Lung, T., Radhakrishnan, A., Lim, S. D., Lin, X., and Edlund, M. (2006). Changes in gap junctional connexin isoforms during prostate cancer progression. Prostate 66, 19-31. doi: 10.1002/pros.20317
    • (2006) Prostate , vol.66 , pp. 19-31
    • Tate, A.W.1    Lung, T.2    Radhakrishnan, A.3    Lim, S.D.4    Lin, X.5    Edlund, M.6
  • 187
    • 84873029942 scopus 로고    scopus 로고
    • The potential prognostic value of connexin 26 and 46 expression in neoadjuvant-treated breast cancer
    • doi: 10.1186/1471-2407-13-50
    • Teleki, I., Krenacs, T., Szasz, M. A., Kulka, J., Wichmann, B., Leo, C., et al. (2013). The potential prognostic value of connexin 26 and 46 expression in neoadjuvant-treated breast cancer. BMC Cancer 13:50. doi: 10.1186/1471-2407-13-50
    • (2013) BMC Cancer , vol.13 , pp. 50
    • Teleki, I.1    Krenacs, T.2    Szasz, M.A.3    Kulka, J.4    Wichmann, B.5    Leo, C.6
  • 188
    • 84864130599 scopus 로고    scopus 로고
    • Extracellular ATP exerts opposite effects on activated and regulatory CD4+ T cells via purinergic P2 receptor activation
    • doi: 10.4049/jimmunol.1103800
    • Trabanelli, S., Ocadlíková, D., Gulinelli, S., Curti, A., Salvestrini, V., Vieira, R. P., et al. (2012). Extracellular ATP exerts opposite effects on activated and regulatory CD4+ T cells via purinergic P2 receptor activation. J. Immunol. 189, 1303-1310. doi: 10.4049/jimmunol.1103800
    • (2012) J. Immunol. , vol.189 , pp. 1303-1310
    • Trabanelli, S.1    Ocadlíková, D.2    Gulinelli, S.3    Curti, A.4    Salvestrini, V.5    Vieira, R.P.6
  • 189
    • 77952363301 scopus 로고    scopus 로고
    • Glutamate receptor ion channels: structure, regulation, and function
    • doi: 10.1124/pr.109.002451
    • Traynelis, S. F., Wollmuth, L. P., McBain, C. J., Menniti, F. S., Vance, K. M., Ogden, K. K., et al. (2010). Glutamate receptor ion channels: structure, regulation, and function. Pharmacol. Rev. 62, 405-496. doi: 10.1124/pr.109.002451
    • (2010) Pharmacol. Rev. , vol.62 , pp. 405-496
    • Traynelis, S.F.1    Wollmuth, L.P.2    McBain, C.J.3    Menniti, F.S.4    Vance, K.M.5    Ogden, K.K.6
  • 190
    • 0021018050 scopus 로고
    • Mechanisms of tumor promotion: potential role of intercellular communication
    • doi: 10.3109/07357908309020276
    • Trosko, J. E., Chang, C. C., and Medcalf, A. (1983). Mechanisms of tumor promotion: potential role of intercellular communication. Cancer Invest. 1, 511-526. doi: 10.3109/07357908309020276
    • (1983) Cancer Invest , vol.1 , pp. 511-526
    • Trosko, J.E.1    Chang, C.C.2    Medcalf, A.3
  • 191
    • 0000299698 scopus 로고    scopus 로고
    • Cell-cell communication in carcinogenesis
    • Trosko, J. E., and Ruch, R. J. (1998). Cell-cell communication in carcinogenesis. Front. Biosci. 3, d208-d236.
    • (1998) Front. Biosci. , vol.3
    • Trosko, J.E.1    Ruch, R.J.2
  • 192
    • 84861587400 scopus 로고    scopus 로고
    • Non-channel functions of connexins in cell growth and cell death
    • doi: 10.1016/j.bbamem.2011.06.011
    • Vinken, M., Decrock, E., Leybaert, L., Bultynck, G., Himpens, B., Vanhaecke, T., et al. (2012). Non-channel functions of connexins in cell growth and cell death. Biochim. Biophys. Acta 1818, 2002-2008. doi: 10.1016/j.bbamem.2011.06.011
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2002-2008
    • Vinken, M.1    Decrock, E.2    Leybaert, L.3    Bultynck, G.4    Himpens, B.5    Vanhaecke, T.6
  • 193
    • 58049181324 scopus 로고    scopus 로고
    • Epigenetic regulation of gap junctional intercellular communication: more than a way to keep cells quiet?
