메뉴 건너뛰기




Volumn 278, Issue C, 2009, Pages 69-118

Chapter 2 Biological and Biophysical Properties of Vascular Connexin Channels

Author keywords

Connexin; Endothelial cells; Hemichannel; Heterocellular communication; Myoendothelial junction; Smooth muscle cells

Indexed keywords

CONNEXIN 37; CONNEXIN 40; CONNEXIN 43; CONNEXIN 45; GAP JUNCTION PROTEIN; TRANSCRIPTION FACTOR;

EID: 73349090269     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1937-6448(09)78002-5     Document Type: Review
Times cited : (84)

References (260)
  • 1
    • 0036683707 scopus 로고    scopus 로고
    • Post-translational integration and oligomerization of connexin 26 in plasma membranes and evidence of formation of membrane pores: implications for the assembly of gap junctions
    • Ahmad S., and Evans W.H. Post-translational integration and oligomerization of connexin 26 in plasma membranes and evidence of formation of membrane pores: implications for the assembly of gap junctions. Biochem. J. 365 (2002) 693-699
    • (2002) Biochem. J. , vol.365 , pp. 693-699
    • Ahmad, S.1    Evans, W.H.2
  • 2
    • 33745190968 scopus 로고    scopus 로고
    • Heteromeric, but not homomeric, connexin channels are selectively permeable to inositol phosphates
    • Ayad W.A., Locke D., Koreen I.V., and Harris A.L. Heteromeric, but not homomeric, connexin channels are selectively permeable to inositol phosphates. J. Biol. Chem. 281 (2006) 16727-16739
    • (2006) J. Biol. Chem. , vol.281 , pp. 16727-16739
    • Ayad, W.A.1    Locke, D.2    Koreen, I.V.3    Harris, A.L.4
  • 3
    • 0034120338 scopus 로고    scopus 로고
    • The influence of surface charges on the conductance of the human connexin37 gap junction channel
    • Banach K., Ramanan S.V., and Brink P.R. The influence of surface charges on the conductance of the human connexin37 gap junction channel. Biophys. J. 78 (2000) 752-760
    • (2000) Biophys. J. , vol.78 , pp. 752-760
    • Banach, K.1    Ramanan, S.V.2    Brink, P.R.3
  • 5
    • 12144288999 scopus 로고    scopus 로고
    • The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins
    • Baranova A., Ivanov D., Petrash N., Pestova A., Skoblov M., Kelmanson I., et al. The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins. Genomics 83 (2004) 706-716
    • (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
  • 6
    • 0030814751 scopus 로고    scopus 로고
    • Species-specific voltage-gating properties of connexin45 junctions expressed in Xenopus oocytes
    • Barrio L.C., Capel J., Jarillo J.A., Castro C., and Revilla A. Species-specific voltage-gating properties of connexin45 junctions expressed in Xenopus oocytes. Biophys. J. 73 (1997) 757-769
    • (1997) Biophys. J. , vol.73 , pp. 757-769
    • Barrio, L.C.1    Capel, J.2    Jarillo, J.A.3    Castro, C.4    Revilla, A.5
  • 7
    • 0031755163 scopus 로고    scopus 로고
    • Capillaries and arterioles are electrically coupled in hamster cheek pouch
    • Beach J.M., McGahren E.D., and Duling B.R. Capillaries and arterioles are electrically coupled in hamster cheek pouch. Am. J. Physiol. 275 (1998) H1489-H1496
    • (1998) Am. J. Physiol. , vol.275
    • Beach, J.M.1    McGahren, E.D.2    Duling, B.R.3
  • 8
    • 0030976035 scopus 로고    scopus 로고
    • Monovalent cation permeation through the connexin40 gap junction channel. Cs, Rb, K, Na, Li, TEA, TMA, TBA, and effects of anions Br, Cl, F, acetate, aspartate, glutamate, and NO3
    • Beblo D.A., and Veenstra R.D. Monovalent cation permeation through the connexin40 gap junction channel. Cs, Rb, K, Na, Li, TEA, TMA, TBA, and effects of anions Br, Cl, F, acetate, aspartate, glutamate, and NO3. J. Gen. Physiol. 109 (1997) 509-522
    • (1997) J. Gen. Physiol. , vol.109 , pp. 509-522
    • Beblo, D.A.1    Veenstra, R.D.2
  • 9
    • 33646586079 scopus 로고    scopus 로고
    • Selective permeability of different connexin channels to the second messenger cyclic AMP
    • Bedner P., Niessen H., Odermatt B., Kretz M., Willecke K., and Harz H. Selective permeability of different connexin channels to the second messenger cyclic AMP. J. Biol. Chem. 281 (2006) 6673-6681
    • (2006) J. Biol. Chem. , vol.281 , pp. 6673-6681
    • Bedner, P.1    Niessen, H.2    Odermatt, B.3    Kretz, M.4    Willecke, K.5    Harz, H.6
  • 10
    • 0242380301 scopus 로고    scopus 로고
    • New roles for astrocytes: gap junction hemichannels have something to communicate
    • Bennett M.V., Contreras J.E., Bukauskas F.F., and Saez J.C. New roles for astrocytes: gap junction hemichannels have something to communicate. Trend Neurosci. 26 (2003) 610-617
    • (2003) Trend Neurosci. , vol.26 , pp. 610-617
    • Bennett, M.V.1    Contreras, J.E.2    Bukauskas, F.F.3    Saez, J.C.4
  • 11
    • 0026530906 scopus 로고
    • An electron-microscopic study of smooth muscle cell dye coupling in the pig coronary arteries. Role of gap junctions
    • Beny J.L., and Connat J.L. An electron-microscopic study of smooth muscle cell dye coupling in the pig coronary arteries. Role of gap junctions. Circ. Res. 70 (1992) 49-55
    • (1992) Circ. Res. , vol.70 , pp. 49-55
    • Beny, J.L.1    Connat, J.L.2
  • 12
    • 0024791786 scopus 로고
    • Dye and electrical coupling of endothelial cells in situ
    • Beny J.L., and Gribi F. Dye and electrical coupling of endothelial cells in situ. Tissue Cell 21 (1989) 797-802
    • (1989) Tissue Cell , vol.21 , pp. 797-802
    • Beny, J.L.1    Gribi, F.2
  • 13
    • 0033525038 scopus 로고    scopus 로고
    • Direct high affinity modulation of connexin channel activity by cyclic nucleotides
    • Bevans C.G., and Harris A.L. Direct high affinity modulation of connexin channel activity by cyclic nucleotides. J. Biol. Chem. 274 (1999) 3720-3725
    • (1999) J. Biol. Chem. , vol.274 , pp. 3720-3725
    • Bevans, C.G.1    Harris, A.L.2
  • 14
    • 0033525213 scopus 로고    scopus 로고
    • Regulation of connexin channels by pH. Direct action of the protonated form of taurine and other aminosulfonates
    • Bevans C.G., and Harris A.L. Regulation of connexin channels by pH. Direct action of the protonated form of taurine and other aminosulfonates. J. Biol. Chem. 274 (1999) 3711-3719
    • (1999) J. Biol. Chem. , vol.274 , pp. 3711-3719
    • Bevans, C.G.1    Harris, A.L.2
  • 15
    • 0032579554 scopus 로고    scopus 로고
    • Isoform composition of connexin channels determines selectivity among second messengers and uncharged molecules
    • Bevans C.G., Kordel M., Rhee S.K., and Harris A.L. Isoform composition of connexin channels determines selectivity among second messengers and uncharged molecules. J. Biol. Chem. 273 (1998) 2808-2816
    • (1998) J. Biol. Chem. , vol.273 , pp. 2808-2816
    • Bevans, C.G.1    Kordel, M.2    Rhee, S.K.3    Harris, A.L.4
  • 16
    • 0034168415 scopus 로고    scopus 로고
    • Modulation of intercellular communication by differential regulation and heteromeric mixing of co-expressed connexins
    • Beyer E.C., Gemel J., Seul K.H., Larson D.M., Banach K., and Brink P.R. Modulation of intercellular communication by differential regulation and heteromeric mixing of co-expressed connexins. Braz. J. Med. Biol. Res. 33 (2000) 391-397
    • (2000) Braz. J. Med. Biol. Res. , vol.33 , pp. 391-397
    • Beyer, E.C.1    Gemel, J.2    Seul, K.H.3    Larson, D.M.4    Banach, K.5    Brink, P.R.6
  • 17
    • 35748965595 scopus 로고    scopus 로고
    • Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane
    • Boassa D., Ambrosi C., Qiu F., Dahl G., Gaietta G., and Sosinsky G. Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane. J. Biol. Chem. 282 (2007) 31733-31743
    • (2007) J. Biol. Chem. , vol.282 , pp. 31733-31743
    • Boassa, D.1    Ambrosi, C.2    Qiu, F.3    Dahl, G.4    Gaietta, G.5    Sosinsky, G.6
  • 18
    • 0032813517 scopus 로고    scopus 로고
    • A genetic polymorphism in connexin 37 as a prognostic marker for atherosclerotic plaque development
    • Boerma M., Forsberg L., Van Zeijl L., Morgenstern R., De Faire U., Lemne C., et al. A genetic polymorphism in connexin 37 as a prognostic marker for atherosclerotic plaque development. J. Int. Med. 246 (1999) 211-218
    • (1999) J. Int. Med. , vol.246 , pp. 211-218
    • Boerma, M.1    Forsberg, L.2    Van Zeijl, L.3    Morgenstern, R.4    De Faire, U.5    Lemne, C.6
  • 19
    • 0026495809 scopus 로고
    • Intercellular propagation of calcium waves mediated by inositol trisphosphate
    • Boitano S., Dirksen E.R., and Sanderson M.J. Intercellular propagation of calcium waves mediated by inositol trisphosphate. Science 258 (1992) 292-295
    • (1992) Science , vol.258 , pp. 292-295
    • Boitano, S.1    Dirksen, E.R.2    Sanderson, M.J.3
  • 20
    • 0030697297 scopus 로고    scopus 로고
    • Evidence for heteromeric gap junction channels formed from rat connexin43 and human connexin37
    • Brink P.R., Cronin K., Banach K., Peterson E., Westphale E.M., Seul K.H., et al. Evidence for heteromeric gap junction channels formed from rat connexin43 and human connexin37. Am. J. Physiol. 273 (1997) C1386-C1396
    • (1997) Am. J. Physiol. , vol.273
    • Brink, P.R.1    Cronin, K.2    Banach, K.3    Peterson, E.4    Westphale, E.M.5    Seul, K.H.6
  • 22
    • 0027419412 scopus 로고
    • Connexin40, a component of gap junctions in vascular endothelium, is restricted in its ability to interact with other connexins
    • Bruzzone R., Haefliger J.A., Gimlich R.L., and Paul D.L. Connexin40, a component of gap junctions in vascular endothelium, is restricted in its ability to interact with other connexins. Mol. Biol. Cell 4 (1993) 7-20
    • (1993) Mol. Biol. Cell , vol.4 , pp. 7-20
    • Bruzzone, R.1    Haefliger, J.A.2    Gimlich, R.L.3    Paul, D.L.4
  • 23
    • 0037963497 scopus 로고    scopus 로고
    • Homocellular conduction along endothelium and smooth muscle of arterioles in hamster cheek pouch: unmasking an NO wave
    • Budel S., Bartlett I.S., and Segal S.S. Homocellular conduction along endothelium and smooth muscle of arterioles in hamster cheek pouch: unmasking an NO wave. Circ. Res. 93 (2003) 61-68
    • (2003) Circ. Res. , vol.93 , pp. 61-68
    • Budel, S.1    Bartlett, I.S.2    Segal, S.S.3
  • 24
    • 0028904228 scopus 로고
    • Heterotypic gap junction channels (connexin26-connexin32) violate the paradigm of unitary conductance
    • Bukauskas F.F., Elfgang C., Willecke K., and Weingart R. Heterotypic gap junction channels (connexin26-connexin32) violate the paradigm of unitary conductance. Pflugers Arch. 429 (1995) 870-872
    • (1995) Pflugers Arch. , vol.429 , pp. 870-872
    • Bukauskas, F.F.1    Elfgang, C.2    Willecke, K.3    Weingart, R.4
  • 25
    • 0034957206 scopus 로고    scopus 로고
    • Gating properties of gap junction channels assembled from connexin43 and connexin43 fused with green fluorescent protein
    • Bukauskas F.F., Bukauskiene A., Bennett M.V., and Verselis V.K. Gating properties of gap junction channels assembled from connexin43 and connexin43 fused with green fluorescent protein. Biophys. J. 81 (2001) 137-152
    • (2001) Biophys. J. , vol.81 , pp. 137-152
    • Bukauskas, F.F.1    Bukauskiene, A.2    Bennett, M.V.3    Verselis, V.K.4
  • 26
    • 33745458793 scopus 로고    scopus 로고
    • Properties of mouse connexin 30.2 and human connexin 31.9 hemichannels: implications for atrioventricular conduction in the heart
    • Bukauskas F.F., Kreuzberg M.M., Rackauskas M., Bukauskiene A., Bennett M.V., Verselis V.K., et al. Properties of mouse connexin 30.2 and human connexin 31.9 hemichannels: implications for atrioventricular conduction in the heart. Proc. Natl. Acad. Sci. USA 103 (2006) 9726-9731
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9726-9731
    • Bukauskas, F.F.1    Kreuzberg, M.M.2    Rackauskas, M.3    Bukauskiene, A.4    Bennett, M.V.5    Verselis, V.K.6
  • 27
    • 0033846942 scopus 로고    scopus 로고
    • Transplant atherosclerosis: role of phenotypic modulation of vascular smooth muscle by nitric oxide
