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Volumn 1818, Issue 8, 2012, Pages 1985-1992

Connexin43 phosphorylation in brain, cardiac, endothelial and epithelial tissues

Author keywords

Cell signalling; Connexin; Gap junction; Phosphorylation; Phosphospecific antibodies

Indexed keywords

CONNEXIN 26; CONNEXIN 30; CONNEXIN 36; CONNEXIN 37; CONNEXIN 40; CONNEXIN 43; CONNEXIN 45; CONNEXIN 46; CYCLIC AMP; FIBROBLAST GROWTH FACTOR 2; GAP JUNCTION PROTEIN; LOW DENSITY LIPOPROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; MONOCLONAL ANTIBODY; REACTIVE OXYGEN METABOLITE;

EID: 84861643461     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.07.028     Document Type: Review
Times cited : (128)

References (133)
  • 1
    • 0037382614 scopus 로고    scopus 로고
    • Beyond the gap: Functions of unpaired connexon channels
    • D.A. Goodenough, and D.L. Paul Beyond the gap: functions of unpaired connexon channels Nat. Rev. Mol. Cell Biol. 4 2003 285 294
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 285-294
    • Goodenough, D.A.1    Paul, D.L.2
  • 3
    • 17344390158 scopus 로고    scopus 로고
    • Plasma membrane channels formed by connexins: Their regulation and functions
    • J.C. Saez, V.M. Berthoud, M.C. Branes, A.D. Martinez, and E.C. Beyer 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
  • 4
    • 34249082403 scopus 로고    scopus 로고
    • Connexin channel permeability to cytoplasmic molecules
    • A.L. Harris Connexin channel permeability to cytoplasmic molecules Prog. Biophys. Mol. Biol. 94 2007 120 143
    • (2007) Prog. Biophys. Mol. Biol. , vol.94 , pp. 120-143
    • Harris, A.L.1
  • 5
    • 75149159657 scopus 로고    scopus 로고
    • The gap junction proteome and its relationship to disease
    • D.W. Laird The gap junction proteome and its relationship to disease Trends Cell Biol. 20 2010 92 101
    • (2010) Trends Cell Biol. , vol.20 , pp. 92-101
    • Laird, D.W.1
  • 6
    • 58149092631 scopus 로고    scopus 로고
    • Connexin-caused genetic diseases and corresponding mouse models
    • R. Dobrowolski, and K. Willecke Connexin-caused genetic diseases and corresponding mouse models Antioxid. Redox Signal. 11 2009 283 295
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 283-295
    • Dobrowolski, R.1    Willecke, K.2
  • 9
    • 48449105610 scopus 로고    scopus 로고
    • Projection structure of a N-terminal deletion mutant of connexin 26 channel with decreased central pore density
    • A. Oshima, K. Tani, Y. Hiroaki, Y. Fujiyoshi, and G.E. Sosinsky Projection structure of a N-terminal deletion mutant of connexin 26 channel with decreased central pore density Cell Commun. Adhes. 15 2008 85 93
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 85-93
    • Oshima, A.1    Tani, K.2    Hiroaki, Y.3    Fujiyoshi, Y.4    Sosinsky, G.E.5
  • 11
    • 0026671599 scopus 로고
    • Inhibition of gap junction and adherens junction assembly by connexin and A-CAM antibodies
    • R.A. Meyer, D.W. Laird, J.-P. Revel, and R.G. Johnson Inhibition of gap junction and adherens junction assembly by connexin and A-CAM antibodies J. Cell Biol. 119 1992 179 189
    • (1992) J. Cell Biol. , vol.119 , pp. 179-189
    • Meyer, R.A.1    Laird, D.W.2    Revel, J.-P.3    Johnson, R.G.4
  • 12
    • 77952929243 scopus 로고    scopus 로고
    • Implications and challenges of connexin connections to cancer
    • C.C. Naus, and D.W. Laird Implications and challenges of connexin connections to cancer Nat. Rev. Cancer 10 2010 435 441
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 435-441
    • Naus, C.C.1    Laird, D.W.2
  • 13
    • 33645002735 scopus 로고    scopus 로고
    • Life cycle of connexins in health and disease
    • D.W. Laird 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
  • 16
    • 80054761014 scopus 로고    scopus 로고
    • The G60S connexin43 mutant regulates hair growth and hair fiber morphology in a mouse model of human oculodentodigital dysplasia
    • doi:10.1038/jid.2011.183 doi:. [Epub ahead of print]
    • J.M. Churko, J. Chan, Q. Shao, and D.W. Laird The G60S connexin43 mutant regulates hair growth and hair fiber morphology in a mouse model of human oculodentodigital dysplasia J. Invest. Dermatol. 2011 doi: 10.1038/jid.2011.183. [Epub ahead of print]
    • (2011) J. Invest. Dermatol.
    • Churko, J.M.1    Chan, J.2    Shao, Q.3    Laird, D.W.4
  • 20
    • 64249170988 scopus 로고    scopus 로고
    • Connexin43 phosphorylation: Structural changes and biological effects
    • J.L. Solan, and P.D. Lampe Connexin43 phosphorylation: structural changes and biological effects Biochem. J. 419 2009 261 272
    • (2009) Biochem. J. , vol.419 , pp. 261-272
    • Solan, J.L.1    Lampe, P.D.2
  • 21
    • 1942470517 scopus 로고    scopus 로고
    • The effects of connexin phosphorylation on gap junctional communication
    • P.D. Lampe, and A.F. Lau 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
  • 22
    • 20444369494 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to gap junction internalization and degradation
    • D.W. Laird Connexin phosphorylation as a regulatory event linked to gap junction internalization and degradation Biochim. Biophys. Acta 1711 2005 172 182
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 172-182
    • Laird, D.W.1
  • 23
    • 20444411484 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to gap junction channel assembly
    • J.L. Solan, and P.D. Lampe 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
  • 24
    • 34249014302 scopus 로고    scopus 로고
    • Gap junction channel gating modulated through protein phosphorylation
    • A.P. Moreno, and A.F. Lau Gap junction channel gating modulated through protein phosphorylation Prog. Biophys. Mol. Biol. 94 2007 107 119
    • (2007) Prog. Biophys. Mol. Biol. , vol.94 , pp. 107-119
    • Moreno, A.P.1    Lau, A.F.2
  • 26
