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Volumn 62, Issue 2, 2004, Pages 335-344

Connexin 43 and ischemic preconditioning

Author keywords

Connexin; Ischemia; Preconditioning; Reperfusion

Indexed keywords

ADENYLATE CYCLASE; CALCIUM; CASEIN KINASE; CONNEXIN 43; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC GMP; CYCLIC GMP DEPENDENT PROTEIN KINASE; CYTOSKELETON PROTEIN; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHODIESTERASE III; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; PROTEIN ZO1; PROTON;

EID: 1942438678     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2003.12.017     Document Type: Review
Times cited : (81)

References (143)
  • 1
    • 0034941724 scopus 로고    scopus 로고
    • Cardiac gap junction channels: Modulation of expression and channel properties
    • van Veen T.A.B., van Rijen H.V.M., Opthof T. Cardiac gap junction channels: modulation of expression and channel properties. Cardiovasc. Res. 51:2001;217-229.
    • (2001) Cardiovasc. Res. , vol.51 , pp. 217-229
    • Van Veen, T.A.B.1    Van Rijen, H.V.M.2    Opthof, T.3
  • 2
    • 0142088520 scopus 로고    scopus 로고
    • Cell coupling between ventricular myocyte pairs from connexin43-deficient murine hearts
    • Yao J.-A., Gutstein D.E., Liu F., Fishman G.I., Wit A.L. Cell coupling between ventricular myocyte pairs from connexin43-deficient murine hearts. Circ. Res. 93:2003;736-743.
    • (2003) Circ. Res. , vol.93 , pp. 736-743
    • Yao, J.-A.1    Gutstein, D.E.2    Liu, F.3    Fishman, G.I.4    Wit, A.L.5
  • 3
    • 0037039391 scopus 로고    scopus 로고
    • Metabolic inhibition induces opening of unopposed connexin 43 gap junction hemichannels and reduces gap junctional communication in cortical astrocytes in culture
    • Contreras J.E., Sánchez H.A., Eugenin E.A.et al. Metabolic inhibition induces opening of unopposed connexin 43 gap junction hemichannels and reduces gap junctional communication in cortical astrocytes in culture. Proc. Natl. Acad. Sci. U. S. A. 99:2002;495-500.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 495-500
    • Contreras, J.E.1    Sánchez, H.A.2    Eugenin, E.A.3
  • 4
    • 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., 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
  • 5
    • 0036237432 scopus 로고    scopus 로고
    • Gap junctions, homeostasis, and injury
    • De Maio A., Vega V.L. Gap junctions, homeostasis, and injury. J. Cell. Physiol. 191:2002;269-282.
    • (2002) J. Cell. Physiol. , vol.191 , pp. 269-282
    • De Maio, A.1    Vega, V.L.2
  • 6
    • 0035754503 scopus 로고    scopus 로고
    • Bisphosphonate-induced, hemichannel-mediated, anti-apoptosis through the Src/ERK pathway: A gap junction-independent action of connexin43
    • Plotkin L.I., Bellido T. Bisphosphonate-induced, hemichannel-mediated, anti-apoptosis through the Src/ERK pathway: a gap junction-independent action of connexin43. Cell Adhes. Commun. 8:2001;377-382.
    • (2001) Cell Adhes. Commun. , vol.8 , pp. 377-382
    • Plotkin, L.I.1    Bellido, T.2
  • 7
    • 0034611012 scopus 로고    scopus 로고
    • Physiological role of gap-junctional hemichannels. Extracellular calcium-dependent isosmotic volume regulation
    • Quist A.P., Rhee S.K., Lin H., Lal R. Physiological role of gap-junctional hemichannels. Extracellular calcium-dependent isosmotic volume regulation. J. Cell Biol. 148:2000;1063-1074.
    • (2000) J. Cell Biol. , vol.148 , pp. 1063-1074
    • Quist, A.P.1    Rhee, S.K.2    Lin, H.3    Lal, R.4
  • 8
    • 0024356206 scopus 로고
    • The 43-kD polypeptide of heart gap junctions: Immunolocalization, topology, and functional domains
    • Yancey S.B., John S.A., Lal R., Austin B.J., Revel J.P. The 43-kD polypeptide of heart gap junctions: immunolocalization, topology, and functional domains. J. Cell Biol. 108:1989;2241-2254.