    • Bundy R.E., Marczin N., Birks E.F., Chester A.H., and Yacoub M.H. Transplant atherosclerosis: role of phenotypic modulation of vascular smooth muscle by nitric oxide. Gen. Pharmacol. 34 (2000) 73-84
    • (2000) Gen. Pharmacol. , vol.34 , pp. 73-84
    • Bundy, R.E.1    Marczin, N.2    Birks, E.F.3    Chester, A.H.4    Yacoub, M.H.5
  • 29
  • 30
    • 0034975688 scopus 로고    scopus 로고
    • Connexin37, not Cx40 and Cx43, is induced in vascular smooth muscle cells during coronary arteriogenesis
    • Cai W.J., Koltai S., Kocsis E., Scholz D., Schaper W., and Schaper J. Connexin37, not Cx40 and Cx43, is induced in vascular smooth muscle cells during coronary arteriogenesis. J. Mol. Cell. Cardiol. 33 (2001) 957-967
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 957-967
    • Cai, W.J.1    Koltai, S.2    Kocsis, E.3    Scholz, D.4    Schaper, W.5    Schaper, J.6
  • 31
    • 4344700109 scopus 로고    scopus 로고
    • Presence of Cx37 and lack of desmin in smooth muscle cells are early markers for arteriogenesis
    • Cai W.J., Kocsis E., Scholz D., Luo X., Schaper W., and Schaper J. Presence of Cx37 and lack of desmin in smooth muscle cells are early markers for arteriogenesis. Mol. Cell. Biochem. 262 (2004) 17-23
    • (2004) Mol. Cell. Biochem. , vol.262 , pp. 17-23
    • Cai, W.J.1    Kocsis, E.2    Scholz, D.3    Luo, X.4    Schaper, W.5    Schaper, J.6
  • 34
    • 33745946267 scopus 로고    scopus 로고
    • Reduced connexin43 expression limits neointima formation after balloon distension injury in hypercholesterolemic mice
    • Chadjichristos C.E., Matter C.M., Roth I., Sutter E., Pelli G., Luscher T.F., et al. Reduced connexin43 expression limits neointima formation after balloon distension injury in hypercholesterolemic mice. Circulation 113 (2006) 2835-2843
    • (2006) Circulation , vol.113 , pp. 2835-2843
    • Chadjichristos, C.E.1    Matter, C.M.2    Roth, I.3    Sutter, E.4    Pelli, G.5    Luscher, T.F.6
  • 35
    • 41449115125 scopus 로고    scopus 로고
    • Targeting connexin 43 prevents platelet-derived growth factor-BB-induced phenotypic change in porcine coronary artery smooth muscle cells
    • Chadjichristos C.E., Morel S., Derouette J.P., Sutter E., Roth I., Brisset A.C., et al. Targeting connexin 43 prevents platelet-derived growth factor-BB-induced phenotypic change in porcine coronary artery smooth muscle cells. Circ. Res. 102 (2008) 653-660
    • (2008) Circ. Res. , vol.102 , pp. 653-660
    • Chadjichristos, C.E.1    Morel, S.2    Derouette, J.P.3    Sutter, E.4    Roth, I.5    Brisset, A.C.6
  • 36
    • 34447526059 scopus 로고    scopus 로고
    • Connexin37: a potential modifier gene of inflammatory disease
    • Chanson M., and Kwak B.R. Connexin37: a potential modifier gene of inflammatory disease. J. Mol. Med. 85 (2007) 787-795
    • (2007) J. Mol. Med. , vol.85 , pp. 787-795
    • Chanson, M.1    Kwak, B.R.2
  • 38
    • 77951644306 scopus 로고    scopus 로고
    • Pannexin protein expression in the rat middle cerebral artery
    • Chen J., Burns A.R., Phillips S.C., and Sokoya E.M. Pannexin protein expression in the rat middle cerebral artery. FASEB J. 22 (2008) 1144
    • (2008) FASEB J. , vol.22 , pp. 1144
    • Chen, J.1    Burns, A.R.2    Phillips, S.C.3    Sokoya, E.M.4
  • 40
    • 36048939780 scopus 로고    scopus 로고
    • Associations between connexin37 gene polymorphism and markers of subclinical atherosclerosis: the Cardiovascular Risk in Young Finns study
    • Collings A., Islam M.S., Juonala M., Rontu R., Kahonen M., Hutri-Kahonen N., et al. Associations between connexin37 gene polymorphism and markers of subclinical atherosclerosis: the Cardiovascular Risk in Young Finns study. Atherosclerosis 195 (2007) 379-384
    • (2007) Atherosclerosis , vol.195 , pp. 379-384
    • Collings, A.1    Islam, M.S.2    Juonala, M.3    Rontu, R.4    Kahonen, M.5    Hutri-Kahonen, N.6
  • 44
    • 0035195813 scopus 로고    scopus 로고
    • Heterotypic gap junction channel formation between heteromeric and homomeric Cx40 and Cx43 connexons
    • Cottrell G.T., and Burt J.M. Heterotypic gap junction channel formation between heteromeric and homomeric Cx40 and Cx43 connexons. Am. J. Physiol. Cell Physiol. 281 (2001) C1559-C1567
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Cottrell, G.T.1    Burt, J.M.2
  • 45
    • 0036083484 scopus 로고    scopus 로고
    • Cx40 and Cx43 expression ratio influences heteromeric/heterotypic gap junction channel properties
    • Cottrell G.T., Wu Y., and Burt J.M. Cx40 and Cx43 expression ratio influences heteromeric/heterotypic gap junction channel properties. Am. J. Physiol. Cell Physiol. 282 (2002) C1469-C1482
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Cottrell, G.T.1    Wu, Y.2    Burt, J.M.3
  • 46
    • 0038724475 scopus 로고    scopus 로고
    • Dynamic changes in connexin expression correlate with key events in the wound healing process
    • Coutinho P., Qiu C., Frank S., Tamber K., and Becker D. Dynamic changes in connexin expression correlate with key events in the wound healing process. Cell Biol. Int. 27 (2003) 525-541
    • (2003) Cell Biol. Int. , vol.27 , pp. 525-541
    • Coutinho, P.1    Qiu, C.2    Frank, S.3    Tamber, K.4    Becker, D.5
  • 47
    • 42149157824 scopus 로고    scopus 로고
    • Gap junction-mimetic peptides do work, but in unexpected ways
    • Dahl G. Gap junction-mimetic peptides do work, but in unexpected ways. Cell Commun. Adhes. 14 (2007) 259-264
    • (2007) Cell Commun. Adhes. , vol.14 , pp. 259-264
    • Dahl, G.1
  • 49
    • 6944244066 scopus 로고    scopus 로고
    • Distinct endothelial phenotypes evoked by arterial waveforms derived from atherosclerosis-susceptible and -resistant regions of human vasculature
    • Dai G., Kaazempur-Mofrad M.R., Natarajan S., Zhang Y., Vaughn S., Blackman B.R., et al. Distinct endothelial phenotypes evoked by arterial waveforms derived from atherosclerosis-susceptible and -resistant regions of human vasculature. Proc. Natl. Acad. Sci. USA 101 (2004) 14871-14876
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14871-14876
    • Dai, G.1    Kaazempur-Mofrad, M.R.2    Natarajan, S.3    Zhang, Y.4    Vaughn, S.5    Blackman, B.R.6
  • 52
    • 30644473750 scopus 로고    scopus 로고
    • Endothelial mediators and communication through vascular gap junctions
    • de Wit C., Hoepfl B., and Wolfle S.E. Endothelial mediators and communication through vascular gap junctions. Biol. Chem. 387 (2006) 3-9
    • (2006) Biol. Chem. , vol.387 , pp. 3-9
    • de Wit, C.1    Hoepfl, B.2    Wolfle, S.E.3
  • 53
    • 33744461864 scopus 로고    scopus 로고
    • Connexin-dependent communication within the vascular wall: contribution to the control of arteriolar diameter
    • de Wit C., Wolfle S.E., and Hopfl B. Connexin-dependent communication within the vascular wall: contribution to the control of arteriolar diameter. Adv. Cardiol. 42 (2006) 268-283
    • (2006) Adv. Cardiol. , vol.42 , pp. 268-283
    • de Wit, C.1    Wolfle, S.E.2    Hopfl, B.3
  • 54
    • 20444482880 scopus 로고    scopus 로고
    • Increased connexin43 expression in human saphenous veins in culture is associated with intimal hyperplasia
    • Deglise S., Martin D., Probst H., Saucy F., Hayoz D., Waeber G., et al. Increased connexin43 expression in human saphenous veins in culture is associated with intimal hyperplasia. J. Vasc. Surg. 41 (2005) 1043-1052
    • (2005) J. Vasc. Surg. , vol.41 , pp. 1043-1052
    • Deglise, S.1    Martin, D.2    Probst, H.3    Saucy, F.4    Hayoz, D.5    Waeber, G.6
  • 55
    • 1942470893 scopus 로고    scopus 로고
    • Structural bases for the chemical regulation of connexin43 channels
    • Delmar M., Coombs W., Sorgen P., Duffy H.S., and Taffet S.M. Structural bases for the chemical regulation of connexin43 channels. Cardiovasc. Res. 62 (2004) 268-275
    • (2004) Cardiovasc. Res. , vol.62 , pp. 268-275
    • Delmar, M.1    Coombs, W.2    Sorgen, P.3    Duffy, H.S.4    Taffet, S.M.5
  • 57
    • 3442896550 scopus 로고    scopus 로고
    • Cardiac connexins Cx43 and Cx45: formation of diverse gap junction channels with diverse electrical properties
    • Desplantez T., Halliday D., Dupont E., and Weingart R. Cardiac connexins Cx43 and Cx45: formation of diverse gap junction channels with diverse electrical properties. Pflugers Arch. 448 (2004) 363-375
    • (2004) Pflugers Arch. , vol.448 , pp. 363-375
    • Desplantez, T.1    Halliday, D.2    Dupont, E.3    Weingart, R.4
  • 58
    • 0000039665 scopus 로고
    • A study of the structure and distribution of the nexus
    • Dewey M.M., and Barr L. A study of the structure and distribution of the nexus. J. Cell Biol. 23 (1964) 553-585
    • (1964) J. Cell Biol. , vol.23 , pp. 553-585
    • Dewey, M.M.1    Barr, L.2
  • 59
    • 0030998442 scopus 로고    scopus 로고
    • Elevation of intracellular calcium in smooth muscle causes endothelial cell generation of NO in arterioles
    • Dora K.A., Doyle M.P., and Duling B.R. Elevation of intracellular calcium in smooth muscle causes endothelial cell generation of NO in arterioles. Proc. Natl. Acad. Sci. USA 94 (1997) 6529-6534
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6529-6534
    • Dora, K.A.1    Doyle, M.P.2    Duling, B.R.3
  • 60
    • 0037183978 scopus 로고    scopus 로고
    • pH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains
    • Duffy H.S., Sorgen P.L., Girvin M.E., O'Donnell P., Coombs W., Taffet S.M., et al. pH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains. J. Biol. Chem. 277 (2002) 36706-36714
    • (2002) J. Biol. Chem. , vol.277 , pp. 36706-36714
    • Duffy, H.S.1    Sorgen, P.L.2    Girvin, M.E.3    O'Donnell, P.4    Coombs, W.5    Taffet, S.M.6
  • 62
    • 30944460666 scopus 로고    scopus 로고
    • Phylogenetic analysis of three complete gap junction gene families reveals lineage-specific duplications and highly supported gene classes
    • Eastman S.D., Chen T.H., Falk M.M., Mendelson T.C., and Iovine M.K. Phylogenetic analysis of three complete gap junction gene families reveals lineage-specific duplications and highly supported gene classes. Genomics 87 (2006) 265-274
    • (2006) Genomics , vol.87 , pp. 265-274
    • Eastman, S.D.1    Chen, T.H.2    Falk, M.M.3    Mendelson, T.C.4    Iovine, M.K.5
  • 63
    • 33646406552 scopus 로고    scopus 로고
    • Flow regulates intercellular communication in HAEC by assembling functional Cx40 and Cx37 gap junctional channels
    • Ebong E.E., Kim S., and DePaola N. Flow regulates intercellular communication in HAEC by assembling functional Cx40 and Cx37 gap junctional channels. Am. J. Physiol. Heart Circ. Physiol. 290 (2006) H2015-H2023
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , vol.290
    • Ebong, E.E.1    Kim, S.2    DePaola, N.3
  • 64
    • 33746566071 scopus 로고    scopus 로고
    • Selectivity of connexin 43 channels is regulated through protein kinase C-dependent phosphorylation
    • Ek-Vitorin J.F., King T.J., Heyman N.S., Lampe P.D., and Burt J.M. Selectivity of connexin 43 channels is regulated through protein kinase C-dependent phosphorylation. Circ. Res. 98 (2006) 1498-1505
    • (2006) Circ. Res. , vol.98 , pp. 1498-1505
    • Ek-Vitorin, J.F.1    King, T.J.2    Heyman, N.S.3    Lampe, P.D.4    Burt, J.M.5
  • 65
    • 0034859346 scopus 로고    scopus 로고
    • Heterotypic docking of Cx43 and Cx45 connexons blocks fast voltage gating of Cx43
    • Elenes S., Martinez A.D., Delmar M., Beyer E.C., and Moreno A.P. Heterotypic docking of Cx43 and Cx45 connexons blocks fast voltage gating of Cx43. Biophys. J. 81 (2001) 1406-1418
    • (2001) Biophys. J. , vol.81 , pp. 1406-1418
    • Elenes, S.1    Martinez, A.D.2    Delmar, M.3    Beyer, E.C.4    Moreno, A.P.5
  • 66
    • 0028915946 scopus 로고
    • Specific permeability and selective formation of gap junction channels in connexin-transfected HeLa cells
    • Elfgang C., Eckert R., Lichtenberg-Frate H., Butterweck A., Traub O., Klein R.A., et al. Specific permeability and selective formation of gap junction channels in connexin-transfected HeLa cells. J. Cell Biol. 129 (1995) 805-817