    • 0037286875 scopus 로고    scopus 로고
    • Ischemia-induced dephosphorylation of cardiomyocyte connexin-43 is reduced by okadaic acid and calyculin A but not fostriecin
    • M. Jeyaraman, S. Tanguy, R.R. Fandrich, A. Lukas, and E. Kardami Ischemia-induced dephosphorylation of cardiomyocyte connexin-43 is reduced by okadaic acid and calyculin A but not fostriecin Mol. Cell. Biochem. 242 2003 129 134
    • (2003) Mol. Cell. Biochem. , vol.242 , pp. 129-134
    • Jeyaraman, M.1    Tanguy, S.2    Fandrich, R.R.3    Lukas, A.4    Kardami, E.5
  • 28
    • 0034671950 scopus 로고    scopus 로고
    • Regulation of gap junctions by phosphorylation of connexins
    • P.D. Lampe, and A.F. Lau Regulation of gap junctions by phosphorylation of connexins Arch. Biochem. Biophys. 384 2000 205 215
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 205-215
    • Lampe, P.D.1    Lau, A.F.2
  • 29
    • 0025340718 scopus 로고
    • The hormone-induced regulation of contact-dependent cell-cell communication by phosphorylation
    • R.B. Stagg, and W.H. Fletcher The hormone-induced regulation of contact-dependent cell-cell communication by phosphorylation Endocr. Rev. 11 1990 302 325
    • (1990) Endocr. Rev. , vol.11 , pp. 302-325
    • Stagg, R.B.1    Fletcher, W.H.2
  • 30
    • 20444404602 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to channel gating
    • A.P. Moreno Connexin phosphorylation as a regulatory event linked to channel gating Biochim. Biophys. Acta 1711 2005 164 171
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 164-171
    • Moreno, A.P.1
  • 31
    • 0025287594 scopus 로고
    • Expression of the gap junction protein connexin43 in embryonic chick lens: Molecular cloning, ultrastructural localization, and post-translational phosphorylation
    • L.S. Musil, E.C. Beyer, and D.A. Goodenough Expression of the gap junction protein connexin43 in embryonic chick lens: molecular cloning, ultrastructural localization, and post-translational phosphorylation J. Membr. Biol. 116 1990 163 175
    • (1990) J. Membr. Biol. , vol.116 , pp. 163-175
    • Musil, L.S.1    Beyer, E.C.2    Goodenough, D.A.3
  • 32
    • 0025261843 scopus 로고
    • Phosphorylation of connexin43 gap junction protein in uninfected and Rous sarcoma virus-transformed mammalian fibroblasts
    • D.S. Crow, E.C. Beyer, D.L. Paul, S.S. Kobe, and A.F. Lau Phosphorylation of connexin43 gap junction protein in uninfected and Rous sarcoma virus-transformed mammalian fibroblasts Mol. Cell. Biol. 10 1990 1754 1763
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1754-1763
    • Crow, D.S.1    Beyer, E.C.2    Paul, D.L.3    Kobe, S.S.4    Lau, A.F.5
  • 33
    • 0026025267 scopus 로고
    • Turnover and phosphorylation dynamics of connexin43 gap junction protein in cultured cardiac myocytes
    • D.W. Laird, K.L. Puranam, and J.P. Revel Turnover and phosphorylation dynamics of connexin43 gap junction protein in cultured cardiac myocytes Biochem. J. 273 1991 67 72
    • (1991) Biochem. J. , vol.273 , pp. 67-72
    • Laird, D.W.1    Puranam, K.L.2    Revel, J.P.3
  • 34
    • 0028584195 scopus 로고
    • Analyzing phorbol ester effects on gap junction communication: A dramatic inhibition of assembly
    • P.D. Lampe Analyzing phorbol ester effects on gap junction communication: a dramatic inhibition of assembly J. Cell Biol. 127 1994 1895 1905
    • (1994) J. Cell Biol. , vol.127 , pp. 1895-1905
    • Lampe, P.D.1
  • 35
    • 0032555956 scopus 로고    scopus 로고
    • Rapid turnover of connexin43 in the adult rat heart
    • M. Beardslee, J. Laing, E. Beyer, and J. Saffitz Rapid turnover of connexin43 in the adult rat heart Circ. Res. 83 1998 629 635
    • (1998) Circ. Res. , vol.83 , pp. 629-635
    • Beardslee, M.1    Laing, J.2    Beyer, E.3    Saffitz, J.4
  • 36
    • 0026527868 scopus 로고
    • Connexin43 in MDCK cells: Regulation by a tumor-promoting phorbol ester and calcium
    • V.M. Berthoud, M.L.S. Ledbetter, E.L. Hertzberg, and J.C. Saez Connexin43 in MDCK cells: regulation by a tumor-promoting phorbol ester and calcium Eur. J. Cell Biol. 57 1992 40 50
    • (1992) Eur. J. Cell Biol. , vol.57 , pp. 40-50
    • Berthoud, V.M.1    Ledbetter, M.L.S.2    Hertzberg, E.L.3    Saez, J.C.4
  • 37
    • 0026045904 scopus 로고
    • The tumor promoter 12-O-tetradecanoylphorbol-13-acetate and the ras oncogene modulate expression and phosphorylation of gap junction proteins
    • J.L. Brissette, N.M. Kumar, N.B. Gilula, and G.P. Dotto The tumor promoter 12-O-tetradecanoylphorbol-13-acetate and the ras oncogene modulate expression and phosphorylation of gap junction proteins Mol. Cell. Biol. 11 1991 5364 5371
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5364-5371
    • Brissette, J.L.1    Kumar, N.M.2    Gilula, N.B.3    Dotto, G.P.4
  • 38
    • 0025959178 scopus 로고
    • Tissue-specific distribution of differentially phosphorylated forms of Cx43
    • R. Kadle, J.T. Zhang, and B.J. Nicholson Tissue-specific distribution of differentially phosphorylated forms of Cx43 Mol. Cell. Biol. 11 1991 363 369
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 363-369
    • Kadle, R.1    Zhang, J.T.2    Nicholson, B.J.3
  • 39
    • 0025155347 scopus 로고
    • Differential phosphorylation of gap junction protein connexin43 in junctional communication-competent and deficient cell lines
    • L.S. Musil, B.A. Cunningham, G.M. Edelman, and D.A. Goodenough Differential phosphorylation of gap junction protein connexin43 in junctional communication-competent and deficient cell lines J. Cell Biol. 111 1990 2077 2088
    • (1990) J. Cell Biol. , vol.111 , pp. 2077-2088
    • Musil, L.S.1    Cunningham, B.A.2    Edelman, G.M.3    Goodenough, D.A.4
  • 40
    • 0025789648 scopus 로고
    • Biochemical analysis of connexin43 intracellular transport, phosphorylation and assembly into gap junctional plaques