    • (1989) J. Cell Biol. , vol.108 , pp. 2241-2254
    • Yancey, S.B.1    John, S.A.2    Lal, R.3    Austin, B.J.4    Revel, J.P.5
  • 9
    • 0024592298 scopus 로고
    • Antisera directed against connexin43 peptides react with a 43-kD protein localized to gap junctions in myocardium and other tissues
    • Beyer E.C., Kistler J., Paul D.L., Goodenough D.A. Antisera directed against connexin43 peptides react with a 43-kD protein localized to gap junctions in myocardium and other tissues. J. Cell Biol. 108:1989;595-605.
    • (1989) J. Cell Biol. , vol.108 , pp. 595-605
    • Beyer, E.C.1    Kistler, J.2    Paul, D.L.3    Goodenough, D.A.4
  • 10
    • 0032557460 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • Toyofuku T., Yabuki M., Otsu K.et al. Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes. J. Biol. Chem. 273:1998;12725-12731.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12725-12731
    • Toyofuku, T.1    Yabuki, M.2    Otsu, K.3
  • 11
    • 0037155043 scopus 로고    scopus 로고
    • Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions
    • Barker R.J., Price R.L., Gourdie R.G. Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions. Circ. Res. 90:2002;317-324.
    • (2002) Circ. Res. , vol.90 , pp. 317-324
    • Barker, R.J.1    Price, R.L.2    Gourdie, R.G.3
  • 12
    • 0025934144 scopus 로고
    • Biochemical and ultrastructural evidence for the association of basic fibroblast growth factor with cardiac gap junctions
    • Kardami E., Stoski R.M., Doble B.W.et al. Biochemical and ultrastructural evidence for the association of basic fibroblast growth factor with cardiac gap junctions. J. Biol. Chem. 266:1991;19551-19557.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19551-19557
    • Kardami, E.1    Stoski, R.M.2    Doble, B.W.3
  • 13
    • 0035806979 scopus 로고    scopus 로고
    • Gap junction protein connexin-43 interacts directly with microtubules
    • Giepmans B.N., Verlaan I., Hengeveld T.et al. Gap junction protein connexin-43 interacts directly with microtubules. Curr. Biol. 11:2001;1364-1368.
    • (2001) Curr. Biol. , vol.11 , pp. 1364-1368
    • Giepmans, B.N.1    Verlaan, I.2    Hengeveld, T.3
  • 14
    • 0028784986 scopus 로고
    • Selectivity of connexin-specific gap junctions does not correlate with channel conductance
    • Veenstra R.D., Wang H.-Z., Beblo D.A.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
  • 15
    • 0025246161 scopus 로고
    • Structure-activity relations of the cardiac gap junction channel
    • Spray D.C., Burt J.M. Structure-activity relations of the cardiac gap junction channel. Am. J. Physiol., Cell Physiol. 258:1990;C195-C205.
    • (1990) Am. J. Physiol., Cell Physiol. , vol.258 , pp. 195-C205
    • Spray, D.C.1    Burt, J.M.2
  • 17
    • 0026464786 scopus 로고
    • Cardiac gap junctions: Three distinct single channel conductances and their modulation by phosphorylating treatments
    • Takens-Kwak B.R., Jongsma H.J. Cardiac gap junctions: three distinct single channel conductances and their modulation by phosphorylating treatments. Pflügers Arch.-Eur. J. Physiol. 422:1992;198-200.
    • (1992) Pflügers Arch.-Eur. J. Physiol. , vol.422 , pp. 198-200
    • Takens-Kwak, B.R.1    Jongsma, H.J.2
  • 20
    • 0034106939 scopus 로고    scopus 로고
    • Analysis of connexin intracellular transport and assembly
    • VanSlyke J.K., Musil L.S. Analysis of connexin intracellular transport and assembly. Methods. 20:2000;156-164.
    • (2000) Methods , vol.20 , pp. 156-164
    • Vanslyke, J.K.1    Musil, L.S.2
  • 21
    • 0025155347 scopus 로고
    • Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell-lines
    • Musil L.S., Cunningham B.A., Edelman G.M., Goodenough D.A. Differential phosphorylation of the 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
  • 22
    • 0031214196 scopus 로고    scopus 로고
    • Phosphorylation of connexin43 and the regulation of neonatal rat cardiac myocyte gap junctions
    • Saez J.C., Nairn A.C., Czernik A.J.et al. Phosphorylation of connexin43 and the regulation of neonatal rat cardiac myocyte gap junctions. J. Mol. Cell. Cardiol. 29:1997;2131-2145.