    • (1995) J. Cell Biol. , vol.129 , pp. 805-817
    • Elfgang, C.1    Eckert, R.2    Lichtenberg-Frate, H.3    Butterweck, A.4    Traub, O.5    Klein, R.A.6
  • 67
    • 0030220781 scopus 로고    scopus 로고
    • Expression of zebrafish connexin43.4 in the notochord and tail bud of wild-type and mutant no tail embryos
    • Essner J.J., Laing J.G., Beyer E.C., Johnson R.G., and Hackett Jr. P.B. Expression of zebrafish connexin43.4 in the notochord and tail bud of wild-type and mutant no tail embryos. Dev. Biol. 177 (1996) 449-462
    • (1996) Dev. Biol. , vol.177 , pp. 449-462
    • Essner, J.J.1    Laing, J.G.2    Beyer, E.C.3    Johnson, R.G.4    Hackett Jr., P.B.5
  • 68
    • 42149125581 scopus 로고    scopus 로고
    • Mimetic peptides as blockers of connexin channel-facilitated intercellular communication
    • Evans W.H., and Leybaert L. Mimetic peptides as blockers of connexin channel-facilitated intercellular communication. Cell Commun. Adhes. 14 (2007) 265-273
    • (2007) Cell Commun. Adhes. , vol.14 , pp. 265-273
    • Evans, W.H.1    Leybaert, L.2
  • 69
    • 0035991948 scopus 로고    scopus 로고
    • Gap junctions: structure and function
    • Evans W.H., and Martin P.E. Gap junctions: structure and function. Mol. Membr. Biol. 19 (2002) 121-136
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 121-136
    • Evans, W.H.1    Martin, P.E.2
  • 70
    • 33745528139 scopus 로고    scopus 로고
    • The gap junction cellular internet: connexin hemichannels enter the signalling limelight
    • Evans W.H., De Vuyst E., and Leybaert L. The gap junction cellular internet: connexin hemichannels enter the signalling limelight. Biochem. J. 397 (2006) 1-14
    • (2006) Biochem. J. , vol.397 , pp. 1-14
    • Evans, W.H.1    De Vuyst, E.2    Leybaert, L.3
  • 71
    • 50949116679 scopus 로고    scopus 로고
    • ATP release from vascular endothelia occurs across Cx43 hemichannels and is attenuated during hypoxia
    • Faigle M., Seessle J., Zug S., El Kasmi K.C., and Eltzschig H.K. ATP release from vascular endothelia occurs across Cx43 hemichannels and is attenuated during hypoxia. PLoS ONE 3 (2008) e2801
    • (2008) PLoS ONE , vol.3
    • Faigle, M.1    Seessle, J.2    Zug, S.3    El Kasmi, K.C.4    Eltzschig, H.K.5
  • 72
    • 0032478623 scopus 로고    scopus 로고
    • Connexin membrane protein biosynthesis is influenced by polypeptide positioning within the translocon and signal peptidase access
    • Falk M.M., and Gilula N.B. Connexin membrane protein biosynthesis is influenced by polypeptide positioning within the translocon and signal peptidase access. J. Biol. Chem. 273 (1998) 7856-7864
    • (1998) J. Biol. Chem. , vol.273 , pp. 7856-7864
    • Falk, M.M.1    Gilula, N.B.2
  • 73
    • 0031001091 scopus 로고    scopus 로고
    • Cell-free synthesis and assembly of connexins into functional gap junction membrane channels
    • Falk M.M., Buehler L.K., Kumar N.M., and Gilula N.B. Cell-free synthesis and assembly of connexins into functional gap junction membrane channels. EMBO J. 16 (1997) 2703-2716
    • (1997) EMBO J. , vol.16 , pp. 2703-2716
    • Falk, M.M.1    Buehler, L.K.2    Kumar, N.M.3    Gilula, N.B.4
  • 74
    • 52449111898 scopus 로고    scopus 로고
    • GRP78 upregulation by atheroprone shear stress via p38-, alpha2beta1-dependent mechanism in endothelial cells
    • Feaver R.E., Hastings N.E., Pryor A., and Blackman B.R. GRP78 upregulation by atheroprone shear stress via p38-, alpha2beta1-dependent mechanism in endothelial cells. Arterioscler. Thromb. Vasc. Biol. 28 (2008) 1534-1541
    • (2008) Arterioscler. Thromb. Vasc. Biol. , vol.28 , pp. 1534-1541
    • Feaver, R.E.1    Hastings, N.E.2    Pryor, A.3    Blackman, B.R.4
  • 75
    • 57049098245 scopus 로고    scopus 로고
    • Dissection of two Cx37-independent conducted vasodilator mechanisms by deletion of Cx40: electrotonic versus regenerative conduction
    • Figueroa X.F., and Duling B.R. Dissection of two Cx37-independent conducted vasodilator mechanisms by deletion of Cx40: electrotonic versus regenerative conduction. Am. J. Physiol. Heart Circ. Physiol. 295 (2008) H2001-H2007
    • (2008) Am. J. Physiol. Heart Circ. Physiol. , vol.295
    • Figueroa, X.F.1    Duling, B.R.2
  • 76
    • 58149100084 scopus 로고    scopus 로고
    • Gap junctions in the control of vascular function
    • Figueroa X.F., and Duling B.R. Gap junctions in the control of vascular function. Antioxid. Redox Signal. 11 (2009) 251-266
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 251-266
    • Figueroa, X.F.1    Duling, B.R.2
  • 77
    • 0344490336 scopus 로고    scopus 로고
    • Central role of connexin40 in the propagation of electrically activated vasodilation in mouse cremasteric arterioles in vivo
    • Figueroa X.F., Paul D.L., Simon A.M., Goodenough D.A., Day K.H., Damon D.N., et al. Central role of connexin40 in the propagation of electrically activated vasodilation in mouse cremasteric arterioles in vivo. Circ. Res. 92 (2003) 793-800
    • (2003) Circ. Res. , vol.92 , pp. 793-800
    • Figueroa, X.F.1    Paul, D.L.2    Simon, A.M.3    Goodenough, D.A.4    Day, K.H.5    Damon, D.N.6
  • 78
    • 8144225088 scopus 로고    scopus 로고
    • Connexins: gaps in our knowledge of vascular function
    • Figueroa X.F., Isakson B.E., and Duling B.R. Connexins: gaps in our knowledge of vascular function. Physiology 19 (2004) 277-284
    • (2004) Physiology , vol.19 , pp. 277-284
    • Figueroa, X.F.1    Isakson, B.E.2    Duling, B.R.3
  • 79
    • 4644228547 scopus 로고    scopus 로고
    • A Calpha model for the transmembrane alpha helices of gap junction intercellular channels
    • Fleishman S.J., Unger V.M., Yeager M., and Ben-Tal N. A Calpha model for the transmembrane alpha helices of gap junction intercellular channels. Mol. Cell 15 (2004) 879-888
    • (2004) Mol. Cell , vol.15 , pp. 879-888
    • Fleishman, S.J.1    Unger, V.M.2    Yeager, M.3    Ben-Tal, N.4
  • 81
    • 0032556026 scopus 로고    scopus 로고
    • Connexin43 is highly localized to sites of disturbed flow in rat aortic endothelium but connexin37 and connexin40 are more uniformly distributed
    • Gabriels J.E., and Paul D.L. Connexin43 is highly localized to sites of disturbed flow in rat aortic endothelium but connexin37 and connexin40 are more uniformly distributed. Circ. Res. 83 (1998) 636-643
    • (1998) Circ. Res. , vol.83 , pp. 636-643
    • Gabriels, J.E.1    Paul, D.L.2
  • 82
    • 0037134035 scopus 로고    scopus 로고
    • Multicolor and electron microscopic imaging of connexin trafficking
    • Gaietta G., Deerinck T.J., Adams S.R., Bouwer J., Tour O., Laird D.W., et al. Multicolor and electron microscopic imaging of connexin trafficking. Science 296 (2002) 503-507
    • (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
  • 83
    • 3042737001 scopus 로고    scopus 로고
    • Connexin43 and connexin26 form gap junctions, but not heteromeric channels in co-expressing cells
    • Gemel J., Valiunas V., Brink P., and Beyer E. Connexin43 and connexin26 form gap junctions, but not heteromeric channels in co-expressing cells. J. Cell Sci. 117 (2004) 2469-2490
    • (2004) J. Cell Sci. , vol.117 , pp. 2469-2490
    • Gemel, J.1    Valiunas, V.2    Brink, P.3    Beyer, E.4
  • 84
    • 0033605658 scopus 로고    scopus 로고
    • Intracellular trafficking pathways in the assembly of connexins into gap junctions
    • George C.H., Kendall J.M., and Evans W.H. Intracellular trafficking pathways in the assembly of connexins into gap junctions. J. Biol. Chem. 274 (1999) 8678-8685
    • (1999) J. Biol. Chem. , vol.274 , pp. 8678-8685
    • George, C.H.1    Kendall, J.M.2    Evans, W.H.3
  • 85
    • 1942503184 scopus 로고    scopus 로고
    • Gap junctions and connexin-interacting proteins
    • Giepmans B.N. Gap junctions and connexin-interacting proteins. Cardiovasc. Res. 62 (2004) 233-245
    • (2004) Cardiovasc. Res. , vol.62 , pp. 233-245
    • Giepmans, B.N.1
  • 86
    • 0037184068 scopus 로고    scopus 로고
    • Gap junctions between cells expressing connexin 43 or 32 show inverse permselectivity to adenosine and ATP
    • Goldberg G.S., Moreno A.P., and Lampe P.D. Gap junctions between cells expressing connexin 43 or 32 show inverse permselectivity to adenosine and ATP. J. Biol. Chem. 277 (2002) 36725-36730
    • (2002) J. Biol. Chem. , vol.277 , pp. 36725-36730
    • Goldberg, G.S.1    Moreno, A.P.2    Lampe, P.D.3
  • 87
    • 0030013202 scopus 로고    scopus 로고
    • Connexins, connexons, and intercellular communication
    • Goodenough D.A., Goliger J.A., and Paul D.L. Connexins, connexons, and intercellular communication. Annu. Rev. Biochem. 65 (1996) 475-502
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 475-502
    • Goodenough, D.A.1    Goliger, J.A.2    Paul, D.L.3
  • 88
    • 0034716923 scopus 로고    scopus 로고
    • Coexpression of connexins 40 and 43 enhances the pH sensitivity of gap junctions: a model for synergistic interactions among connexins
    • Gu H., Ek-Vitorin J.F., Taffet S.M., and Delmar M. Coexpression of connexins 40 and 43 enhances the pH sensitivity of gap junctions: a model for synergistic interactions among connexins. Circ. Res. 86 (2000) E98-E103
    • (2000) Circ. Res. , vol.86
    • Gu, H.1    Ek-Vitorin, J.F.2    Taffet, S.M.3    Delmar, M.4
  • 90
    • 0034957254 scopus 로고    scopus 로고
    • Connexins 40 and 43 are differentially regulated within the kidneys of rats with renovascular hypertension
    • Haefliger J.A., Demotz S., Braissant O., Suter E., Waeber B., Nicod P., et al. Connexins 40 and 43 are differentially regulated within the kidneys of rats with renovascular hypertension. Kidney Int. 60 (2001) 190-201
    • (2001) Kidney Int. , vol.60 , pp. 190-201
    • Haefliger, J.A.1    Demotz, S.2    Braissant, O.3    Suter, E.4    Waeber, B.5    Nicod, P.6
  • 91
    • 1942470625 scopus 로고    scopus 로고
    • Contribution of connexins to the function of the vascular wall
    • Haefliger J.A., Nicod P., and Meda P. Contribution of connexins to the function of the vascular wall. Cardiovasc. Res. 62 (2004) 345-356
    • (2004) Cardiovasc. Res. , vol.62 , pp. 345-356
    • Haefliger, J.A.1    Nicod, P.2    Meda, P.3
  • 93
    • 49249090855 scopus 로고    scopus 로고
    • Connexin isoform expression in smooth muscle cells and endothelial cells of hamster cheek pouch arterioles and retractor feed arteries
    • Hakim C.H., Jackson W.F., and Segal S.S. Connexin isoform expression in smooth muscle cells and endothelial cells of hamster cheek pouch arterioles and retractor feed arteries. Microcirculation 15 (2008) 503-514
    • (2008) Microcirculation , vol.15 , pp. 503-514
    • Hakim, C.H.1    Jackson, W.F.2    Segal, S.S.3
  • 94
    • 0035704411 scopus 로고    scopus 로고
    • Emerging issues of connexin channels: biophysics fills the gap
    • Harris A.L. Emerging issues of connexin channels: biophysics fills the gap. Q. Rev. Biophys. 34 (2001) 325-472
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 325-472
    • Harris, A.L.1
  • 96
    • 0034625245 scopus 로고    scopus 로고
    • Mechanism and selectivity of the effects of halothane on gap junction channel function
    • He D.S., and Burt J.M. Mechanism and selectivity of the effects of halothane on gap junction channel function. Circ. Res. 86 (2000) E104-E109
    • (2000) Circ. Res. , vol.86
    • He, D.S.1    Burt, J.M.2
  • 97
    • 0001203743 scopus 로고    scopus 로고
    • Formation of heteromeric gap junction channels by connexins 40 and 43 in vascular smooth muscle cells
    • He D.S., Jiang J.X., Taffet S.M., and Burt J.M. Formation of heteromeric gap junction channels by connexins 40 and 43 in vascular smooth muscle cells. Proc. Natl. Acad. Sci. USA 96 (1999) 6495-6500
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6495-6500
    • He, D.S.1    Jiang, J.X.2    Taffet, S.M.3    Burt, J.M.4
  • 98
    • 67650308876 scopus 로고    scopus 로고
    • The myoendothelial junction: breaking through the matrix?