    • L.S. Musil, and D.A. Goodenough 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
  • 42
    • 0029176855 scopus 로고
    • Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells
    • D.L. Laird, M. Castillo, and L. Kasprzak Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells J. Cell Biol. 131 1995 1193 1203
    • (1995) J. Cell Biol. , vol.131 , pp. 1193-1203
    • Laird, D.L.1    Castillo, M.2    Kasprzak, L.3
  • 44
    • 27244462402 scopus 로고
    • Tyrosine phosphorylation of the gap junction protein connexin43 is required for pp 60src-induced inhibition of communication
    • K.I. Swenson, H. Piwnica-Worms, H. McNamee, and D.L. Paul Tyrosine phosphorylation of the gap junction protein connexin43 is required for pp 60src-induced inhibition of communication Cell Regul. 1 1990 989 1002
    • (1990) Cell Regul. , vol.1 , pp. 989-1002
    • Swenson, K.I.1    Piwnica-Worms, H.2    McNamee, H.3    Paul, D.L.4
  • 45
    • 0031059261 scopus 로고    scopus 로고
    • The gap junction protein connexin 56 is phosphorylated in the intracellular loop and the carboxy-terminal region
    • V.M. Berthoud, E.C. Beyer, W.E. Kurata, A.F. Lau, and P.D. Lampe The gap junction protein connexin 56 is phosphorylated in the intracellular loop and the carboxy-terminal region Eur. J. Biochem. 244 1997 89 97
    • (1997) Eur. J. Biochem. , vol.244 , pp. 89-97
    • Berthoud, V.M.1    Beyer, E.C.2    Kurata, W.E.3    Lau, A.F.4    Lampe, P.D.5
  • 46
    • 34548501240 scopus 로고    scopus 로고
    • Connexin 35/36 is phosphorylated at regulatory sites in the retina
    • W.W. Kothmann, X. Li, G.S. Burr, and J. O'Brien Connexin 35/36 is phosphorylated at regulatory sites in the retina Vis. Neurosci. 24 2007 363 375
    • (2007) Vis. Neurosci. , vol.24 , pp. 363-375
    • Kothmann, W.W.1    Li, X.2    Burr, G.S.3    O'Brien, J.4
  • 47
    • 0030883743 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of connexin 43 by v-Src is mediated by SH2 and SH3 domain interactions
    • M.Y. Kanemitsu, L.W. Loo, S. Simon, A.F. Lau, and W. Eckhart Tyrosine phosphorylation of connexin 43 by v-Src is mediated by SH2 and SH3 domain interactions J. Biol. Chem. 272 1997 22824 22831
    • (1997) J. Biol. Chem. , vol.272 , pp. 22824-22831
    • Kanemitsu, M.Y.1    Loo, L.W.2    Simon, S.3    Lau, A.F.4    Eckhart, W.5
  • 48
    • 0032415677 scopus 로고    scopus 로고
    • Characterization of the gap junction protein connexin37 in murine endothelium, respiratory epithelium, and after transfection in human HeLa cells
    • O. Traub, B. Hertlein, M. Kasper, R. Eckert, A. Krisciukaitis, D. Hulser, and K. Willecke Characterization of the gap junction protein connexin37 in murine endothelium, respiratory epithelium, and after transfection in human HeLa cells Eur. J. Cell Biol. 77 1998 313 322
    • (1998) Eur. J. Cell Biol. , vol.77 , pp. 313-322
    • Traub, O.1    Hertlein, B.2    Kasper, M.3    Eckert, R.4    Krisciukaitis, A.5    Hulser, D.6    Willecke, K.7
  • 49
    • 0029083331 scopus 로고
    • Cyclic AMP modifies the cellular distribution of connexin 43 and induces a persistent increase in the junctional permeability of mouse mammary tumor cells
    • M.M. Atkinson, P.D. Lampe, H.H. Lin, R. Kollander, X.-R. Li, and D.T. Kiang Cyclic AMP modifies the cellular distribution of connexin 43 and induces a persistent increase in the junctional permeability of mouse mammary tumor cells J. Cell Sci. 108 1995 3079 3090
    • (1995) J. Cell Sci. , vol.108 , pp. 3079-3090
    • Atkinson, M.M.1    Lampe, P.D.2    Lin, H.H.3    Kollander, R.4    Li, X.-R.5    Kiang, D.T.6
  • 50
    • 0029609073 scopus 로고
    • Cyclic AMP induces rapid increases in gap junction permeability and changes in the cellular distribution of connexin43
    • R.C. Burghardt, R. Barhoumi, T.C. Sewall, and J.A. Bowen Cyclic AMP induces rapid increases in gap junction permeability and changes in the cellular distribution of connexin43 J. Membr. Biol. 148 1995 243 253
    • (1995) J. Membr. Biol. , vol.148 , pp. 243-253
    • Burghardt, R.C.1    Barhoumi, R.2    Sewall, T.C.3    Bowen, J.A.4
  • 51
  • 52
    • 0036716820 scopus 로고    scopus 로고
    • The connexin43 gap junction protein is phosphorylated by protein kinase A and protein kinase C: In vivo and in vitro studies
    • M.M. Shah, A.-M. Martinez, and W.H. Fletcher The connexin43 gap junction protein is phosphorylated by protein kinase A and protein kinase C: in vivo and in vitro studies Mol. Cell. Biochem. 238 2002 57 68
    • (2002) Mol. Cell. Biochem. , vol.238 , pp. 57-68
    • Shah, M.M.1    Martinez, A.-M.2    Fletcher, W.H.3
  • 53
    • 0037032416 scopus 로고    scopus 로고
    • Identification and functional analysis of novel phosphorylation sites in Cx43 in rat primary granulosa cells
    • K. Yogo, T. Ogawa, M. Akiyama, N. Ishida, and T. Takeya Identification and functional analysis of novel phosphorylation sites in Cx43 in rat primary granulosa cells FEBS Lett. 531 2002 132 136
    • (2002) FEBS Lett. , vol.531 , pp. 132-136
    • Yogo, K.1    Ogawa, T.2    Akiyama, M.3    Ishida, N.4    Takeya, T.5
  • 54
    • 0034717680 scopus 로고    scopus 로고
    • Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication
    • P.D. Lampe, E.M. TenBroek, J.M. Burt, W.E. Kurata, R.G. Johnson, and A.F. Lau Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication J. Cell Biol. 126 2000 1503 1512
    • (2000) J. Cell Biol. , vol.126 , pp. 1503-1512
    • Lampe, P.D.1    Tenbroek, E.M.2    Burt, J.M.3    Kurata, W.E.4    Johnson, R.G.5    Lau, A.F.6
  • 56
    • 0842302372 scopus 로고    scopus 로고
    • Phosphorylation of serine 262 in the gap junction protein connexin-43 regulates DNA synthesis in cell-cell contact forming cardiomyocytes