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 2131-2145
    • Saez, J.C.1    Nairn, A.C.2    Czernik, A.J.3
  • 23
    • 0342879924 scopus 로고    scopus 로고
    • Use of antibodies in the analysis of connexin 43 turnover and phosphorylation
    • Hertzberg E.L., Sáez J.C., Corpina R.A., Roy C., Kessler J.A. Use of antibodies in the analysis of connexin 43 turnover and phosphorylation. Methods. 20:2000;129-139.
    • (2000) Methods , vol.20 , pp. 129-139
    • Hertzberg, E.L.1    Sáez, J.C.2    Corpina, R.A.3    Roy, C.4    Kessler, J.A.5
  • 24
    • 0029119513 scopus 로고
    • TPA increases conductance but decreases permeability in neonatal rat cardiomyocyte gap junction channels
    • Kwak B.R., van Veen T.A., Analbers L.J., Jongsma H.J. TPA increases conductance but decreases permeability in neonatal rat cardiomyocyte gap junction channels. Exp. Cell Res. 220:1995;456-463.
    • (1995) Exp. Cell Res. , vol.220 , pp. 456-463
    • Kwak, B.R.1    Van Veen, T.A.2    Analbers, L.J.3    Jongsma, H.J.4
  • 25
    • 0029878244 scopus 로고    scopus 로고
    • Regulation of cardiac gap junction channel permeability and conductance by several phosphorylating conditions
    • Kwak B.R., Jongsma H.J. Regulation of cardiac gap junction channel permeability and conductance by several phosphorylating conditions. Mol. Cell. Biochem. 157:1996;93-99.
    • (1996) Mol. Cell. Biochem. , vol.157 , pp. 93-99
    • Kwak, B.R.1    Jongsma, H.J.2
  • 29
    • 0023916274 scopus 로고
    • Inotropic agents modulate gap junctional conductance between cardiac myocytes
    • Burt J.M., Spray D.C. Inotropic agents modulate gap junctional conductance between cardiac myocytes. Am. J. Physiol., Heart Circ. Physiol. 254:1988;H1206-H1210.
    • (1988) Am. J. Physiol., Heart Circ. Physiol. , vol.254 , pp. 1206-H1210
    • Burt, J.M.1    Spray, D.C.2
  • 30
    • 0030070278 scopus 로고    scopus 로고
    • Impaired regulation of cell communication by β-adrenergic receptor activation in the failing heart
    • De Mello W.C. Impaired regulation of cell communication by β-adrenergic receptor activation in the failing heart. Hypertension. 27:1996;265-268.
    • (1996) Hypertension , vol.27 , pp. 265-268
    • De Mello, W.C.1
  • 31
    • 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.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
  • 32
    • 0034799390 scopus 로고    scopus 로고
    • Gap junction assembly: PTX-sensitive G proteins regulate the distribution of connexin43 within cells
    • Lampe P.D., Qiu Q., Meyer R.A.et al. Gap junction assembly: PTX-sensitive G proteins regulate the distribution of connexin43 within cells. Am. J. Physiol., Cell Physiol. 281:2001;C1211-C1222.
    • (2001) Am. J. Physiol., Cell Physiol. , vol.281 , pp. 1211-C1222
    • Lampe, P.D.1    Qiu, Q.2    Meyer, R.A.3
  • 33
    • 0033061853 scopus 로고    scopus 로고
    • Regulation of basal myocardial function by NO
    • Kojda G., Kottenberg K. Regulation of basal myocardial function by NO. Cardiovasc. Res. 41:1999;514-523.
    • (1999) Cardiovasc. Res. , vol.41 , pp. 514-523
    • Kojda, G.1    Kottenberg, K.2
  • 34
    • 0036065962 scopus 로고    scopus 로고
    • Vasoprotection by nitric oxide: Mechanisms and therapeutic potential
    • Gewaltig M.T., Kojda G. Vasoprotection by nitric oxide: mechanisms and therapeutic potential. Cardiovasc. Res. 55:2002;250-260.
    • (2002) Cardiovasc. Res. , vol.55 , pp. 250-260
    • Gewaltig, M.T.1    Kojda, G.2
  • 35
    • 0043269271 scopus 로고    scopus 로고
    • Regulation of nitric oxide-sensitive guanylyl cyclase
    • Friebe A., Koesling D. Regulation of nitric oxide-sensitive guanylyl cyclase. Circ. Res. 93:2003;96-105.
    • (2003) Circ. Res. , vol.93 , pp. 96-105
    • Friebe, A.1    Koesling, D.2
  • 36
    • 0035910607 scopus 로고    scopus 로고
    • Functional proteomic analysis of protein kinase C ε signaling complexes in the normal heart and during cardioprotection
    • Ping P., Zhang J., Pierce W.M., Bolli R. Functional proteomic analysis of protein kinase C ε signaling complexes in the normal heart and during cardioprotection. Circ. Res. 88:2001;59-62.