    • Heberlein K.R., Straub A.C., and Isakson B.E. The myoendothelial junction: breaking through the matrix?. Microcirculation 16 (2009) 307-322
    • (2009) Microcirculation , vol.16 , pp. 307-322
    • Heberlein, K.R.1    Straub, A.C.2    Isakson, B.E.3
  • 99
    • 0026776750 scopus 로고
    • Molecular cloning and functional expression of mouse connexin40, a second gap junction gene preferentially expressed in lung
    • Hennemann H., Suchyna T., Lichtenberg-Frate H., Jungbluth S., Dahl E., Schwarz J., et al. Molecular cloning and functional expression of mouse connexin40, a second gap junction gene preferentially expressed in lung. J. Cell Biol. 117 (1992) 1299-1310
    • (1992) J. Cell Biol. , vol.117 , pp. 1299-1310
    • Hennemann, H.1    Suchyna, T.2    Lichtenberg-Frate, H.3    Jungbluth, S.4    Dahl, E.5    Schwarz, J.6
  • 100
    • 33744473829 scopus 로고    scopus 로고
    • Pharmacology of cardiovascular gap junctions
    • Herve J.C., and Dhein S. Pharmacology of cardiovascular gap junctions. Adv. Cardiol. 42 (2006) 107-131
    • (2006) Adv. Cardiol. , vol.42 , pp. 107-131
    • Herve, J.C.1    Dhein, S.2
  • 101
    • 20044369560 scopus 로고    scopus 로고
    • Connexin-made channels as pharmacological targets
    • Herve J.C., and Sarrouilhe D. Connexin-made channels as pharmacological targets. Curr. Pharm. Des. 11 (2005) 1941-1958
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 1941-1958
    • Herve, J.C.1    Sarrouilhe, D.2
  • 102
    • 38549177905 scopus 로고    scopus 로고
    • Hindered diffusion through an aqueous pore describes invariant dye selectivity of Cx43 junctions
    • Heyman N.S., and Burt J.M. Hindered diffusion through an aqueous pore describes invariant dye selectivity of Cx43 junctions. Biophys. J. 94 (2008) 840-854
    • (2008) Biophys. J. , vol.94 , pp. 840-854
    • Heyman, N.S.1    Burt, J.M.2
  • 103
    • 0035173328 scopus 로고    scopus 로고
    • Heterogeneous control of blood flow amongst different vascular beds
    • Hill C.E., Phillips J.K., and Sandow S.L. Heterogeneous control of blood flow amongst different vascular beds. Med. Res. Rev. 21 (2001) 1-60
    • (2001) Med. Res. Rev. , vol.21 , pp. 1-60
    • Hill, C.E.1    Phillips, J.K.2    Sandow, S.L.3
  • 104
    • 34548304825 scopus 로고    scopus 로고
    • Functional rescue of elastin insufficiency in mice by the human elastin gene: implications for mouse models of human disease
    • Hirano E., Knutsen R.H., Sugitani H., Ciliberto C.H., and Mecham R.P. Functional rescue of elastin insufficiency in mice by the human elastin gene: implications for mouse models of human disease. Circ. Res. 101 (2007) 523-531
    • (2007) Circ. Res. , vol.101 , pp. 523-531
    • Hirano, E.1    Knutsen, R.H.2    Sugitani, H.3    Ciliberto, C.H.4    Mecham, R.P.5
  • 105
    • 0242627404 scopus 로고    scopus 로고
    • Nitric oxide enhances de novo formation of endothelial gap junctions
    • Hoffmann A., Gloe T., Pohl U., and Zahler S. Nitric oxide enhances de novo formation of endothelial gap junctions. Cardiovasc. Res. 60 (2003) 421-430
    • (2003) Cardiovasc. Res. , vol.60 , pp. 421-430
    • Hoffmann, A.1    Gloe, T.2    Pohl, U.3    Zahler, S.4
  • 106
    • 77049198073 scopus 로고
    • Role of the cell membrane and mitochondria in the phenomenon of ion transport in cardiac muscle
    • Holland W.C., and Dunn C.E. Role of the cell membrane and mitochondria in the phenomenon of ion transport in cardiac muscle. Am. J. Physiol. 179 (1954) 486-490
    • (1954) Am. J. Physiol. , vol.179 , pp. 486-490
    • Holland, W.C.1    Dunn, C.E.2
  • 107
    • 47249142934 scopus 로고    scopus 로고
    • Diabetes reduces aortic endothelial gap junctions in ApoE-deficient mice: simvastatin exacerbates the reduction
    • Hou C.J., Tsai C.H., Su C.H., Wu Y.J., Chen S.J., Chiu J.J., et al. Diabetes reduces aortic endothelial gap junctions in ApoE-deficient mice: simvastatin exacerbates the reduction. J. Histochem. Cytochem. 56 (2008) 745-752
    • (2008) J. Histochem. Cytochem. , vol.56 , pp. 745-752
    • Hou, C.J.1    Tsai, C.H.2    Su, C.H.3    Wu, Y.J.4    Chen, S.J.5    Chiu, J.J.6
  • 108
    • 33646137561 scopus 로고    scopus 로고
    • Conductance of connexin hemichannels segregates with the first transmembrane segment
    • Hu X., Ma M., and Dahl G. Conductance of connexin hemichannels segregates with the first transmembrane segment. Biophys. J. 90 (2006) 140-150
    • (2006) Biophys. J. , vol.90 , pp. 140-150
    • Hu, X.1    Ma, M.2    Dahl, G.3
  • 109
    • 0035146667 scopus 로고    scopus 로고
    • Functional rescue of defective mutant connexons by pairing with wild-type connexons
    • Hulser D.F., Rutz M.L., Eckert R., and Traub O. Functional rescue of defective mutant connexons by pairing with wild-type connexons. Pflugers Arch. Eur. J. Physiol. 441 (2001) 521-528
    • (2001) Pflugers Arch. Eur. J. Physiol. , vol.441 , pp. 521-528
    • Hulser, D.F.1    Rutz, M.L.2    Eckert, R.3    Traub, O.4
  • 110
    • 28644434657 scopus 로고    scopus 로고
    • Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion
    • Hunter A.W., Barker R.J., Zhu C., and Gourdie R.G. Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion. Mol. Biol. Cell 16 (2005) 5686-5698
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5686-5698
    • Hunter, A.W.1    Barker, R.J.2    Zhu, C.3    Gourdie, R.G.4
  • 111
    • 0342948933 scopus 로고    scopus 로고
    • Heterogeneous localization of connexin40 in the renal vasculature
    • Hwan Seul K., and Beyer E.C. Heterogeneous localization of connexin40 in the renal vasculature. Microvasc. Res. 59 (2000) 140-148
    • (2000) Microvasc. Res. , vol.59 , pp. 140-148
    • Hwan Seul, K.1    Beyer, E.C.2
  • 113
    • 0034997332 scopus 로고    scopus 로고
    • 2+ signaling in alveolar epithelial cells through gap junctions and by extracellular ATP
    • 2+ signaling in alveolar epithelial cells through gap junctions and by extracellular ATP. Am. J. Physiol. Lung Cell. Mol. Physiol. 280 (2001) L221-L228
    • (2001) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.280
    • Isakson, B.E.1
  • 114
    • 59149101575 scopus 로고    scopus 로고
    • 2+ communication
    • 2+ communication. J. Cell Sci. 121 (2008) 3664-3673
    • (2008) J. Cell Sci. , vol.121 , pp. 3664-3673
    • Isakson, B.E.1
  • 115
    • 22144479749 scopus 로고    scopus 로고
    • Heterocellular contact at the myoendothelial junction influences gap junction organization
    • Isakson B.E., and Duling B.R. Heterocellular contact at the myoendothelial junction influences gap junction organization. Circ. Res. 97 (2005) 44-51
    • (2005) Circ. Res. , vol.97 , pp. 44-51
    • Isakson, B.E.1    Duling, B.R.2
  • 117
    • 33749068711 scopus 로고    scopus 로고
    • Oxidized phospholipids alter vascular connexin expression, phosphorylation, and heterocellular communication
    • Isakson B.E., Kronke G., Kadl A., Leitinger N., and Duling B.R. Oxidized phospholipids alter vascular connexin expression, phosphorylation, and heterocellular communication. Arterioscler. Thromb. Vasc. Biol. 26 (2006) 2216-2221
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 2216-2221
    • Isakson, B.E.1    Kronke, G.2    Kadl, A.3    Leitinger, N.4    Duling, B.R.5
  • 118
    • 33846844784 scopus 로고    scopus 로고
    • 2+ and inositol 1, 4, 5-trisphosphate-mediated signaling across the myoendothelial junction
    • 2+ and inositol 1, 4, 5-trisphosphate-mediated signaling across the myoendothelial junction. Circ. Res. 100 (2007) 246-254
    • (2007) Circ. Res. , vol.100 , pp. 246-254
    • Isakson, B.E.1    Ramos, S.I.2    Duling, B.R.3
  • 119
    • 49249110266 scopus 로고    scopus 로고
    • Incidence of protein on actin bridges between endothelium and smooth muscle in arterioles demonstrates heterogeneous connexin expression and phosphorylation
    • Isakson B.E., Best A.K., and Duling B.R. Incidence of protein on actin bridges between endothelium and smooth muscle in arterioles demonstrates heterogeneous connexin expression and phosphorylation. Am. J. Physiol. Heart Circ. Physiol. 294 (2008) H2898-H2904
    • (2008) Am. J. Physiol. Heart Circ. Physiol. , vol.294
    • Isakson, B.E.1    Best, A.K.2    Duling, B.R.3
  • 120
    • 35148873636 scopus 로고    scopus 로고
    • Endothelial connexin 37, connexin 40, and connexin 43 respond uniquely to substrate and shear stress
    • Johnson T.L., and Nerem R.M. Endothelial connexin 37, connexin 40, and connexin 43 respond uniquely to substrate and shear stress. Endothelium 14 (2007) 215-226
    • (2007) Endothelium , vol.14 , pp. 215-226
    • Johnson, T.L.1    Nerem, R.M.2
  • 121
  • 122
    • 67649739081 scopus 로고    scopus 로고
    • Connexin 40 mediates the tubuloglomerular feedback contribution to renal blood flow autoregulation
    • Just A., Kurtz L., de Wit C., Wagner C., Kurtz A., and Arendshorst W.J. Connexin 40 mediates the tubuloglomerular feedback contribution to renal blood flow autoregulation. J. Am. Soc. Nephrol. 20 (2009) 1577-1585
    • (2009) J. Am. Soc. Nephrol. , vol.20 , pp. 1577-1585
    • Just, A.1    Kurtz, L.2    de Wit, C.3    Wagner, C.4    Kurtz, A.5    Arendshorst, W.J.6
  • 124
    • 14744275510 scopus 로고    scopus 로고
    • Nitric oxide specifically reduces the permeability of Cx37-containing gap junctions to small molecules
    • Kameritsch P., Khandoga N., Nagel W., Hundhausen C., Lidington D., and Pohl U. Nitric oxide specifically reduces the permeability of Cx37-containing gap junctions to small molecules. J. Cell. Physiol. 203 (2005) 233-242
    • (2005) J. Cell. Physiol. , vol.203 , pp. 233-242
    • Kameritsch, P.1    Khandoga, N.2    Nagel, W.3    Hundhausen, C.4    Lidington, D.5    Pohl, U.6
  • 126
    • 0035823043 scopus 로고    scopus 로고
    • Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells
    • Kausalya P.J., Reichert M., and Hunziker W. Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells. FEBS Lett. 505 (2001) 92-96
    • (2001) FEBS Lett. , vol.505 , pp. 92-96
    • Kausalya, P.J.1    Reichert, M.2    Hunziker, W.3
  • 127
    • 0032934609 scopus 로고    scopus 로고
    • Connexin make-up of endothelial gap junctions in the rat pulmonary artery as revealed by immunoconfocal microscopy and triple-label immunogold electron microscopy
    • Ko Y.S., Yeh H.I., Rothery S., Dupont E., Coppen S.R., and Severs N.J. Connexin make-up of endothelial gap junctions in the rat pulmonary artery as revealed by immunoconfocal microscopy and triple-label immunogold electron microscopy. J. Histochem. Cytochem. 47 (1999) 683-692
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 683-692
    • Ko, Y.S.1    Yeh, H.I.2    Rothery, S.3    Dupont, E.4    Coppen, S.R.5    Severs, N.J.6
  • 129
    • 33644826498 scopus 로고    scopus 로고
    • Pathways and control of connexin oligomerization
    • Koval M. Pathways and control of connexin oligomerization. Trends Cell Biol. 16 (2006) 159-166
    • (2006) Trends Cell Biol. , vol.16 , pp. 159-166
    • Koval, M.1
  • 131
    • 0036244808 scopus 로고    scopus 로고
    • Altered dye diffusion and upregulation of connexin37 in mouse aortic endothelium deficient in connexin40
    • Kruger O., Beny J.L., Chabaud F., Traub O., Theis M., Brix K., et al. Altered dye diffusion and upregulation of connexin37 in mouse aortic endothelium deficient in connexin40. J. Vasc. Res. 39 (2002) 160-172
    • (2002) J. Vasc. Res. , vol.39 , pp. 160-172
    • Kruger, O.1    Beny, J.L.2    Chabaud, F.3    Traub, O.4    Theis, M.5    Brix, K.6
  • 134
    • 34047207791 scopus 로고    scopus 로고
    • Lack of connexin 40 causes displacement of renin-producing cells from afferent arterioles to the extraglomerular mesangium