    • B.W. Doble, X. Dang, P. Ping, R.R. Fandrich, B.E. Nickel, Y. Jin, P.A. Cattini, and E. Kardami Phosphorylation of serine 262 in the gap junction protein connexin-43 regulates DNA synthesis in cell-cell contact forming cardiomyocytes J. Cell Sci. 117 2004 507 514
    • (2004) J. Cell Sci. , vol.117 , pp. 507-514
    • Doble, B.W.1    Dang, X.2    Ping, P.3    Fandrich, R.R.4    Nickel, B.E.5    Jin, Y.6    Cattini, P.A.7    Kardami, E.8
  • 57
    • 33746566071 scopus 로고    scopus 로고
    • Selectivity of connexin 43 channels is regulated through protein kinase C-dependent phosphorylation
    • J.F. Ek-Vitorin, T.J. King, N.S. Heyman, P.D. Lampe, and J.M. Burt 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
  • 58
    • 2442431501 scopus 로고    scopus 로고
    • Regulation of purified and reconstituted connexin 43 hemichannels by protein kinase C-mediated phosphorylation of serine 368
    • X. Bao, L. Reuss, and G.A. Altenberg Regulation of purified and reconstituted connexin 43 hemichannels by protein kinase C-mediated phosphorylation of serine 368 J. Biol. Chem. 279 2004 20058 20066
    • (2004) J. Biol. Chem. , vol.279 , pp. 20058-20066
    • Bao, X.1    Reuss, L.2    Altenberg, G.A.3
  • 60
    • 0344420042 scopus 로고    scopus 로고
    • Protein kinase Cgamma regulation of gap junction activity through caveolin-1-containing lipid rafts
    • D. Lin, J. Zhou, P.S. Zelenka, and D.J. Takemoto Protein kinase Cgamma regulation of gap junction activity through caveolin-1-containing lipid rafts Invest. Ophthalmol. Vis. Sci. 44 2003 5259 5268
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 5259-5268
    • Lin, D.1    Zhou, J.2    Zelenka, P.S.3    Takemoto, D.J.4
  • 61
    • 0033621884 scopus 로고    scopus 로고
    • The epsilon subtype of protein kinase C is required for cardiomyocyte connexin-43 phosphorylation
    • B.W. Doble, P. Ping, and E. Kardami The epsilon subtype of protein kinase C is required for cardiomyocyte connexin-43 phosphorylation Circ. Res. 86 2000 293 301
    • (2000) Circ. Res. , vol.86 , pp. 293-301
    • Doble, B.W.1    Ping, P.2    Kardami, E.3
  • 62
    • 0037160066 scopus 로고    scopus 로고
    • Casein kinase 1 regulates connexin43 gap junction assembly
    • C.D. Cooper, and P.D. Lampe Casein kinase 1 regulates connexin43 gap junction assembly J. Biol. Chem. 277 2002 44962 44968
    • (2002) J. Biol. Chem. , vol.277 , pp. 44962-44968
    • Cooper, C.D.1    Lampe, P.D.2
  • 63
    • 0037303074 scopus 로고    scopus 로고
    • Mechanism of v-Src- and mitogen-activated protein kinase-induced reduction of gap junction communication
    • G.T. Cottrell, R. Lin, B.J. Warn-Cramer, A.F. Lau, and J.M. Burt Mechanism of v-Src- and mitogen-activated protein kinase-induced reduction of gap junction communication Am. J. Physiol. Cell Physiol. 284 2003 C511 C520
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Cottrell, G.T.1    Lin, R.2    Warn-Cramer, B.J.3    Lau, A.F.4    Burt, J.M.5
  • 64
    • 0031974956 scopus 로고    scopus 로고
    • Cdc2-mediated phosphorylation of the gap junction protein, connexin43, during mitosis
    • M.Y. Kanemitsu, W. Jiang, and W. Eckhart Cdc2-mediated phosphorylation of the gap junction protein, connexin43, during mitosis Cell Growth Differ. 9 1998 13 21
    • (1998) Cell Growth Differ. , vol.9 , pp. 13-21
    • Kanemitsu, M.Y.1    Jiang, W.2    Eckhart, W.3
  • 65
    • 0031563776 scopus 로고    scopus 로고
    • Selective monoclonal antibody recognition and cellular localization of an unphosporylated form of connexin43
    • J.I. Nagy, W.E.I. Li, C. Roy, B.W. Doble, J.S. Gilchrist, E. Kardami, and E.L. Hertzberg Selective monoclonal antibody recognition and cellular localization of an unphosporylated form of connexin43 Exper. Cell Res. 236 1997 127 136
    • (1997) Exper. Cell Res. , vol.236 , pp. 127-136
    • Nagy, J.I.1    Li, W.E.I.2    Roy, C.3    Doble, B.W.4    Gilchrist, J.S.5    Kardami, E.6    Hertzberg, E.L.7
  • 66
    • 0031841797 scopus 로고    scopus 로고
    • Immunorecognition, ultrastructure and phosphorylation status of astrocytic gap junctions and connexin43 in rat brain after cerebral focal ischaemia
    • W.E. Li, P.A. Ochalski, E.L. Hertzberg, and J.I. Nagy Immunorecognition, ultrastructure and phosphorylation status of astrocytic gap junctions and connexin43 in rat brain after cerebral focal ischaemia Eur. J. Neurosci. 10 1998 2444 2463
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 2444-2463
    • Li, W.E.1    Ochalski, P.A.2    Hertzberg, E.L.3    Nagy, J.I.4
  • 67
    • 0038727330 scopus 로고    scopus 로고
    • Mechanisms of delayed electrical uncoupling induced by ischemic preconditioning
    • S.K. Jain, R.B. Schuessler, and J.E. Saffitz Mechanisms of delayed electrical uncoupling induced by ischemic preconditioning Circ. Res. 92 2003 1138 1144
    • (2003) Circ. Res. , vol.92 , pp. 1138-1144
    • Jain, S.K.1    Schuessler, R.B.2    Saffitz, J.E.3
  • 68
    • 40649116404 scopus 로고    scopus 로고
    • N-cadherin haploinsufficiency affects cardiac gap junctions and arrhythmic susceptibility
    • J. Li, M.D. Levin, Y. Xiong, N. Petrenko, V.V. Patel, and G.L. Radice N-cadherin haploinsufficiency affects cardiac gap junctions and arrhythmic susceptibility J. Mol. Cell. Cardiol. 44 2008 597 606
    • (2008) J. Mol. Cell. Cardiol. , vol.44 , pp. 597-606
    • Li, J.1    Levin, M.D.2    Xiong, Y.3    Petrenko, N.4    Patel, V.V.5    Radice, G.L.6
  • 70
  • 71
    • 0033567979 scopus 로고    scopus 로고
    • Stimulated phosphorylation of intracellular connexin43
    • V. Cruciani, and S.O. Mikalsen Stimulated phosphorylation of intracellular connexin43 Exp. Cell Res. 251 1999 285 298
    • (1999) Exp. Cell Res. , vol.251 , pp. 285-298
    • Cruciani, V.1    Mikalsen, S.O.2
  • 72
    • 37249013014 scopus 로고    scopus 로고
    • The C-terminus of connexin43 adopts different conformations in the Golgi and gap junction as detected with structure specific antibodies