    • (2001) Circ. Res. , vol.88 , pp. 59-62
    • Ping, P.1    Zhang, J.2    Pierce, W.M.3    Bolli, R.4
  • 37
    • 0037590100 scopus 로고    scopus 로고
    • Ischemic preconditioning preserves connexin 43 phosphorylation during sustained ischemia in pig hearts in vivo
    • Schulz R., Gres P., Skyschally A.et al. 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
  • 38
    • 0033621884 scopus 로고    scopus 로고
    • The ε subtype of protein kinase C is required for cardiomyocyte connexin-43 phosphorylation
    • Doble B.W., Ping P., Kardami E. The ε 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
  • 39
    • 0034965843 scopus 로고    scopus 로고
    • Protein kinase C-α and -ε Modulate connexin-43 phosphorylation in human heart
    • Bowling N., Huang X., Sandusky G.E.et al. Protein kinase C-α and -ε modulate connexin-43 phosphorylation in human heart. J. Mol. Cell. Cardiol. 33:2001;789-798.
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 789-798
    • Bowling, N.1    Huang, X.2    Sandusky, G.E.3
  • 40
    • 0035757714 scopus 로고    scopus 로고
    • Protein kinase C-epsilon mediates phorbol ester-induced phosphorylation of connexin-43
    • Doble B.W., Ping P., Fandrich R.R., Cattani P.A., Kardami E. Protein kinase C-epsilon mediates phorbol ester-induced phosphorylation of connexin-43. Cell Adhes. Commun. 8:2001;253-256.
    • (2001) Cell Adhes. Commun. , vol.8 , pp. 253-256
    • Doble, B.W.1    Ping, P.2    Fandrich, R.R.3    Cattani, P.A.4    Kardami, E.5
  • 41
    • 0034717680 scopus 로고    scopus 로고
    • Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication
    • Lampe P.D., TenBreok E.M., Burt J.M.et al. Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication. J. Cell Biol. 149:2000;1503-1512.
    • (2000) J. Cell Biol. , vol.149 , pp. 1503-1512
    • Lampe, P.D.1    Tenbreok, E.M.2    Burt, J.M.3
  • 42
    • 0036634865 scopus 로고    scopus 로고
    • Pharmacological modification of gap junction coupling by an antiarrhythmic peptide via protein kinase C activation
    • Weng S., Lauven M., Schaefer T.et al. Pharmacological modification of gap junction coupling by an antiarrhythmic peptide via protein kinase C activation. FASEB J. 16:2002;1114-1116.
    • (2002) FASEB J. , vol.16 , pp. 1114-1116
    • Weng, S.1    Lauven, M.2    Schaefer, T.3
  • 43
    • 0033569865 scopus 로고    scopus 로고
    • Functional role of c-Src in gap junctions of the cardiomyopathic heart
    • Toyofuku T., Yabuki M., Kuzuya T., Tada M., Hori M. Functional role of c-Src in gap junctions of the cardiomyopathic heart. Circ. Res. 85:1999;672-681.
    • (1999) Circ. Res. , vol.85 , pp. 672-681
    • Toyofuku, T.1    Yabuki, M.2    Kuzuya, T.3    Tada, M.4    Hori, M.5
  • 44
    • 0035921428 scopus 로고    scopus 로고
    • V-Src phosphorylation of connexin 43 on Tyr247 and Tyr265 disrupts gap junctional communication
    • Lin R., Warn-Cramer B.J., Kurata W.E., Lau A.F. v-Src phosphorylation of connexin 43 on Tyr247 and Tyr265 disrupts gap junctional communication. J. Cell Biol. 4:2001;815-827.
    • (2001) J. Cell Biol. , vol.4 , pp. 815-827
    • Lin, R.1    Warn-Cramer, B.J.2    Kurata, W.E.3    Lau, A.F.4
  • 45
    • 0035750739 scopus 로고    scopus 로고
    • V-Src-mediated phosphorylation of connexin43 on tyrosine disrupts gap junctional communication in mammalian cells
    • Lin R., Warn-Cramer B.J., Kurata W.E., Lau A.F. v-Src-mediated phosphorylation of connexin43 on tyrosine disrupts gap junctional communication in mammalian cells. Cell Adhes. Commun. 8:2001;265-269.