    • Kurtz L., Schweda F., de Wit C., Kriz W., Witzgall R., Warth R., et al. Lack of connexin 40 causes displacement of renin-producing cells from afferent arterioles to the extraglomerular mesangium. J. Am. Soc. Nephrol. 18 (2007) 1103-1111
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 1103-1111
    • Kurtz, L.1    Schweda, F.2    de Wit, C.3    Kriz, W.4    Witzgall, R.5    Warth, R.6
  • 135
    • 68049094115 scopus 로고    scopus 로고
    • Replacement of Cx40 by Cx45 causes ectopic localization of renin-producing cells in the kidney but maintains the in vivo control of renin gene expression
    • Kurtz L., Gerl M., Kriz W., Wagner C., and Kurtz A. Replacement of Cx40 by Cx45 causes ectopic localization of renin-producing cells in the kidney but maintains the in vivo control of renin gene expression. Am. J. Physiol. Renal Physiol. 297 (2009) F403-F409
    • (2009) Am. J. Physiol. Renal Physiol. , vol.297
    • Kurtz, L.1    Gerl, M.2    Kriz, W.3    Wagner, C.4    Kurtz, A.5
  • 136
    • 0036164668 scopus 로고    scopus 로고
    • Altered pattern of vascular connexin expression in atherosclerotic plaques
    • Kwak B.R. Altered pattern of vascular connexin expression in atherosclerotic plaques. Arterioscler. Thromb. Vasc. Biol. 22 (2002) 225-230
    • (2002) Arterioscler. Thromb. Vasc. Biol. , vol.22 , pp. 225-230
    • Kwak, B.R.1
  • 138
    • 0037465360 scopus 로고    scopus 로고
    • Reduced connexin43 expression inhibits atherosclerotic lesion formation in low-density lipoprotein receptor-deficient mice
    • Kwak B.R., Veillard N., Pelli G., Mulhaupt F., James R.W., Chanson M., et al. Reduced connexin43 expression inhibits atherosclerotic lesion formation in low-density lipoprotein receptor-deficient mice. Circulation 107 (2003) 1033-1039
    • (2003) Circulation , vol.107 , pp. 1033-1039
    • Kwak, B.R.1    Veillard, N.2    Pelli, G.3    Mulhaupt, F.4    James, R.W.5    Chanson, M.6
  • 139
    • 52649159328 scopus 로고    scopus 로고
    • An intact connexin N-terminus is required for function but not gap junction formation
    • Kyle J.W., Minogue P.J., Thomas B.C., Domowicz D.A., Berthoud V.M., Hanck D.A., et al. An intact connexin N-terminus is required for function but not gap junction formation. J. Cell Sci. 121 (2008) 2744-2750
    • (2008) J. Cell Sci. , vol.121 , pp. 2744-2750
    • Kyle, J.W.1    Minogue, P.J.2    Thomas, B.C.3    Domowicz, D.A.4    Berthoud, V.M.5    Hanck, D.A.6
  • 140
    • 0042386448 scopus 로고    scopus 로고
    • Specific amino-acid residues in the N-terminus and TM3 implicated in channel function and oligomerization compatibility of connexin43
    • Lagree V., Brunschwig K., Lopez P., Gilula N.B., Richard G., and Falk M.M. Specific amino-acid residues in the N-terminus and TM3 implicated in channel function and oligomerization compatibility of connexin43. J. Cell Sci. 116 (2003) 3189-3201
    • (2003) J. Cell Sci. , vol.116 , pp. 3189-3201
    • Lagree, V.1    Brunschwig, K.2    Lopez, P.3    Gilula, N.B.4    Richard, G.5    Falk, M.M.6
  • 142
    • 33645002735 scopus 로고    scopus 로고
    • Life cycle of connexins in health and disease
    • Laird D.W. Life cycle of connexins in health and disease. Biochem. J. 394 (2006) 527-543
    • (2006) Biochem. J. , vol.394 , pp. 527-543
    • Laird, D.W.1
  • 143
    • 14744290484 scopus 로고    scopus 로고
    • Evidence for signaling via gap junctions from smooth muscle to endothelial cells in rat mesenteric arteries: possible implication of a second messenger
    • Lamboley M., Pittet P., Koenigsberger M., Sauser R., Beny J.L., and Meister J.J. Evidence for signaling via gap junctions from smooth muscle to endothelial cells in rat mesenteric arteries: possible implication of a second messenger. Cell Calcium 37 (2005) 311-320
    • (2005) Cell Calcium , vol.37 , pp. 311-320
    • Lamboley, M.1    Pittet, P.2    Koenigsberger, M.3    Sauser, R.4    Beny, J.L.5    Meister, J.J.6
  • 144
    • 1942470517 scopus 로고    scopus 로고
    • The effects of connexin phosphorylation on gap junctional communication
    • Lampe P.D., and Lau A.F. The effects of connexin phosphorylation on gap junctional communication. Int. J. Biochem. Cell Biol. 36 (2004) 1171-1186
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1171-1186
    • Lampe, P.D.1    Lau, A.F.2
  • 146
    • 41649104490 scopus 로고    scopus 로고
    • Caveolin-1 and -2 interact with connexin43 and regulate gap junctional intercellular communication in keratinocytes
    • Langlois S., Cowan K.N., Shao Q., Cowan B.J., and Laird D.W. Caveolin-1 and -2 interact with connexin43 and regulate gap junctional intercellular communication in keratinocytes. Mol. Biol. Cell 19 (2008) 912-928
    • (2008) Mol. Biol. Cell , vol.19 , pp. 912-928
    • Langlois, S.1    Cowan, K.N.2    Shao, Q.3    Cowan, B.J.4    Laird, D.W.5
  • 147
    • 0032400930 scopus 로고    scopus 로고
    • Inositol-trisphosphate-dependent intercellular calcium signaling in and between astrocytes and endothelial cells
    • Leybaert L., Paemeleire K., Strahonja A., and Sanderson M.J. Inositol-trisphosphate-dependent intercellular calcium signaling in and between astrocytes and endothelial cells. Glia 24 (1998) 398-407
    • (1998) Glia , vol.24 , pp. 398-407
    • Leybaert, L.1    Paemeleire, K.2    Strahonja, A.3    Sanderson, M.J.4
  • 148
    • 0033546257 scopus 로고    scopus 로고
    • Multiple connexins form gap junction channels in rat basilar artery smooth muscle cells
    • Li X., and Simard J.M. Multiple connexins form gap junction channels in rat basilar artery smooth muscle cells. Circ. Res. 84 (1999) 1277-1284
    • (1999) Circ. Res. , vol.84 , pp. 1277-1284
    • Li, X.1    Simard, J.M.2
  • 149
    • 0036899042 scopus 로고    scopus 로고
    • Increase in Cx45 gap junction channels in cerebral smooth muscle cells from SHR
    • Li X., and Simard J.M. Increase in Cx45 gap junction channels in cerebral smooth muscle cells from SHR. Hypertension 40 (2002) 940-946
    • (2002) Hypertension , vol.40 , pp. 940-946
    • Li, X.1    Simard, J.M.2
  • 150
    • 0035859833 scopus 로고    scopus 로고
    • Endothelial cell-specific knockout of connexin 43 causes hypotension and bradycardia in mice
    • Liao Y. Endothelial cell-specific knockout of connexin 43 causes hypotension and bradycardia in mice. Proc. Natl. Acad. Sci. USA 98 (2001) 9989-9994
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9989-9994
    • Liao, Y.1
  • 151
    • 34247375905 scopus 로고    scopus 로고
    • Smooth muscle-targeted knockout of connexin43 enhances neointimal formation in response to vascular injury
    • Liao Y., Regan C.P., Manabe I., Owens G.K., Day K.H., Damon D.N., et al. Smooth muscle-targeted knockout of connexin43 enhances neointimal formation in response to vascular injury. Arterioscler. Thromb. Vasc. Biol. 27 (2007) 1037-1042
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 1037-1042
    • Liao, Y.1    Regan, C.P.2    Manabe, I.3    Owens, G.K.4    Day, K.H.5    Damon, D.N.6
  • 152
    • 33644857148 scopus 로고    scopus 로고
    • An amino-terminal lysine residue of rat connexin40 that is required for spermine block
    • Lin X., Fenn E., and Veenstra R.D. An amino-terminal lysine residue of rat connexin40 that is required for spermine block. J. Physiol. 570 (2006) 251-269
    • (2006) J. Physiol. , vol.570 , pp. 251-269
    • Lin, X.1    Fenn, E.2    Veenstra, R.D.3
  • 153
    • 0028940823 scopus 로고
    • Connexin 43 and connexin 40 gap junctional proteins are present in arteriolar smooth muscle and endothelium in vivo
    • Little T.L., Beyer E.C., and Duling B.R. Connexin 43 and connexin 40 gap junctional proteins are present in arteriolar smooth muscle and endothelium in vivo. Am. J. Physiol. 268 (1995) H729-H739
    • (1995) Am. J. Physiol. , vol.268
    • Little, T.L.1    Beyer, E.C.2    Duling, B.R.3
  • 154
    • 0028804566 scopus 로고
    • Dye tracers define differential endothelial and smooth muscle coupling patterns within the arteriolar wall
    • Little T.L., Xia J., and Duling B.R. Dye tracers define differential endothelial and smooth muscle coupling patterns within the arteriolar wall. Circ. Res. 76 (1995) 498-504
    • (1995) Circ. Res. , vol.76 , pp. 498-504
    • Little, T.L.1    Xia, J.2    Duling, B.R.3
  • 155
    • 69849103802 scopus 로고    scopus 로고
    • Connexin channels and phospholipids: Association and modulation
    • Locke D., and Harris A.L. Connexin channels and phospholipids: Association and modulation. BMC Biology 7 (2009) 52
    • (2009) BMC Biology , vol.7 , pp. 52
    • Locke, D.1    Harris, A.L.2
  • 156
    • 3242729342 scopus 로고    scopus 로고
    • Altered permeability and modulatory character of connexin channels during mammary gland development
    • Locke D., Stein T., Davies C., Morris J., Harris A.L., Evans W.H., et al. Altered permeability and modulatory character of connexin channels during mammary gland development. Exp. Cell Res. 298 (2004) 643-660
    • (2004) Exp. Cell Res. , vol.298 , pp. 643-660
    • Locke, D.1    Stein, T.2    Davies, C.3    Morris, J.4    Harris, A.L.5    Evans, W.H.6
  • 157
    • 25444475775 scopus 로고    scopus 로고
    • Lipid rafts prepared by different methods contain different connexin channels, but gap junctions are not lipid rafts
    • Locke D., Liu J., and Harris A.L. Lipid rafts prepared by different methods contain different connexin channels, but gap junctions are not lipid rafts. Biochemistry 44 (2005) 13027-13042
    • (2005) Biochemistry , vol.44 , pp. 13027-13042
    • Locke, D.1    Liu, J.2    Harris, A.L.3
  • 159
    • 33846438625 scopus 로고    scopus 로고
    • Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex
    • Locovei S., Scemes E., Qiu F., Spray D.C., and Dahl G. Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex. FEBS Lett. 581 (2007) 483-488
    • (2007) FEBS Lett. , vol.581 , pp. 483-488
    • Locovei, S.1    Scemes, E.2    Qiu, F.3    Spray, D.C.4    Dahl, G.5
  • 160
    • 4344694192 scopus 로고    scopus 로고
    • Connexin expression and conducted vasodilation along arteriolar endothelium in mouse skeletal muscle
    • Looft-Wilson R.C., Payne G.W., and Segal S.S. Connexin expression and conducted vasodilation along arteriolar endothelium in mouse skeletal muscle. J. Appl. Physiol. 97 (2004) 1152-1158
    • (2004) J. Appl. Physiol. , vol.97 , pp. 1152-1158
    • Looft-Wilson, R.C.1    Payne, G.W.2    Segal, S.S.3
  • 161
    • 63849141447 scopus 로고    scopus 로고
    • Structure of the connexin 26 gap junction channel at 3.5 Å resolution
    • Maeda S., Nakagawa S., Suga M., Yamashita E., Oshima A., Fujiyoshi Y., et al. Structure of the connexin 26 gap junction channel at 3.5 Å resolution. Nature 458 (2009) 597-602
    • (2009) Nature , vol.458 , pp. 597-602
    • Maeda, S.1    Nakagawa, S.2    Suga, M.3    Yamashita, E.4    Oshima, A.5    Fujiyoshi, Y.6
  • 162
    • 0033591383 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of the mouse gap junction gene connexin-57 in human HeLa cells
    • Manthey D., Bukauskas F., Lee C.G., Kozak C.A., and Willecke K. Molecular cloning and functional expression of the mouse gap junction gene connexin-57 in human HeLa cells. J. Biol. Chem. 274 (1999) 14716-14723
    • (1999) J. Biol. Chem. , vol.274 , pp. 14716-14723
    • Manthey, D.1    Bukauskas, F.2    Lee, C.G.3    Kozak, C.A.4    Willecke, K.5
  • 163
    • 0035188530 scopus 로고    scopus 로고
    • Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels
    • Martin P.E., Blundell G., Ahmad S., Errington R.J., and Evans W.H. Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels. J. Cell Sci. 114 (2001) 3845-3855
    • (2001) J. Cell Sci. , vol.114 , pp. 3845-3855
    • Martin, P.E.1    Blundell, G.2    Ahmad, S.3    Errington, R.J.4    Evans, W.H.5
  • 164