    • doi: 10.1016/j.bbcan.2008.08.002
    • Vinken, M., De Rop, E., Decrock, E., De Vuyst, E., Leybaert, L., Vanhaecke, T., et al. (2009). Epigenetic regulation of gap junctional intercellular communication: more than a way to keep cells quiet? Biochim. Biophys. Acta 1795, 53-61. doi: 10.1016/j.bbcan.2008.08.002
    • (2009) Biochim. Biophys. Acta , vol.1795 , pp. 53-61
    • Vinken, M.1    De Rop, E.2    Decrock, E.3    De Vuyst, E.4    Leybaert, L.5    Vanhaecke, T.6
  • 195
    • 84867644930 scopus 로고    scopus 로고
    • Connexin mimetic peptides inhibit Cx43 hemichannel opening triggered by voltage and intracellular Ca2+ elevation
    • doi: 10.1007/s00395-012-0304-2
    • Wang, N., De Bock, M., Antoons, G., Gadicherla, A. K., Bol, M., Decrock, E., et al. (2012). Connexin mimetic peptides inhibit Cx43 hemichannel opening triggered by voltage and intracellular Ca2+ elevation. Basic Res. Cardiol. 107:304. doi: 10.1007/s00395-012-0304-2
    • (2012) Basic Res. Cardiol. , vol.107 , pp. 304
    • Wang, N.1    De Bock, M.2    Antoons, G.3    Gadicherla, A.K.4    Bol, M.5    Decrock, E.6
  • 196
    • 84890433663 scopus 로고    scopus 로고
    • Connexin targeting peptides as inhibitors of voltage- and intracellular Ca(2+)-triggered Cx43 hemichannel opening
    • doi: 10.1016/j.neuropharm.2013.08.021
    • Wang, N., De Bock, M., Decrock, E., Bol, M., Gadicherla, A., Bultynck, G., et al. (2013a). Connexin targeting peptides as inhibitors of voltage- and intracellular Ca(2+)-triggered Cx43 hemichannel opening. Neuropharmacology. 75, 506-516. doi: 10.1016/j.neuropharm.2013.08.021
    • (2013) Neuropharmacology , vol.75 , pp. 506-516
    • Wang, N.1    De Bock, M.2    Decrock, E.3    Bol, M.4    Gadicherla, A.5    Bultynck, G.6
  • 197
    • 78649825336 scopus 로고    scopus 로고
    • Current and emerging biomarkers in breast cancer: prognosis and prediction. Endocr. Relat
    • doi: 10.1677/ERC-10-0136
    • Weigel, M. T., and Dowsett, M. (2010). Current and emerging biomarkers in breast cancer: prognosis and prediction. Endocr. Relat. Cancer 17, R245-R262. doi: 10.1677/ERC-10-0136
    • (2010) Cancer , vol.17
    • Weigel, M.T.1    Dowsett, M.2
  • 198
    • 4444222881 scopus 로고    scopus 로고
    • Calcium waves propagate through radial glial cells and modulate proliferation in the developing neocortex
    • doi: 10.1016/j.neuron.2004.08.015
    • Weissman, T. A., Riquelme, P. A., Ivic, L., Flint, A. C., and Kriegstein, A. R. (2004). Calcium waves propagate through radial glial cells and modulate proliferation in the developing neocortex. Neuron 43, 647-661. doi: 10.1016/j.neuron.2004.08.015
    • (2004) Neuron , vol.43 , pp. 647-661
    • Weissman, T.A.1    Riquelme, P.A.2    Ivic, L.3    Flint, A.C.4    Kriegstein, A.R.5
  • 199
    • 33645977207 scopus 로고    scopus 로고
    • P2 receptors and cancer
    • doi: 10.1016/j.tips.2006.02.004
    • White, N., and Burnstock, G. (2006). P2 receptors and cancer. Trends Pharmacol. Sci. 27, 211-217. doi: 10.1016/j.tips.2006.02.004
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 211-217