    • G.E. Sosinsky, J.L. Solan, G.M. Gaietta, L. Ngan, G.J. Lee, M.R. Mackey, and P.D. Lampe The C-terminus of connexin43 adopts different conformations in the Golgi and gap junction as detected with structure specific antibodies Biochem. J. 408 2007 375 385
    • (2007) Biochem. J. , vol.408 , pp. 375-385
    • Sosinsky, G.E.1    Solan, J.L.2    Gaietta, G.M.3    Ngan, L.4    Lee, G.J.5    MacKey, M.R.6    Lampe, P.D.7
  • 73
    • 37249083141 scopus 로고    scopus 로고
    • Phosphorylation of Cx43 at S365 is a gatekeeper event that changes the structure of Cx43 and prevents downregulation by PKC
    • J.L. Solan, L. Marquez-Rosado, P.L. Sorgen, P.J. Thornton, P.R. Gafken, and P.D. Lampe Phosphorylation of Cx43 at S365 is a gatekeeper event that changes the structure of Cx43 and prevents downregulation 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
  • 74
    • 18744378257 scopus 로고    scopus 로고
    • Phosphorylation and subcellular distribution of connexin43 in normal and stressed cells
    • K. Leykauf, M. Durst, and A. Alonso Phosphorylation and subcellular distribution of connexin43 in normal and stressed cells Cell Tissue Res. 311 2003 23 30
    • (2003) Cell Tissue Res. , vol.311 , pp. 23-30
    • Leykauf, K.1    Durst, M.2    Alonso, A.3
  • 75
    • 58149395024 scopus 로고    scopus 로고
    • Luteinizing hormone causes MAP kinase-dependent phosphorylation and closure of connexin 43 gap junctions in mouse ovarian follicles: One of two paths to meiotic resumption
    • R.P. Norris, M. Freudzon, L.M. Mehlmann, A.E. Cowan, A.M. Simon, D.L. Paul, P.D. Lampe, and L.A. Jaffe Luteinizing hormone causes MAP kinase-dependent phosphorylation and closure of connexin 43 gap junctions in mouse ovarian follicles: one of two paths to meiotic resumption Development 135 2008 3229 3238
    • (2008) Development , vol.135 , pp. 3229-3238
    • Norris, R.P.1    Freudzon, M.2    Mehlmann, L.M.3    Cowan, A.E.4    Simon, A.M.5    Paul, D.L.6    Lampe, P.D.7    Jaffe, L.A.8
  • 76
    • 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
    • J.L. Solan, and P.D. Lampe 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
  • 78
    • 33748795808 scopus 로고    scopus 로고
    • Analysis of connexin43 phosphorylated at S325, S328 and S330 in normoxic and ischemic heart
    • P.D. Lampe, C.D. Cooper, T.J. King, and J.M. Burt Analysis of connexin43 phosphorylated at S325, S328 and S330 in normoxic and ischemic heart J. Cell Sci. 119 2006 3435 3442
    • (2006) J. Cell Sci. , vol.119 , pp. 3435-3442
    • Lampe, P.D.1    Cooper, C.D.2    King, T.J.3    Burt, J.M.4
  • 79
    • 0035921428 scopus 로고    scopus 로고
    • V-Src phosphorylation of connexin 43 on Tyr247 and Tyr265 disrupts gap junctional communication
    • R. Lin, B.J. Warn-Cramer, W.E. Kurata, and A.F. Lau v-Src phosphorylation of connexin 43 on Tyr247 and Tyr265 disrupts gap junctional communication J. Cell Biol. 154 2001 815 827
    • (2001) J. Cell Biol. , vol.154 , pp. 815-827
    • Lin, R.1    Warn-Cramer, B.J.2    Kurata, W.E.3    Lau, A.F.4
  • 80
    • 33747459250 scopus 로고    scopus 로고
    • V-Src tyrosine phosphorylation of connexin43: Regulation of gap junction communication and effects on cell transformation
    • R. Lin, K.D. Martyn, C.V. Guyette, A.F. Lau, and B.J. Warn-Cramer v-Src tyrosine phosphorylation of connexin43: regulation of gap junction communication and effects on cell transformation Cell Commun. Adhes. 13 2006 199 216
    • (2006) Cell Commun. Adhes. , vol.13 , pp. 199-216
    • Lin, R.1    Martyn, K.D.2    Guyette, C.V.3    Lau, A.F.4    Warn-Cramer, B.J.5
  • 81
    • 33845961237 scopus 로고    scopus 로고
    • Protein kinase A-mediated phosphorylation of connexin36 in mouse retina results in decreased gap junctional communication between AII amacrine cells
    • S. Urschel, T. Hoher, T. Schubert, C. Alev, G. Sohl, P. Worsdorfer, T. Asahara, R. Dermietzel, R. Weiler, and K. Willecke Protein kinase A-mediated phosphorylation of connexin36 in mouse retina results in decreased gap junctional communication between AII amacrine cells J. Biol. Chem. 281 2006 33163 33171
    • (2006) J. Biol. Chem. , vol.281 , pp. 33163-33171
    • Urschel, S.1    Hoher, T.2    Schubert, T.3    Alev, C.4    Sohl, G.5    Worsdorfer, P.6    Asahara, T.7    Dermietzel, R.8    Weiler, R.9    Willecke, K.10
  • 83
    • 0042122377 scopus 로고    scopus 로고
    • Astrocytic gap junctions composed of connexin 43 reduce apoptotic neuronal damage in cerebral ischemia
    • T. Nakase, S. Fushiki, and C.C. Naus Astrocytic gap junctions composed of connexin 43 reduce apoptotic neuronal damage in cerebral ischemia Stroke 34 2003 1987 1993
    • (2003) Stroke , vol.34 , pp. 1987-1993
    • Nakase, T.1    Fushiki, S.2    Naus, C.C.3
  • 86
    • 60849097265 scopus 로고    scopus 로고
    • Involvement of the cytoplasmic C-terminal domain of connexin43 in neuronal migration
    • C. Cina, K. Maass, M. Theis, K. Willecke, J.F. Bechberger, and C.C. Naus Involvement of the cytoplasmic C-terminal domain of connexin43 in neuronal migration J. Neurosci. 29 2009 2009 2021
    • (2009) J. Neurosci. , vol.29 , pp. 2009-2021
    • Cina, C.1    Maass, K.2    Theis, M.3    Willecke, K.4    Bechberger, J.F.5    Naus, C.C.6
  • 87
    • 9644289646 scopus 로고    scopus 로고
    • Gap junctions in developing neocortex: A review
    • R.J. Montoro, and R. Yuste Gap junctions in developing neocortex: a review Brain Res. Brain Res. Rev. 47 2004 216 226
    • (2004) Brain Res. Brain Res. Rev. , vol.47 , pp. 216-226
    • Montoro, R.J.1    Yuste, R.2
  • 88
    • 65949085338 scopus 로고    scopus 로고
    • Lack of connexin43-mediated bergmann glial gap junctional coupling does not affect cerebellar long-term depression, motor coordination, or eyeblink conditioning