    • 0037205321 scopus 로고    scopus 로고
    • Connexin43 and connexin45 form heteromeric gap junction channels in which individual components determine permeability and regulation
    • Martinez A.D., Hayrapetyan V., Moreno A.P., and Beyer E.C. Connexin43 and connexin45 form heteromeric gap junction channels in which individual components determine permeability and regulation. Circ. Res. 90 (2002) 1100-1107
    • (2002) Circ. Res. , vol.90 , pp. 1100-1107
    • Martinez, A.D.1    Hayrapetyan, V.2    Moreno, A.P.3    Beyer, E.C.4
  • 166
    • 24044530701 scopus 로고    scopus 로고
    • Rapid endothelial cell-selective loading of connexin 40 antibody blocks endothelium-derived hyperpolarizing factor dilation in rat small mesenteric arteries
    • Mather S., Dora K.A., Sandow S.L., Winter P., and Garland C.J. Rapid endothelial cell-selective loading of connexin 40 antibody blocks endothelium-derived hyperpolarizing factor dilation in rat small mesenteric arteries. Circ. Res. 97 (2005) 399-407
    • (2005) Circ. Res. , vol.97 , pp. 399-407
    • Mather, S.1    Dora, K.A.2    Sandow, S.L.3    Winter, P.4    Garland, C.J.5
  • 167
    • 20444387943 scopus 로고    scopus 로고
    • Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum
    • Maza J., Das Sarma J., and Koval M. Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum. J. Biol. Chem. 280 (2005) 21115-21121
    • (2005) J. Biol. Chem. , vol.280 , pp. 21115-21121
    • Maza, J.1    Das Sarma, J.2    Koval, M.3
  • 168
    • 0028362273 scopus 로고
    • Gap junction channels: distinct voltage-sensitive and -insensitive conductance states
    • Moreno A.P., Rook M.B., Fishman G.I., and Spray D.C. Gap junction channels: distinct voltage-sensitive and -insensitive conductance states. Biophys. J. 67 (1994) 113-119
    • (1994) Biophys. J. , vol.67 , pp. 113-119
    • Moreno, A.P.1    Rook, M.B.2    Fishman, G.I.3    Spray, D.C.4
  • 169
    • 0028283183 scopus 로고
    • Human connexin43 gap junction channels. Regulation of unitary conductances by phosphorylation
    • Moreno A.P., Saez J.C., Fishman G.I., and Spray D.C. Human connexin43 gap junction channels. Regulation of unitary conductances by phosphorylation. Circ. Res. 74 (1994) 1050-1057
    • (1994) Circ. Res. , vol.74 , pp. 1050-1057
    • Moreno, A.P.1    Saez, J.C.2    Fishman, G.I.3    Spray, D.C.4
  • 170
    • 0025789648 scopus 로고
    • Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques
    • Musil L.S., and Goodenough D.A. Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques. J. Cell Biol. 115 (1991) 1357-1374
    • (1991) J. Cell Biol. , vol.115 , pp. 1357-1374
    • Musil, L.S.1    Goodenough, D.A.2
  • 171
  • 172
    • 0032888052 scopus 로고    scopus 로고
    • Molecular determinants of electrical rectification of single channel conductance in gap junctions formed by connexins 26 and 32
    • Oh S., Rubin J.B., Bennett M.V., Verselis V.K., and Bargiello T.A. Molecular determinants of electrical rectification of single channel conductance in gap junctions formed by connexins 26 and 32. J. Gen. Physiol. 114 (1999) 339-364
    • (1999) J. Gen. Physiol. , vol.114 , pp. 339-364
    • Oh, S.1    Rubin, J.B.2    Bennett, M.V.3    Verselis, V.K.4    Bargiello, T.A.5
  • 173
    • 4143088047 scopus 로고    scopus 로고
    • Determinants of gating polarity of a connexin 32 hemichannel
    • Oh S., Rivkin S., Tang Q., Verselis V.K., and Bargiello T.A. Determinants of gating polarity of a connexin 32 hemichannel. Biophys. J. 87 (2004) 912-928
    • (2004) Biophys. J. , vol.87 , pp. 912-928
    • Oh, S.1    Rivkin, S.2    Tang, Q.3    Verselis, V.K.4    Bargiello, T.A.5
  • 174
    • 0020521968 scopus 로고
    • Microvasculature as studied by the microvascular corrosion casting/scanning electron microscope method. I. Endocrine and digestive system
    • Ohtani O., Kikuta A., Ohtsuka A., Taguchi T., and Murakami T. Microvasculature as studied by the microvascular corrosion casting/scanning electron microscope method. I. Endocrine and digestive system. Arch. Histol. Jpn. 46 (1983) 1-42
    • (1983) Arch. Histol. Jpn. , vol.46 , pp. 1-42
    • Ohtani, O.1    Kikuta, A.2    Ohtsuka, A.3    Taguchi, T.4    Murakami, T.5
  • 175
    • 34547224262 scopus 로고    scopus 로고
    • Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule
    • Oshima A., Tani K., Hiroaki Y., Fujiyoshi Y., and Sosinsky G.E. Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule. Proc. Natl. Acad. Sci. USA 104 (2007) 10034-10039
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10034-10039
    • Oshima, A.1    Tani, K.2    Hiroaki, Y.3    Fujiyoshi, Y.4    Sosinsky, G.E.5
  • 176
    • 36048932052 scopus 로고    scopus 로고
    • Phosphorylation of connexin43 induced by Src: regulation of gap junctional communication between transformed cells
    • Pahujaa M., Anikin M., and Goldberg G.S. Phosphorylation of connexin43 induced by Src: regulation of gap junctional communication between transformed cells. Exp. Cell Res. 313 (2007) 4083-4090
    • (2007) Exp. Cell Res. , vol.313 , pp. 4083-4090
    • Pahujaa, M.1    Anikin, M.2    Goldberg, G.S.3
  • 177
    • 70349395734 scopus 로고    scopus 로고
    • Heterotypic gap junction channels as voltage-sensitive valves for intercellular signaling
    • in press
    • Palacios-Prado, N., Bukauskas. F.F. 2009. Heterotypic gap junction channels as voltage-sensitive valves for intercellular signaling. Proc. Natl. Acad. Sci. USA. (in press)
    • (2009) Proc. Natl. Acad. Sci. USA
    • Palacios-Prado, N.1    Bukauskas, F.F.2
  • 179
    • 0033828666 scopus 로고    scopus 로고
    • Cyclic AMP and LDL trigger a rapid enhancement in gap junction assembly through a stimulation of connexin trafficking
    • Paulson A.F., Lampe P.D., Meyer R.A., TenBroek E., Atkinson M.M., Walseth T.F., et al. Cyclic AMP and LDL trigger a rapid enhancement in gap junction assembly through a stimulation of connexin trafficking. J. Cell Sci. 113 (2000) 3037-3049
    • (2000) J. Cell Sci. , vol.113 , pp. 3037-3049
    • Paulson, A.F.1    Lampe, P.D.2    Meyer, R.A.3    TenBroek, E.4    Atkinson, M.M.5    Walseth, T.F.6
  • 180
    • 8644220461 scopus 로고    scopus 로고
    • Polyvalent cations constitute the voltage gating particle in human connexin37 hemichannels
    • Puljung M.C., Berthoud V.M., Beyer E.C., and Hanck D.A. Polyvalent cations constitute the voltage gating particle in human connexin37 hemichannels. J. Gen. Physiol. 124 (2004) 587-603
    • (2004) J. Gen. Physiol. , vol.124 , pp. 587-603
    • Puljung, M.C.1    Berthoud, V.M.2    Beyer, E.C.3    Hanck, D.A.4
  • 182
    • 0037154271 scopus 로고    scopus 로고
    • Function of the voltage gate of gap junction channels: selective exclusion of molecules
    • Qu Y., and Dahl G. Function of the voltage gate of gap junction channels: selective exclusion of molecules. Proc. Natl. Acad. Sci. USA 99 (2002) 697-702
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 697-702
    • Qu, Y.1    Dahl, G.2
  • 184
    • 34547096966 scopus 로고    scopus 로고
    • Lipid rafts of primary endothelial cells are essential for Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8-induced phosphatidylinositol 3-kinase and RhoA-GTPases critical for microtubule dynamics and nuclear delivery of viral DNA but dispensable for binding and entry
    • Raghu H., Sharma-Walia N., Veettil M.V., Sadagopan S., Caballero A., Sivakumar R., et al. Lipid rafts of primary endothelial cells are essential for Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8-induced phosphatidylinositol 3-kinase and RhoA-GTPases critical for microtubule dynamics and nuclear delivery of viral DNA but dispensable for binding and entry. J. Virol. 81 (2007) 7941-7959
    • (2007) J. Virol. , vol.81 , pp. 7941-7959
    • Raghu, H.1    Sharma-Walia, N.2    Veettil, M.V.3    Sadagopan, S.4    Caballero, A.5    Sivakumar, R.6
  • 185
    • 0027409355 scopus 로고
    • Molecular cloning and functional expression of human connexin37, an endothelial cell gap junction protein
    • Reed K.E., Westphale E.M., Larson D.M., Wang H.Z., Veenstra R.D., and Beyer E.C. Molecular cloning and functional expression of human connexin37, an endothelial cell gap junction protein. J. Clin. Invest. 91 (1993) 997-1004
    • (1993) J. Clin. Invest. , vol.91 , pp. 997-1004
    • Reed, K.E.1    Westphale, E.M.2    Larson, D.M.3    Wang, H.Z.4    Veenstra, R.D.5    Beyer, E.C.6
  • 186
    • 0025266543 scopus 로고
    • Proliferation of smooth muscle cells at sites distant from vascular injury
    • Reidy M.A. Proliferation of smooth muscle cells at sites distant from vascular injury. Arteriosclerosis 10 (1990) 298-305
    • (1990) Arteriosclerosis , vol.10 , pp. 298-305
    • Reidy, M.A.1
  • 187
    • 33645238079 scopus 로고    scopus 로고
    • S-nitrosylation and permeation through connexin 43 hemichannels in astrocytes: induction by oxidant stress and reversal by reducing agents
    • Retamal M.A., Cortes C.J., Reuss L., Bennett M.V., and Saez J.C. S-nitrosylation and permeation through connexin 43 hemichannels in astrocytes: induction by oxidant stress and reversal by reducing agents. Proc. Natl. Acad. Sci. USA 103 (2006) 4475-4480
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4475-4480
    • Retamal, M.A.1    Cortes, C.J.2    Reuss, L.3    Bennett, M.V.4    Saez, J.C.5
  • 188
    • 0014097086 scopus 로고
    • Hexagonal array of subunits in intercellular junctions of the mouse heart and liver
    • Revel J.P., and Karnovsky M.J. Hexagonal array of subunits in intercellular junctions of the mouse heart and liver. J. Cell Biol. 33 (1967) C7-C12
    • (1967) J. Cell Biol. , vol.33
    • Revel, J.P.1    Karnovsky, M.J.2
  • 189
    • 0034687649 scopus 로고    scopus 로고
    • Molecular determinants of membrane potential dependence in vertebrate gap junction channels
    • Revilla A., Bennett M.V., and Barrio L.C. Molecular determinants of membrane potential dependence in vertebrate gap junction channels. Proc. Natl. Acad. Sci. USA 97 (2000) 14760-14765
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14760-14765
    • Revilla, A.1    Bennett, M.V.2    Barrio, L.C.3
  • 190
    • 0014071399 scopus 로고
    • The ultrastructure of mammalian arterioles and precapillary sphincters
    • Rhodin J.A. The ultrastructure of mammalian arterioles and precapillary sphincters. J. Ultrastruct. Res. 18 (1967) 181-223
    • (1967) J. Ultrastruct. Res. , vol.18 , pp. 181-223
    • Rhodin, J.A.1
  • 191
    • 9144244263 scopus 로고    scopus 로고
    • Vascular gap junctions and implications for hypertension
    • Rummery N.M., and Hill C.E. Vascular gap junctions and implications for hypertension. Clin. Exp. Pharmacol. Physiol. 31 (2004) 659-667
    • (2004) Clin. Exp. Pharmacol. Physiol. , vol.31 , pp. 659-667
    • Rummery, N.M.1    Hill, C.E.2
  • 193
    • 17344390158 scopus 로고    scopus 로고
    • Plasma membrane channels formed by connexins: their regulation and functions
    • Saez J.C., Berthoud V.M., Branes M.C., Martinez A.D., and Beyer E.C. Plasma membrane channels formed by connexins: their regulation and functions. Physiol. Rev. 83 (2003) 1359-1400
    • (2003) Physiol. Rev. , vol.83 , pp. 1359-1400
    • Saez, J.C.1    Berthoud, V.M.2    Branes, M.C.3    Martinez, A.D.4    Beyer, E.C.5
  • 195
    • 2442656544 scopus 로고    scopus 로고
    • Levels of gap junction proteins in coronary arterioles and aorta of hamsters exposed to the cold and during hibernation and arousal
    • Saitongdee P., Becker D.L., Milner P., Knight G.E., and Burnstock G. Levels of gap junction proteins in coronary arterioles and aorta of hamsters exposed to the cold and during hibernation and arousal. J. Histochem. Cytochem. 52 (2004) 603-615