    • White, N.1    Burnstock, G.2
  • 200
    • 84858964705 scopus 로고    scopus 로고
    • Pannexin 1 regulates postnatal neural stem and progenitor cell proliferation
    • doi: 10.1186/1749-8104-7-11
    • Wicki-Stordeur, L. E., Dzugalo, A. D., Swansburg, R. M., Suits, J. M., and Swayne, L. A. (2012). Pannexin 1 regulates postnatal neural stem and progenitor cell proliferation. Neural Dev. 7:11. doi: 10.1186/1749-8104-7-11
    • (2012) Neural Dev , vol.7 , pp. 11
    • Wicki-Stordeur, L.E.1    Dzugalo, A.D.2    Swansburg, R.M.3    Suits, J.M.4    Swayne, L.A.5
  • 201
    • 78149326486 scopus 로고    scopus 로고
    • Pannexin-1 hemichannel-mediated ATP release together with P2X1 and P2X4 receptors regulate T-cell activation at the immune synapse
    • doi: 10.1182/blood-2010-04-277707
    • Woehrle, T., Yip, L., Elkhal, A., Sumi, Y., Chen, Y., Yao, Y., et al. (2010). Pannexin-1 hemichannel-mediated ATP release together with P2X1 and P2X4 receptors regulate T-cell activation at the immune synapse. Blood 116, 3475-3484. doi: 10.1182/blood-2010-04-277707
    • (2010) Blood , vol.116 , pp. 3475-3484
    • Woehrle, T.1    Yip, L.2    Elkhal, A.3    Sumi, Y.4    Chen, Y.5    Yao, Y.6
  • 202
    • 33746855402 scopus 로고    scopus 로고
    • Connexin37 protects against atherosclerosis by regulating monocyte adhesion
    • doi: 10.1038/nm1441
    • Wong, C. W., Christen, T., Roth, I., Chadjichristos, C. E., Derouette, J. P., Foglia, B. F., et al. (2006). Connexin37 protects against atherosclerosis by regulating monocyte adhesion. Nat. Med. 12, 950-954. doi: 10.1038/nm1441
    • (2006) Nat. Med. , vol.12 , pp. 950-954
    • Wong, C.W.1    Christen, T.2    Roth, I.3    Chadjichristos, C.E.4    Derouette, J.P.5    Foglia, B.F.6
  • 203
    • 84861005703 scopus 로고    scopus 로고
    • Neurons respond directly to mechanical deformation with pannexin-mediated ATP release and autostimulation of P2X7 receptors
    • doi: 10.1113/jphysiol.2012.227983
    • Xia, J., Lim, J. C., Lu, W., Beckel, J. M., Macarak, E. J., Laties, A. M., et al. (2012). Neurons respond directly to mechanical deformation with pannexin-mediated ATP release and autostimulation of P2X7 receptors. J. Physiol. 590(Pt 10), 2285-2304. doi: 10.1113/jphysiol.2012.227983
    • (2012) J. Physiol. , vol.590 , Issue.PART 10 , pp. 2285-2304
    • Xia, J.1    Lim, J.C.2    Lu, W.3    Beckel, J.M.4    Macarak, E.J.5    Laties, A.M.6
  • 204
    • 84869204632 scopus 로고    scopus 로고
    • Pannexin1 contributes to pathophysiological ATP release in lipoapoptosis induced by saturated free fatty acids in liver cells
    • doi: 10.1152/ajpcell.00175.2012
    • Xiao, F., Waldrop, S. L., Khimji, A. K., and Kilic, G. (2012). Pannexin1 contributes to pathophysiological ATP release in lipoapoptosis induced by saturated free fatty acids in liver cells. Am. J. Physiol. Cell Physiol. 303, C1034-C1044. doi: 10.1152/ajpcell.00175.2012
    • (2012) Am. J. Physiol. Cell Physiol. , vol.303
    • Xiao, F.1    Waldrop, S.L.2    Khimji, A.K.3    Kilic, G.4
  • 205
    • 0026134909 scopus 로고