    • M. Tanaka, K. Yamaguchi, T. Tatsukawa, C. Nishioka, H. Nishiyama, M. Theis, K. Willecke, and S. Itohara Lack of connexin43-mediated bergmann glial gap junctional coupling does not affect cerebellar long-term depression, motor coordination, or eyeblink conditioning Front. Behav. Neurosci. 2 2008 1
    • (2008) Front. Behav. Neurosci. , vol.2 , pp. 1
    • Tanaka, M.1    Yamaguchi, K.2    Tatsukawa, T.3    Nishioka, C.4    Nishiyama, H.5    Theis, M.6    Willecke, K.7    Itohara, S.8
  • 90
    • 0014097086 scopus 로고
    • Hexagonal array of subunits in intercellular junctions of the mouse heart and liver
    • J.P. Revel, and M.J. Karnovsky 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
  • 91
    • 0025159130 scopus 로고
    • The cardiac gap junction and intercalated disc
    • N.J. Severs The cardiac gap junction and intercalated disc Int. J. Cardiol. 26 1990 137 173
    • (1990) Int. J. Cardiol. , vol.26 , pp. 137-173
    • Severs, N.J.1
  • 92
    • 0031024666 scopus 로고    scopus 로고
    • Dissociated spatial patterning of gap junctions and cell adhesion junctions during postnatal differentiation of ventricular myocardium
    • B.D. Angst, L.U. Khan, N.J. Severs, K. Whitely, S. Rothery, R.P. Thompson, A.I. Magee, and R.G. Gourdie Dissociated spatial patterning of gap junctions and cell adhesion junctions during postnatal differentiation of ventricular myocardium Circ. Res. 80 1997 88 94
    • (1997) Circ. Res. , vol.80 , pp. 88-94
    • Angst, B.D.1    Khan, L.U.2    Severs, N.J.3    Whitely, K.4    Rothery, S.5    Thompson, R.P.6    Magee, A.I.7    Gourdie, R.G.8
  • 93
    • 84861614344 scopus 로고    scopus 로고
    • Connexins in the heart
    • A. Harris, D. Locke, Humana Press New York
    • N.J. Severs Connexins in the heart A. Harris, D. Locke, Connexins: A Guide 2009 Humana Press New York 435 456
    • (2009) Connexins: A Guide , pp. 435-456
    • Severs, N.J.1
  • 95
    • 0037590100 scopus 로고    scopus 로고
    • Ischemic preconditioning preserves connexin 43 phosphorylation during sustained ischemia in pig hearts in vivo
    • R. Schulz, P. Gres, A. Skyschally, A. Duschin, S. Belosjorow, I. Konietzka, and G. Heusch Ischemic preconditioning preserves connexin 43 phosphorylation during sustained ischemia in pig hearts in vivo FASEB J. 17 2003 1355 1357
    • (2003) FASEB J. , vol.17 , pp. 1355-1357
    • Schulz, R.1    Gres, P.2    Skyschally, A.3    Duschin, A.4    Belosjorow, S.5    Konietzka, I.6    Heusch, G.7
  • 98
    • 36248947234 scopus 로고    scopus 로고
    • Remodeling of gap junctions in ischemic and nonischemic forms of heart disease
    • J.E. Saffitz, K.Y. Hames, and S. Kanno Remodeling of gap junctions in ischemic and nonischemic forms of heart disease J. Membr. Biol. 218 2007 65 71
    • (2007) J. Membr. Biol. , vol.218 , pp. 65-71
    • Saffitz, J.E.1    Hames, K.Y.2    Kanno, S.3
  • 99
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium
    • C.E. Murry, R.B. Jennings, and K.A. Reimer Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium Circulation 74 1986 1124 1136
    • (1986) Circulation , vol.74 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 100
    • 0347635344 scopus 로고    scopus 로고
    • Role of connexin 43 in ischemic preconditioning does not involve intercellular communication through gap junctions
    • X. Li, F.R. Heinzel, K. Boengler, R. Schulz, and G. Heusch Role of connexin 43 in ischemic preconditioning does not involve intercellular communication through gap junctions J. Mol. Cell. Cardiol. 36 2004 161 163
    • (2004) J. Mol. Cell. Cardiol. , vol.36 , pp. 161-163
    • Li, X.1    Heinzel, F.R.2    Boengler, K.3    Schulz, R.4    Heusch, G.5
  • 102
    • 0038407350 scopus 로고    scopus 로고
    • No ischemic preconditioning in heterozygous connexin 43-deficient mice - A further in vivo study
    • U. Schwanke, X. Li, R. Schulz, and G. Heusch No ischemic preconditioning in heterozygous connexin 43-deficient mice - a further in vivo study Basic Res. Cardiol. 98 2003 181 182
    • (2003) Basic Res. Cardiol. , vol.98 , pp. 181-182
    • Schwanke, U.1    Li, X.2    Schulz, R.3    Heusch, G.4
  • 103
    • 0037454041 scopus 로고    scopus 로고
    • Connexin43 as a determinant of myocardial infarct size following coronary occlusion in mice
    • S. Kanno, A. Kovacs, K.A. Yamada, and J.E. Saffitz Connexin43 as a determinant of myocardial infarct size following coronary occlusion in mice J. Am. Coll. Cardiol. 41 2003 681 686
    • (2003) J. Am. Coll. Cardiol. , vol.41 , pp. 681-686
    • Kanno, S.1    Kovacs, A.2    Yamada, K.A.3    Saffitz, J.E.4
  • 104
    • 1942438678 scopus 로고    scopus 로고
    • Connexin 43 and ischemic preconditioning
    • R. Schulz, and G. Heusch Connexin 43 and ischemic preconditioning Cardiovasc. Res. 62 2004 335 344
    • (2004) Cardiovasc. Res. , vol.62 , pp. 335-344
    • Schulz, R.1    Heusch, G.2
  • 106
    • 7444225800 scopus 로고    scopus 로고
    • Chronic regulation of the expression of gap junction proteins connexin40, connexin43, and connexin45 in neonatal rat cardiomyocytes
    • A. Salameh, P. Schneider, K. Muhlberg, A. Hagendorff, S. Dhein, and D. Pfeiffer Chronic regulation of the expression of gap junction proteins connexin40, connexin43, and connexin45 in neonatal rat cardiomyocytes Eur. J. Pharmacol. 503 2004 9 16
    • (2004) Eur. J. Pharmacol. , vol.503 , pp. 9-16
    • Salameh, A.1    Schneider, P.2    Muhlberg, K.3    Hagendorff, A.4    Dhein, S.5    Pfeiffer, D.6
  • 107
    • 70349251708 scopus 로고    scopus 로고
    • Replacement of connexin 43 by connexin 32 in a knock-in mice model attenuates aortic endothelium-derived hyperpolarizing factor-mediated relaxation
    • D. Lopez, A. Rodriguez-Sinovas, E. Agullo, A. Garcia, J.A. Sanchez, and D. Garcia-Dorado Replacement of connexin 43 by connexin 32 in a knock-in mice model attenuates aortic endothelium-derived hyperpolarizing factor-mediated relaxation Exp. Physiol. 94 2009 1088 1097