    • (2004) J. Histochem. Cytochem. , vol.52 , pp. 603-615
    • Saitongdee, P.1    Becker, D.L.2    Milner, P.3    Knight, G.E.4    Burnstock, G.5
  • 196
    • 33746041455 scopus 로고    scopus 로고
    • Tolbutamide reduces glioma cell proliferation by increasing connexin43, which promotes the up-regulation of p21 and p27 and subsequent changes in retinoblastoma phosphorylation
    • Sanchez-Alvarez R., Paino T., Herrero-Gonzalez S., Medina J.M., and Tabernero A. Tolbutamide reduces glioma cell proliferation by increasing connexin43, which promotes the up-regulation of p21 and p27 and subsequent changes in retinoblastoma phosphorylation. Glia 54 (2006) 125-134
    • (2006) Glia , vol.54 , pp. 125-134
    • Sanchez-Alvarez, R.1    Paino, T.2    Herrero-Gonzalez, S.3    Medina, J.M.4    Tabernero, A.5
  • 197
    • 70450231063 scopus 로고    scopus 로고
    • Spatial association of K-Ca and gap junction connexins in rat mesenteric artery
    • Sandow S.L., and Garland C.J. Spatial association of K-Ca and gap junction connexins in rat mesenteric artery. FASEB J. 20 (2006) A275
    • (2006) FASEB J. , vol.20
    • Sandow, S.L.1    Garland, C.J.2
  • 198
    • 0344196790 scopus 로고    scopus 로고
    • Expression of homocellular and heterocellular gap junctions in hamster arterioles and feed arteries
    • Sandow S.L., Looft-Wilson R., Doran B., Grayson T.H., Segal S.S., and Hill C.E. Expression of homocellular and heterocellular gap junctions in hamster arterioles and feed arteries. Cardiovasc. Res. 60 (2003) 643-653
    • (2003) Cardiovasc. Res. , vol.60 , pp. 643-653
    • Sandow, S.L.1    Looft-Wilson, R.2    Doran, B.3    Grayson, T.H.4    Segal, S.S.5    Hill, C.E.6
  • 200
    • 37349056508 scopus 로고    scopus 로고
    • Modulation of astrocyte P2Y1 receptors by the carboxyl terminal domain of the gap junction protein Cx43
    • Scemes E. Modulation of astrocyte P2Y1 receptors by the carboxyl terminal domain of the gap junction protein Cx43. Glia 56 (2008) 145-153
    • (2008) Glia , vol.56 , pp. 145-153
    • Scemes, E.1
  • 202
    • 60749131296 scopus 로고    scopus 로고
    • Substitution of connexin40 with connexin45 prevents hyperreninemia and attenuates hypertension
    • Schweda F., Kurtz L., de Wit C., Janssen-Bienhold U., Kurtz A., and Wagner C. Substitution of connexin40 with connexin45 prevents hyperreninemia and attenuates hypertension. Kidney Int. 75 (2009) 482-489
    • (2009) Kidney Int. , vol.75 , pp. 482-489
    • Schweda, F.1    Kurtz, L.2    de Wit, C.3    Janssen-Bienhold, U.4    Kurtz, A.5    Wagner, C.6
  • 203
    • 0026648501 scopus 로고
    • Intracellular recording and dye transfer in arterioles during blood flow control
    • Segal S.S., and Beny J.L. Intracellular recording and dye transfer in arterioles during blood flow control. Am. J. Physiol. 263 (1992) H1-H7
    • (1992) Am. J. Physiol. , vol.263
    • Segal, S.S.1    Beny, J.L.2
  • 204
    • 0023009542 scopus 로고
    • Flow control among microvessels coordinated by intercellular conduction
    • Segal S.S., and Duling B.R. Flow control among microvessels coordinated by intercellular conduction. Science 234 (1986) 868-870
    • (1986) Science , vol.234 , pp. 868-870
    • Segal, S.S.1    Duling, B.R.2
  • 205
    • 0035498630 scopus 로고    scopus 로고
    • Role for endothelial cell conduction in ascending vasodilatation and exercise hyperaemia in hamster skeletal muscle
    • Segal S.S., and Jacobs T.L. Role for endothelial cell conduction in ascending vasodilatation and exercise hyperaemia in hamster skeletal muscle. J. Physiol. 536 (2001) 937-946
    • (2001) J. Physiol. , vol.536 , pp. 937-946
    • Segal, S.S.1    Jacobs, T.L.2
  • 206
    • 15744376289 scopus 로고    scopus 로고
    • Modifications in the biophysical properties of connexin43 channels by a peptide of the cytoplasmic loop region
    • Seki A., Duffy H.S., Coombs W., Spray D.C., Taffet S.M., and Delmar M. Modifications in the biophysical properties of connexin43 channels by a peptide of the cytoplasmic loop region. Circ. Res. 95 (2004) e22-e28
    • (2004) Circ. Res. , vol.95
    • Seki, A.1    Duffy, H.S.2    Coombs, W.3    Spray, D.C.4    Taffet, S.M.5    Delmar, M.6
  • 207
    • 0035252340 scopus 로고    scopus 로고
    • Immunocytochemical analysis of connexin expression in the healthy and diseased cardiovascular system
    • Severs N.J. Immunocytochemical analysis of connexin expression in the healthy and diseased cardiovascular system. Microsc. Res. Tech. 52 (2001) 301-322
    • (2001) Microsc. Res. Tech. , vol.52 , pp. 301-322
    • Severs, N.J.1
  • 208
    • 33745389980 scopus 로고    scopus 로고
    • Identification of a novel peptide that interferes with the chemical regulation of connexin43
    • Shibayama J., Lewandowski R., Kieken F., Coombs W., Shah S., Sorgen P.L., et al. Identification of a novel peptide that interferes with the chemical regulation of connexin43. Circ. Res. 98 (2006) 1365-1372
    • (2006) Circ. Res. , vol.98 , pp. 1365-1372
    • Shibayama, J.1    Lewandowski, R.2    Kieken, F.3    Coombs, W.4    Shah, S.5    Sorgen, P.L.6
  • 209
    • 26844534967 scopus 로고    scopus 로고
    • Myoendothelial coupling is not prominent in arterioles within the mouse cremaster microcirculation in vivo
    • Siegl D., Koeppen M., Wölfle S.E., Pohl U., and de Wit C. Myoendothelial coupling is not prominent in arterioles within the mouse cremaster microcirculation in vivo. Circ. Res. 97 (2005) 781-788
    • (2005) Circ. Res. , vol.97 , pp. 781-788
    • Siegl, D.1    Koeppen, M.2    Wölfle, S.E.3    Pohl, U.4    de Wit, C.5
  • 210
    • 64849099976 scopus 로고    scopus 로고
    • Cx43 has distinct mobility within plasma-membrane domains, indicative of progressive formation of gap-junction plaques
    • Simek J., Churko J., Shao Q., and Laird D.W. Cx43 has distinct mobility within plasma-membrane domains, indicative of progressive formation of gap-junction plaques. J. Cell Sci. 122 (2009) 554-562
    • (2009) J. Cell Sci. , vol.122 , pp. 554-562
    • Simek, J.1    Churko, J.2    Shao, Q.3    Laird, D.W.4
  • 211
    • 0017229099 scopus 로고
    • Segmental differentiations of cell junctions in the vascular endothelium. Arteries and veins
    • Simionescu M., Simionescu N., and Palade G.E. Segmental differentiations of cell junctions in the vascular endothelium. Arteries and veins. J. Cell Biol. 68 (1976) 705-723
    • (1976) J. Cell Biol. , vol.68 , pp. 705-723
    • Simionescu, M.1    Simionescu, N.2    Palade, G.E.3
  • 212
    • 0036436688 scopus 로고    scopus 로고
    • Vascular abnormalities in mice lacking the endothelial gap junction proteins connexin37 and connexin40
    • Simon A.M., and McWhorter A.R. Vascular abnormalities in mice lacking the endothelial gap junction proteins connexin37 and connexin40. Dev. Biol. 251 (2002) 206-220
    • (2002) Dev. Biol. , vol.251 , pp. 206-220
    • Simon, A.M.1    McWhorter, A.R.2
  • 213
    • 0038010467 scopus 로고    scopus 로고
    • Decreased intercellular dye-transfer and downregulation of non-ablated connexins in aortic endothelium deficient in connexin37 or connexin40
    • Simon A.M., and McWhorter A.R. Decreased intercellular dye-transfer and downregulation of non-ablated connexins in aortic endothelium deficient in connexin37 or connexin40. J. Cell Sci. 116 (2003) 2223-2236
    • (2003) J. Cell Sci. , vol.116 , pp. 2223-2236
    • Simon, A.M.1    McWhorter, A.R.2
  • 214
    • 5644239564 scopus 로고    scopus 로고
    • Decreased intercellular communication and connexin expression in mouse aortic endothelium during lipopolysaccharide-induced inflammation
    • Simon A.M., McWhorter A.R., Chen H., Jackson C.L., and Ouellette Y. Decreased intercellular communication and connexin expression in mouse aortic endothelium during lipopolysaccharide-induced inflammation. J. Vasc. Res. 41 (2004) 323-333
    • (2004) J. Vasc. Res. , vol.41 , pp. 323-333
    • Simon, A.M.1    McWhorter, A.R.2    Chen, H.3    Jackson, C.L.4    Ouellette, Y.5
  • 215
    • 34249821627 scopus 로고    scopus 로고
    • Myoendothelial gap junction frequency does not account for sex differences in EDHF responses in rat MCA
    • Sokoya E.M., Burns A.R., Marrelli S.P., and Chen J. Myoendothelial gap junction frequency does not account for sex differences in EDHF responses in rat MCA. Microvasc. Res. 74 (2007) 39-44
    • (2007) Microvasc. Res. , vol.74 , pp. 39-44
    • Sokoya, E.M.1    Burns, A.R.2    Marrelli, S.P.3    Chen, J.4
  • 216
    • 20444411484 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to gap junction channel assembly
    • Solan J.L., and Lampe P.D. Connexin phosphorylation as a regulatory event linked to gap junction channel assembly. Biochim. Biophys. Acta 1711 (2005) 154-163
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 154-163
    • Solan, J.L.1    Lampe, P.D.2
  • 217
    • 36349007570 scopus 로고    scopus 로고
    • Key connexin 43 phosphorylation events regulate the gap junction life cycle
    • Solan J.L., and Lampe P.D. Key connexin 43 phosphorylation events regulate the gap junction life cycle. J. Membr. Biol. 217 (2007) 35-41
    • (2007) J. Membr. Biol. , vol.217 , pp. 35-41
    • Solan, J.L.1    Lampe, P.D.2
  • 218
    • 48449089173 scopus 로고    scopus 로고
    • Connexin 43 in LA-25 cells with active v-src is phosphorylated on Y247, Y265, S262, S279/282, and S368 via multiple signaling pathways
    • Solan J.L., and Lampe P.D. Connexin 43 in LA-25 cells with active v-src is phosphorylated on Y247, Y265, S262, S279/282, and S368 via multiple signaling pathways. Cell Commun. Adhes. 15 (2008) 75-84
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 75-84
    • Solan, J.L.1    Lampe, P.D.2
  • 219
    • 37249083141 scopus 로고    scopus 로고
    • Phosphorylation at S365 is a gatekeeper event that changes the structure of Cx43 and prevents down-regulation by PKC
    • Solan J.L., Marquez-Rosado L., Sorgen P.L., Thornton P.J., Gafken P.R., and Lampe P.D. Phosphorylation at S365 is a gatekeeper event that changes the structure of Cx43 and prevents down-regulation by PKC. J. Cell Biol. 179 (2007) 1301-1309
    • (2007) J. Cell Biol. , vol.179 , pp. 1301-1309
    • Solan, J.L.1    Marquez-Rosado, L.2    Sorgen, P.L.3    Thornton, P.J.4    Gafken, P.R.5    Lampe, P.D.6
  • 220
    • 20444397355 scopus 로고    scopus 로고
    • Structural organization of gap junction channels
    • Sosinsky G.E., and Nicholson B.J. Structural organization of gap junction channels. Biochim. Biophys. Acta 1711 (2005) 99-125
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 99-125
    • Sosinsky, G.E.1    Nicholson, B.J.2
  • 221
    • 0025246161 scopus 로고
    • Structure-activity relations of the cardiac gap junction channel
    • Spray D.C., and Burt J.M. Structure-activity relations of the cardiac gap junction channel. Am. J. Physiol. 258 (1990) C195-C205
    • (1990) Am. J. Physiol. , vol.258
    • Spray, D.C.1    Burt, J.M.2
  • 222
    • 33750300467 scopus 로고    scopus 로고
    • Functional connexin "hemichannels": a critical appraisal
    • Spray D.C., Ye Z.C., and Ransom B.R. Functional connexin "hemichannels": a critical appraisal. Glia 54 (2006) 758-773
    • (2006) Glia , vol.54 , pp. 758-773
    • Spray, D.C.1    Ye, Z.C.2    Ransom, B.R.3
  • 224
    • 72049084553 scopus 로고    scopus 로고
    • Site specific connexin phosphorylation is associated with reduced heterocellular communication between smooth muscle and endothelium
    • (in press)
    • Straub A.C., Johnstone S.R., Rizzo M.J., Heberlein K.R., Best A.K., Boitano S., and Isakson B.E. Site specific connexin phosphorylation is associated with reduced heterocellular communication between smooth muscle and endothelium. J. Vasc. Res. (2009) (in press)
    • (2009) J. Vasc. Res.