    • Maize mesocotyl plasmodesmata proteins cross-react with connexin gap junction protein antibodies
    • doi: 10.1105/tpc.3.4.407
    • Yahalom, A., Warmbrodt, R. D., Laird, D. W., Traub, O., Revel, J. P., Willecke, K., et al. (1991). Maize mesocotyl plasmodesmata proteins cross-react with connexin gap junction protein antibodies. Plant Cell 3, 407-417. doi: 10.1105/tpc.3.4.407
    • (1991) Plant Cell , vol.3 , pp. 407-417
    • Yahalom, A.1    Warmbrodt, R.D.2    Laird, D.W.3    Traub, O.4    Revel, J.P.5    Willecke, K.6
  • 206
    • 0025374396 scopus 로고
    • Gap junctional intercellular communication and carcinogenesis
    • doi: 10.1093/carcin/11.7.1051
    • Yamasaki, H. (1990). Gap junctional intercellular communication and carcinogenesis. Carcinogenesis 11, 1051-1058. doi: 10.1093/carcin/11.7.1051
    • (1990) Carcinogenesis , vol.11 , pp. 1051-1058
    • Yamasaki, H.1
  • 207
    • 34548463101 scopus 로고    scopus 로고
    • Downregulation of connexin 43 in nasopharyngeal carcinoma cells is related to promoter methylation
    • doi: 10.1016/j.oraloncology.2006.11.004
    • Yi, Z. C., Wang, H., Zhang, G. Y., and Xia, B. (2007). Downregulation of connexin 43 in nasopharyngeal carcinoma cells is related to promoter methylation. Oral. Oncol. 43, 898-904. doi: 10.1016/j.oraloncology.2006.11.004
    • (2007) Oral. Oncol. , vol.43 , pp. 898-904
    • Yi, Z.C.1    Wang, H.2    Zhang, G.Y.3    Xia, B.4
  • 208
    • 56349121125 scopus 로고    scopus 로고
    • An oncogenomics-based in vivo RNAi screen identifies tumor suppressors in liver cancer
    • doi: 10.1016/j.cell.2008.09.061
    • Zender, L., Xue, W., Zuber, J., Semighini, C. P., Krasnitz, A., Ma, B., et al. (2008). An oncogenomics-based in vivo RNAi screen identifies tumor suppressors in liver cancer. Cell 135, 852-864. doi: 10.1016/j.cell.2008.09.061
    • (2008) Cell , vol.135 , pp. 852-864
    • Zender, L.1    Xue, W.2    Zuber, J.3    Semighini, C.P.4    Krasnitz, A.5    Ma, B.6
  • 209
    • 29444434679 scopus 로고    scopus 로고
    • Gap junctional hemichannel-mediated ATP release and hearing controls in the inner ear
    • doi: 10.1073/pnas.0506481102
    • Zhao, H. B., Yu, N., and Fleming, C. R. (2005). Gap junctional hemichannel-mediated ATP release and hearing controls in the inner ear. Proc. Natl. Acad. Sci. U.S.A. 102, 18724-18729. doi: 10.1073/pnas.0506481102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18724-18729
    • Zhao, H.B.1    Yu, N.2    Fleming, C.R.3
  • 210
    • 84900359119 scopus 로고    scopus 로고
    • Differential impact of adenosine nucleotides released by osteocytes on breast cancer growth and bone metastasis
    • doi: 10.1038/onc.2014.113. [Epub ahead of print]
    • Zhou, J. Z., Riquelme, M. A., Gao, X., Ellies, L. G., Sun, L. Z., and Jiang, J. X. (2014). Differential impact of adenosine nucleotides released by osteocytes on breast cancer growth and bone metastasis. Oncogene. doi: 10.1038/onc.2014.113. [Epub ahead of print].
    • (2014) Oncogene
    • Zhou, J.Z.1    Riquelme, M.A.2    Gao, X.3    Ellies, L.G.4    Sun, L.Z.5    Jiang, J.X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.