    • (2009) Exp. Physiol. , vol.94 , pp. 1088-1097
    • Lopez, D.1    Rodriguez-Sinovas, A.2    Agullo, E.3    Garcia, A.4    Sanchez, J.A.5    Garcia-Dorado, D.6
  • 108
    • 0942298111 scopus 로고    scopus 로고
    • Preservation of base-line hemodynamic function and loss of inducible cardioprotection in adult mice lacking protein kinase C epsilon
    • M.O. Gray, H.Z. Zhou, I. Schafhalter-Zoppoth, P. Zhu, D. Mochly-Rosen, and R.O. Messing Preservation of base-line hemodynamic function and loss of inducible cardioprotection in adult mice lacking protein kinase C epsilon J. Biol. Chem. 279 2004 3596 3604
    • (2004) J. Biol. Chem. , vol.279 , pp. 3596-3604
    • Gray, M.O.1    Zhou, H.Z.2    Schafhalter-Zoppoth, I.3    Zhu, P.4    Mochly-Rosen, D.5    Messing, R.O.6
  • 109
    • 0036023643 scopus 로고    scopus 로고
    • Targeted disruption of the protein kinase C epsilon gene abolishes the infarct size reduction that follows ischaemic preconditioning of isolated buffer-perfused mouse hearts
    • A.T. Saurin, D.J. Pennington, N.J. Raat, D.S. Latchman, M.J. Owen, and M.S. Marber Targeted disruption of the protein kinase C epsilon gene abolishes the infarct size reduction that follows ischaemic preconditioning of isolated buffer-perfused mouse hearts Cardiovasc. Res. 55 2002 672 680
    • (2002) Cardiovasc. Res. , vol.55 , pp. 672-680
    • Saurin, A.T.1    Pennington, D.J.2    Raat, N.J.3    Latchman, D.S.4    Owen, M.J.5    Marber, M.S.6
  • 110
    • 34548235903 scopus 로고    scopus 로고
    • Protein kinase Cepsilon mediates salutary effects on electrical coupling induced by ischemic preconditioning
    • T.J. Hund, D.L. Lerner, K.A. Yamada, R.B. Schuessler, and J.E. Saffitz Protein kinase Cepsilon mediates salutary effects on electrical coupling induced by ischemic preconditioning Hear. Rhythm. 4 2007 1183 1193
    • (2007) Hear. Rhythm. , vol.4 , pp. 1183-1193
    • Hund, T.J.1    Lerner, D.L.2    Yamada, K.A.3    Schuessler, R.B.4    Saffitz, J.E.5
  • 112
    • 33646084855 scopus 로고    scopus 로고
    • Administration of FGF-2 to the heart stimulates connexin-43 phosphorylation at protein kinase C target sites
    • W. Srisakuldee, B.E. Nickel, R.R. Fandrich, Z.S. Jiang, and E. Kardami Administration of FGF-2 to the heart stimulates connexin-43 phosphorylation at protein kinase C target sites Cell Commun. Adhes. 13 2006 13 19
    • (2006) Cell Commun. Adhes. , vol.13 , pp. 13-19
    • Srisakuldee, W.1    Nickel, B.E.2    Fandrich, R.R.3    Jiang, Z.S.4    Kardami, E.5
  • 113
    • 34548437020 scopus 로고    scopus 로고
    • Delta-opioid receptor activation before ischemia reduces gap junction permeability in ischemic myocardium by PKC-epsilon-mediated phosphorylation of connexin 43
    • T. Miura, T. Yano, K. Naitoh, M. Nishihara, T. Miki, M. Tanno, and K. Shimamoto Delta-opioid receptor activation before ischemia reduces gap junction permeability in ischemic myocardium by PKC-epsilon-mediated phosphorylation of connexin 43 Am. J. Physiol. Heart Circ. Physiol. 293 2007 H1425 H1431
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.293
    • Miura, T.1    Yano, T.2    Naitoh, K.3    Nishihara, M.4    Miki, T.5    Tanno, M.6    Shimamoto, K.7
  • 115
    • 80054693038 scopus 로고    scopus 로고
    • Oxidative stress-induced formation of a positive-feedback loop for the sustained activation of p38 MAPK leading to the loss of cell division in cardiomyocytes soon after birth
    • doi:10.1007/s00395-011-0178-8 doi: Epub ahead of print
    • D. Matsuyama, and K. Kawahara Oxidative stress-induced formation of a positive-feedback loop for the sustained activation of p38 MAPK leading to the loss of cell division in cardiomyocytes soon after birth Basic Res. Cardiol. 2011 doi: 10.1007/s00395-011-0178-8 Epub ahead of print
    • (2011) Basic Res. Cardiol.
    • Matsuyama, D.1    Kawahara, K.2
  • 116
    • 77958097322 scopus 로고    scopus 로고
    • Mitochondria-specific transgenic overexpression of connexin-43 simulates preconditioning-induced cytoprotection of stem cells
    • G. Lu, H. Haider, A. Porollo, and M. Ashraf Mitochondria-specific transgenic overexpression of connexin-43 simulates preconditioning-induced cytoprotection of stem cells Cardiovasc. Res. 88 2010 277 286
    • (2010) Cardiovasc. Res. , vol.88 , pp. 277-286
    • Lu, G.1    Haider, H.2    Porollo, A.3    Ashraf, M.4
  • 117
    • 84861614342 scopus 로고    scopus 로고
    • Connexins in the vasculature
    • A. Harris, D. Locke, Humana Press New York
    • C. de Wit, and S.E. Wolfe Connexins in the vasculature A. Harris, D. Locke, Connexins: A Guide 2009 Humana Press New York 457 468
    • (2009) Connexins: A Guide , pp. 457-468
    • De Wit, C.1    Wolfe, S.E.2
  • 118
    • 33846844784 scopus 로고    scopus 로고
    • Ca2+ and inositol 1,4,5-trisphosphate-mediated signaling across the myoendothelial junction
    • B.E. Isakson, S.I. Ramos, and B.R. Duling Ca2+ 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
    • 0014071399 scopus 로고
    • The ultrastructure of mammalian arterioles and precapillary sphincters
    • J.A. Rhodin 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
  • 120
    • 72049084553 scopus 로고    scopus 로고
    • Site-specific connexin phosphorylation is associated with reduced heterocellular communication between smooth muscle and endothelium
    • A.C. Straub, S.R. Johnstone, K.R. Heberlein, M.J. Rizzo, A.K. Best, S. Boitano, and B.E. Isakson Site-specific connexin phosphorylation is associated with reduced heterocellular communication between smooth muscle and endothelium J. Vasc. Res. 47 2010 277 286
    • (2010) J. Vasc. Res. , vol.47 , pp. 277-286
    • Straub, A.C.1    Johnstone, S.R.2    Heberlein, K.R.3    Rizzo, M.J.4    Best, A.K.5    Boitano, S.6    Isakson, B.E.7
  • 122
    • 68449098301 scopus 로고    scopus 로고