    • Straub, A.C.1    Johnstone, S.R.2    Rizzo, M.J.3    Heberlein, K.R.4    Best, A.K.5    Boitano, S.6    Isakson, B.E.7
  • 225
    • 0032764028 scopus 로고    scopus 로고
    • Different ionic selectivities for connexins 26 and 32 produce rectifying gap junction channels
    • Suchyna T.M., Nitsche J.M., Chilton M., Harris A.L., Veenstra R.D., and Nicholson B.J. Different ionic selectivities for connexins 26 and 32 produce rectifying gap junction channels. Biophys. J. 77 (1999) 2968-2987
    • (1999) Biophys. J. , vol.77 , pp. 2968-2987
    • Suchyna, T.M.1    Nitsche, J.M.2    Chilton, M.3    Harris, A.L.4    Veenstra, R.D.5    Nicholson, B.J.6
  • 226
    • 33645104766 scopus 로고    scopus 로고
    • Increased levels of cyclins D1 and D3 after inhibition of gap junctional communication in astrocytes
    • Tabernero A., Sanchez-Alvarez R., and Medina J.M. Increased levels of cyclins D1 and D3 after inhibition of gap junctional communication in astrocytes. J. Neurochem. 96 (2006) 973-982
    • (2006) J. Neurochem. , vol.96 , pp. 973-982
    • Tabernero, A.1    Sanchez-Alvarez, R.2    Medina, J.M.3
  • 227
    • 27644547807 scopus 로고    scopus 로고
    • Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration
    • Thomas T., Jordan K., Simek J., Shao Q., Jedeszko C., Walton P., et al. Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration. J. Cell Sci. 118 (2005) 4451-4462
    • (2005) J. Cell Sci. , vol.118 , pp. 4451-4462
    • Thomas, T.1    Jordan, K.2    Simek, J.3    Shao, Q.4    Jedeszko, C.5    Walton, P.6
  • 228
    • 0033582686 scopus 로고    scopus 로고
    • Three-dimensional structure of a recombinant gap junction membrane channel
    • Unger V.M., Kumar N.M., Gilula N.B., and Yeager M. Three-dimensional structure of a recombinant gap junction membrane channel. Science 283 (1999) 1176-1180
    • (1999) Science , vol.283 , pp. 1176-1180
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 229
    • 0036091454 scopus 로고    scopus 로고
    • Biophysical properties of connexin-45 gap junction hemichannels studied in vertebrate cells
    • Valiunas V. Biophysical properties of connexin-45 gap junction hemichannels studied in vertebrate cells. J. Gen. Physiol. 119 (2002) 147-164
    • (2002) J. Gen. Physiol. , vol.119 , pp. 147-164
    • Valiunas, V.1
  • 230
    • 0034602889 scopus 로고    scopus 로고
    • Formation of heterotypic gap junction channels by connexins 40 and 43
    • Valiunas V., Weingart R., and Brink P.R. Formation of heterotypic gap junction channels by connexins 40 and 43. Circ. Res. 86 (2000) E42-E49
    • (2000) Circ. Res. , vol.86
    • Valiunas, V.1    Weingart, R.2    Brink, P.R.3
  • 232
    • 0033503617 scopus 로고    scopus 로고
    • Distribution of connexin37, connexin40 and connexin43 in the aorta and coronary artery of several mammals
    • van Kempen M.J., and Jongsma H.J. Distribution of connexin37, connexin40 and connexin43 in the aorta and coronary artery of several mammals. Histochem. Cell Biol. 112 (1999) 479-486
    • (1999) Histochem. Cell Biol. , vol.112 , pp. 479-486
    • van Kempen, M.J.1    Jongsma, H.J.2
  • 234
    • 0034031992 scopus 로고    scopus 로고
    • Electrical conductance of mouse connexin45 gap junction channels is modulated by phosphorylation
    • van Veen T.A., van Rijen H.V., and Jongsma H.J. Electrical conductance of mouse connexin45 gap junction channels is modulated by phosphorylation. Cardiovasc. Res. 46 (2000) 496-510
    • (2000) Cardiovasc. Res. , vol.46 , pp. 496-510
    • van Veen, T.A.1    van Rijen, H.V.2    Jongsma, H.J.3
  • 235
    • 34249890495 scopus 로고    scopus 로고
    • Regulation of connexin43 gap junctional communication by phosphatidylinositol 4, 5-bisphosphate
    • van Zeijl L., Ponsioen B., Giepmans B.N., Ariaens A., Postma F.R., Varnai P., et al. Regulation of connexin43 gap junctional communication by phosphatidylinositol 4, 5-bisphosphate. J. Cell Biol. 177 (2007) 881-891
    • (2007) J. Cell Biol. , vol.177 , pp. 881-891
    • van Zeijl, L.1    Ponsioen, B.2    Giepmans, B.N.3    Ariaens, A.4    Postma, F.R.5    Varnai, P.6
  • 236
    • 0028025010 scopus 로고
    • Selective dye and ionic permeability of gap junction channels formed by connexin45
    • Veenstra R.D., Wang H.Z., Beyer E.C., and Brink P.R. Selective dye and ionic permeability of gap junction channels formed by connexin45. Circ. Res. 75 (1994) 483-490
    • (1994) Circ. Res. , vol.75 , pp. 483-490
    • Veenstra, R.D.1    Wang, H.Z.2    Beyer, E.C.3    Brink, P.R.4
  • 237
    • 0028200977 scopus 로고
    • Connexin37 forms high conductance gap junction channels with subconductance state activity and selective dye and ionic permeabilities
    • Veenstra R.D., Wang H.Z., Beyer E.C., Ramanan S.V., and Brink P.R. Connexin37 forms high conductance gap junction channels with subconductance state activity and selective dye and ionic permeabilities. Biophys. J. 66 (1994) 1915-1928
    • (1994) Biophys. J. , vol.66 , pp. 1915-1928
    • Veenstra, R.D.1    Wang, H.Z.2    Beyer, E.C.3    Ramanan, S.V.4    Brink, P.R.5
  • 238
    • 0028784986 scopus 로고
    • Selectivity of connexin-specific gap junctions does not correlate with channel conductance
    • Veenstra R.D., Wang H.Z., Beblo D.A., Chilton M.G., Harris A.L., Beyer E.C., et al. Selectivity of connexin-specific gap junctions does not correlate with channel conductance. Circ. Res. 77 (1995) 1156-1165
    • (1995) Circ. Res. , vol.77 , pp. 1156-1165
    • Veenstra, R.D.1    Wang, H.Z.2    Beblo, D.A.3    Chilton, M.G.4    Harris, A.L.5    Beyer, E.C.6
  • 239
    • 33947514231 scopus 로고    scopus 로고
    • Connexin40 is essential for the pressure control of renin synthesis and secretion
    • Wagner C., de Wit C., Kurtz L., Grunberger C., Kurtz A., and Schweda F. Connexin40 is essential for the pressure control of renin synthesis and secretion. Circ. Res. 100 (2007) 556-563
    • (2007) Circ. Res. , vol.100 , pp. 556-563
    • Wagner, C.1    de Wit, C.2    Kurtz, L.3    Grunberger, C.4    Kurtz, A.5    Schweda, F.6
  • 240
    • 0030986975 scopus 로고    scopus 로고
    • Monovalent ion selectivity sequences of the rat connexin43 gap junction channel
    • Wang H.Z., and Veenstra R.D. Monovalent ion selectivity sequences of the rat connexin43 gap junction channel. J. Gen. Physiol. 109 (1997) 491-507
    • (1997) J. Gen. Physiol. , vol.109 , pp. 491-507
    • Wang, H.Z.1    Veenstra, R.D.2
  • 242
    • 34548764500 scopus 로고    scopus 로고
    • Modulation of membrane channel currents by gap junction protein mimetic peptides: size matters
    • Wang J., Ma M., Locovei S., Keane R.W., and Dahl G. Modulation of membrane channel currents by gap junction protein mimetic peptides: size matters. Am. J. Physiol. Cell Physiol. 293 (2007) C1112-C1119
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Wang, J.1    Ma, M.2    Locovei, S.3    Keane, R.W.4    Dahl, G.5
  • 243
    • 1942485065 scopus 로고    scopus 로고
    • The permeability of gap junction channels to probes of different size is dependent on connexin composition and permeant-pore affinities
    • Weber P.A., Chang H.C., Spaeth K.E., Nitsche J.M., and Nicholson B.J. The permeability of gap junction channels to probes of different size is dependent on connexin composition and permeant-pore affinities. Biophys. J. 87 (2004) 958-973
    • (2004) Biophys. J. , vol.87 , pp. 958-973
    • Weber, P.A.1    Chang, H.C.2    Spaeth, K.E.3    Nitsche, J.M.4    Nicholson, B.J.5
  • 244
    • 33750888832 scopus 로고    scopus 로고
    • Endothelial and smooth muscle cell conduction in arterioles controlling blood flow
    • Welsh D.G., and Segal S.S. Endothelial and smooth muscle cell conduction in arterioles controlling blood flow. Am. J. Physiol. 274 (1998) H178-H186
    • (1998) Am. J. Physiol. , vol.274
    • Welsh, D.G.1    Segal, S.S.2
  • 246
    • 34247105350 scopus 로고    scopus 로고
    • Replacement of connexin43 by connexin26 in transgenic mice leads to dysfunctional reproductive organs and slowed ventricular conduction in the heart
    • Winterhager E., Pielensticker N., Freyer J., Ghanem A., Schrickel J.W., Kim J.S., et al. Replacement of connexin43 by connexin26 in transgenic mice leads to dysfunctional reproductive organs and slowed ventricular conduction in the heart. BMC Dev. Biol. 7 (2007) 26
    • (2007) BMC Dev. Biol. , vol.7 , pp. 26
    • Winterhager, E.1    Pielensticker, N.2    Freyer, J.3    Ghanem, A.4    Schrickel, J.W.5    Kim, J.S.6
  • 247
    • 37349051401 scopus 로고    scopus 로고
    • Connexin45 cannot replace the function of connexin40 in conducting endothelium-dependent dilations along arterioles
    • Wolfle S.E., Schmidt V.J., Hoepfl B., Gebert A., Alcolea S., Gros D., et al. Connexin45 cannot replace the function of connexin40 in conducting endothelium-dependent dilations along arterioles. Circ. Res. 101 (2007) 1292-1299
    • (2007) Circ. Res. , vol.101 , pp. 1292-1299
    • Wolfle, S.E.1    Schmidt, V.J.2    Hoepfl, B.3    Gebert, A.4    Alcolea, S.5    Gros, D.6
  • 248
    • 0014037112 scopus 로고
    • A lamellar unit of aortic medial structure and function in mammals
    • Wolinsky H., and Glagov S. A lamellar unit of aortic medial structure and function in mammals. Circ. Res. 20 (1967) 99-111
    • (1967) Circ. Res. , vol.20 , pp. 99-111
    • Wolinsky, H.1    Glagov, S.2
  • 250
    • 33646065973 scopus 로고    scopus 로고
    • Gap junctions modulate apoptosis and colony growth of human embryonic stem cells maintained in a serum-free system
    • Wong R.C., Dottori M., Koh K.L., Nguyen L.T., Pera M.F., and Pebay A. Gap junctions modulate apoptosis and colony growth of human embryonic stem cells maintained in a serum-free system. Biochem. Biophys. Res. Commun. 344 (2006) 181-188
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 181-188
    • Wong, R.C.1    Dottori, M.2    Koh, K.L.3    Nguyen, L.T.4    Pera, M.F.5    Pebay, A.6
  • 251
    • 0030944270 scopus 로고    scopus 로고
    • A mitosis-specific phosphorylation of the gap junction protein connexin43 in human vascular cells: biochemical characterization and localization
    • Xie H., Laird D.W., Chang T.H., and Hu V.W. A mitosis-specific phosphorylation of the gap junction protein connexin43 in human vascular cells: biochemical characterization and localization. J. Cell Biol. 137 (1997) 203-210
    • (1997) J. Cell Biol. , vol.137 , pp. 203-210
    • Xie, H.1    Laird, D.W.2    Chang, T.H.3    Hu, V.W.4
  • 252
    • 35548930792 scopus 로고    scopus 로고
    • Gap junction channel structure in the early 21st century: facts and fantasies
    • Yeager M., and Harris A.L. Gap junction channel structure in the early 21st century: facts and fantasies. Curr. Opin. Cell Biol. 19 (2007) 521-528
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 521-528
    • Yeager, M.1    Harris, A.L.2
  • 253
    • 0033798039 scopus 로고    scopus 로고
    • Age-related alteration of gap junction distribution and connexin expression in rat aortic endothelium
    • Yeh H.I., Chang H.M., Lu W.W., Lee Y.N., Ko Y.S., Severs N.J., et al. Age-related alteration of gap junction distribution and connexin expression in rat aortic endothelium. J. Histochem. Cytochem. 48 (2000) 1377-1389
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 1377-1389
    • Yeh, H.I.1    Chang, H.M.2    Lu, W.W.3    Lee, Y.N.4    Ko, Y.S.5    Severs, N.J.6
  • 255
    • 0035910005 scopus 로고    scopus 로고
    • Heterogeneity of myocardial sleeve morphology and gap junctions in canine superior vena cava
    • Yeh H.I., Lai Y.J., Lee S.H., Lee Y.N., Ko Y.S., Chen S.A., et al. Heterogeneity of myocardial sleeve morphology and gap junctions in canine superior vena cava. Circulation 104 (2001) 3152-3157
    • (2001) Circulation , vol.104 , pp. 3152-3157
    • Yeh, H.I.1    Lai, Y.J.2    Lee, S.H.3    Lee, Y.N.4    Ko, Y.S.5    Chen, S.A.6
  • 256
    • 34249060921 scopus 로고    scopus 로고
    • Gap junctional proteins of animals: the innexin/pannexin superfamily
    • Yen M.R., and Saier Jr. M.H. Gap junctional proteins of animals: the innexin/pannexin superfamily. Prog. Biophys. Mol. Biol. 94 (2007) 5-14
    • (2007) Prog. Biophys. Mol. Biol. , vol.94 , pp. 5-14
    • Yen, M.R.1    Saier Jr., M.H.2
  • 257
    • 0026690832 scopus 로고
    • Early disulfide bond formation prevents heterotypic aggregation of membrane proteins in a cell-free translation system
    • Yilla M., Doyle D., and Sawyer J.T. Early disulfide bond formation prevents heterotypic aggregation of membrane proteins in a cell-free translation system. J. Cell Biol. 118 (1992) 245-252
    • (1992) J. Cell Biol. , vol.118 , pp. 245-252
    • Yilla, M.1    Doyle, D.2    Sawyer, J.T.3
  • 258
    • 32044446954 scopus 로고    scopus 로고
    • Length of C-terminus of rCx46 influences oligomerization and hemichannel properties
    • Zeilinger C., Steffens M., and Kolb H.A. Length of C-terminus of rCx46 influences oligomerization and hemichannel properties. Biochim. Biophys. Acta 1720 (2005) 35-43
    • (2005) Biochim. Biophys. Acta , vol.1720 , pp. 35-43
    • Zeilinger, C.1    Steffens, M.2    Kolb, H.A.3
  • 259
    • 0345701926 scopus 로고    scopus 로고
    • Communication between malignant glioma cells and vascular endothelial cells through gap junctions
    • Zhang W., DeMattia J.A., Song H., and Couldwell W.T. Communication between malignant glioma cells and vascular endothelial cells through gap junctions. J. Neurosurg. 98 (2003) 846-853
    • (2003) J. Neurosurg. , vol.98 , pp. 846-853
    • Zhang, W.1    DeMattia, J.A.2    Song, H.3    Couldwell, W.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.