    • Oxidized phospholipid species promote in vivo differential cx43 phosphorylation and vascular smooth muscle cell proliferation
    • S.R. Johnstone, J. Ross, M.J. Rizzo, A.C. Straub, P.D. Lampe, N. Leitinger, and B.E. Isakson Oxidized phospholipid species promote in vivo differential cx43 phosphorylation and vascular smooth muscle cell proliferation Am. J. Pathol. 175 2009 916 924
    • (2009) Am. J. Pathol. , vol.175 , pp. 916-924
    • Johnstone, S.R.1    Ross, J.2    Rizzo, M.J.3    Straub, A.C.4    Lampe, P.D.5    Leitinger, N.6    Isakson, B.E.7
  • 123
    • 69249109191 scopus 로고    scopus 로고
    • TLR2 mediates gap junctional intercellular communication through connexin-43 in intestinal epithelial barrier injury
    • B. Ey, A. Eyking, G. Gerken, D.K. Podolsky, and E. Cario TLR2 mediates gap junctional intercellular communication through connexin-43 in intestinal epithelial barrier injury J. Biol. Chem. 284 2009 22332 22343
    • (2009) J. Biol. Chem. , vol.284 , pp. 22332-22343
    • Ey, B.1    Eyking, A.2    Gerken, G.3    Podolsky, D.K.4    Cario, E.5
  • 124
    • 20144382766 scopus 로고    scopus 로고
    • The phosphorylated form of connexin43 is up-regulated in breast hyperplasias and carcinomas and in their neoformed capillaries
    • V.E. Gould, J.M. Mosquera, K. Leykauf, P. Gattuso, M. Durst, and A. Alonso The phosphorylated form of connexin43 is up-regulated in breast hyperplasias and carcinomas and in their neoformed capillaries Hum. Pathol. 36 2005 536 545
    • (2005) Hum. Pathol. , vol.36 , pp. 536-545
    • Gould, V.E.1    Mosquera, J.M.2    Leykauf, K.3    Gattuso, P.4    Durst, M.5    Alonso, A.6
  • 125
    • 44349184836 scopus 로고    scopus 로고
    • Decreased levels of connexin43 result in impaired development of the mammary gland in a mouse model of oculodentodigital dysplasia
    • I. Plante, and D.W. Laird Decreased levels of connexin43 result in impaired development of the mammary gland in a mouse model of oculodentodigital dysplasia Dev. Biol. 318 2008 312 322
    • (2008) Dev. Biol. , vol.318 , pp. 312-322
    • Plante, I.1    Laird, D.W.2
  • 126
    • 12344301871 scopus 로고    scopus 로고
    • Expression and function of connexins in the epidermis, analyzed with transgenic mouse mutants
    • M. Kretz, K. Maass, and K. Willecke Expression and function of connexins in the epidermis, analyzed with transgenic mouse mutants Eur. J. Cell Biol. 83 2004 647 654
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 647-654
    • Kretz, M.1    Maass, K.2    Willecke, K.3
  • 127
    • 84920075952 scopus 로고    scopus 로고
    • Connexins in skin biology
    • A. Harris, D. Locke, Humana New York
    • T. Aasen, and D.P. Kelsell Connexins in skin biology A. Harris, D. Locke, Connexins: A Guide 2009 Humana New York 307 322
    • (2009) Connexins: A Guide , pp. 307-322
    • Aasen, T.1    Kelsell, D.P.2
  • 128
    • 28944433824 scopus 로고    scopus 로고
    • Temporal regulation of connexin phosphorylation in embryonic and adult tissues
    • T.J. King, and P.D. Lampe Temporal regulation of connexin phosphorylation in embryonic and adult tissues Biochim. Biophys. Acta 1719 2005 24 35
    • (2005) Biochim. Biophys. Acta , vol.1719 , pp. 24-35
    • King, T.J.1    Lampe, P.D.2
  • 129
    • 8444252937 scopus 로고    scopus 로고
    • Protein kinase C spatially and temporally regulates gap junctional communication during human wound repair via phosphorylation of connexin43 on serine368
    • T.S. Richards, C.A. Dunn, W.G. Carter, M.L. Usui, J.E. Olerud, and P.D. Lampe Protein kinase C spatially and temporally regulates gap junctional communication during human wound repair via phosphorylation of connexin43 on serine368 J. Cell Biol. 167 2004 555 562
    • (2004) J. Cell Biol. , vol.167 , pp. 555-562
    • Richards, T.S.1    Dunn, C.A.2    Carter, W.G.3    Usui, M.L.4    Olerud, J.E.5    Lampe, P.D.6
  • 130
    • 84861614343 scopus 로고    scopus 로고
    • Connexins in the female reproductive system
    • A. Harris, D. Locke, Humana Press New York
    • G.M. Kidder, and E. Winterhager Connexins in the female reproductive system A. Harris, D. Locke, Connexins: A Guide 2009 Humana Press New York 481 494
    • (2009) Connexins: A Guide , pp. 481-494
    • Kidder, G.M.1    Winterhager, E.2
  • 131
    • 0027986578 scopus 로고
    • Phosphorylation and expression of connexin-43 ovarian gap junction protein are regulated by luteinizing hormone
    • I. Granot, and N. Dekel Phosphorylation and expression of connexin-43 ovarian gap junction protein are regulated by luteinizing hormone J. Biol. Chem. 269 1994 30502 30509
    • (1994) J. Biol. Chem. , vol.269 , pp. 30502-30509
    • Granot, I.1    Dekel, N.2
  • 132
    • 14244260063 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase mediates luteinizing hormone-induced breakdown of communication and oocyte maturation in rat ovarian follicles
    • S. Sela-Abramovich, E. Chorev, D. Galiani, and N. Dekel Mitogen-activated protein kinase mediates luteinizing hormone-induced breakdown of communication and oocyte maturation in rat ovarian follicles Endocrinology 146 2005 1236 1244
    • (2005) Endocrinology , vol.146 , pp. 1236-1244
    • Sela-Abramovich, S.1    Chorev, E.2    Galiani, D.3    Dekel, N.4
  • 133
    • 79955787349 scopus 로고    scopus 로고
    • Phosphorylation of connexin 50 by protein kinase a enhances gap junction and hemichannel function
    • J. Liu, J.F. Ek Vitorin, S.T. Weintraub, S. Gu, Q. Shi, J.M. Burt, and J.X. Jiang Phosphorylation of connexin 50 by protein kinase a enhances gap junction and hemichannel function J. Biol. Chem. 286 2011 16914 16928
    • (2011) J. Biol. Chem. , vol.286 , pp. 16914-16928
    • Liu, J.1    Ek Vitorin, J.F.2    Weintraub, S.T.3    Gu, S.4    Shi, Q.5    Burt, J.M.6    Jiang, J.X.7


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