    • (2001) Cell Adhes. Commun. , vol.8 , pp. 265-269
    • Lin, R.1    Warn-Cramer, B.J.2    Kurata, W.E.3    Lau, A.F.4
  • 46
    • 0037303074 scopus 로고    scopus 로고
    • Mechanism of v-src- and mitogen-activated protein kinase-induced reduction of gap junction communication
    • Cottrell G.T., Lin R., Warn-Cramer B.J., Lau A.F., Burt J.M. 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 , pp. 511-C520
    • Cottrell, G.T.1    Lin, R.2    Warn-Cramer, B.J.3    Lau, A.F.4    Burt, J.M.5
  • 47
    • 0029838641 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 decreases metabolic coupling and stimulates phosphorylation as well as masking of connexin43 epitopes in cardiac myocytes
    • Doble B.W., Chen Y., Bosc D.G., Litchfield D.W., Kardami E. Fibroblast growth factor-2 decreases metabolic coupling and stimulates phosphorylation as well as masking of connexin43 epitopes in cardiac myocytes. Circ. Res. 79:1996;647-658.
    • (1996) Circ. Res. , vol.79 , pp. 647-658
    • Doble, B.W.1    Chen, Y.2    Bosc, D.G.3    Litchfield, D.W.4    Kardami, E.5
  • 48
    • 0035910415 scopus 로고    scopus 로고
    • C-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes
    • Toyofuku T., Akamatsu Y., Zhang H., Tada M., Hori M. c-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes. J. Biol. Chem. 276:2001;1780-1788.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1780-1788
    • Toyofuku, T.1    Akamatsu, Y.2    Zhang, H.3    Tada, M.4    Hori, M.5
  • 49
    • 0036888480 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced reductions in cellular coupling correlate with tyrosine phosphorylation of connexin 43
    • Lidington D., Tyml K., Ouellette Y. Lipopolysaccharide-induced reductions in cellular coupling correlate with tyrosine phosphorylation of connexin 43. J. Cell. Physiol. 193:2002;373-379.
    • (2002) J. Cell. Physiol. , vol.193 , pp. 373-379
    • Lidington, D.1    Tyml, K.2    Ouellette, Y.3
  • 50
    • 0036357653 scopus 로고    scopus 로고
    • Chronic effects of endothelin 1 and angiotensin II on gap junctions and intercellular communication in cardiac cells
    • Polontchouk L., Ebelt B., Jackels M., Dhein S. Chronic effects of endothelin 1 and angiotensin II on gap junctions and intercellular communication in cardiac cells. FASEB J. 16:2002;87-89.
    • (2002) FASEB J. , vol.16 , pp. 87-89
    • Polontchouk, L.1    Ebelt, B.2    Jackels, M.3    Dhein, S.4
  • 51
    • 0035987781 scopus 로고    scopus 로고
    • The extracellular regulated kinases (ERK) 1/2 mediate cannabinoid-induced inhibition of gap junctional communication in endothelial cells
    • Brandes R.P., Popp R., Ott G.et al. The extracellular regulated kinases (ERK) 1/2 mediate cannabinoid-induced inhibition of gap junctional communication in endothelial cells. Br. J. Pharmacol. 136:2002;709-716.
    • (2002) Br. J. Pharmacol. , vol.136 , pp. 709-716
    • Brandes, R.P.1    Popp, R.2    Ott, G.3
  • 52
    • 0000210839 scopus 로고    scopus 로고
    • Gating connexin 43 channels reconstituted in lipid vesicles by mitogen-activated protein kinase phosphorylation
    • Kim D.Y., Kam Y., Koo S.K., Joe C.O. Gating connexin 43 channels reconstituted in lipid vesicles by mitogen-activated protein kinase phosphorylation. J. Biol. Chem. 274:1999;5581-5587.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5581-5587
    • Kim, D.Y.1    Kam, Y.2    Koo, S.K.3    Joe, C.O.4
  • 53
    • 0032502785 scopus 로고    scopus 로고
    • Regulation of connexin-43 gap junctional intercellular communication by mitogen-activated protein kinase
    • Warn-Cramer B.J., Cottrell G.T., Burt J.M., Lau A.F. Regulation of connexin-43 gap junctional intercellular communication by mitogen-activated protein kinase. J. Biol. Chem. 273:1998;9188-9196.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9188-9196
    • Warn-Cramer, B.J.1    Cottrell, G.T.2    Burt, J.M.3    Lau, A.F.4
  • 54
    • 0037705381 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor-induced connexin 43 gap junction communication by big mitogen-activated protein kinase 1/ERK 5 but not ERK1/2 kinase activation
    • Cameron S.J., Malik S., Akaibe M.et al. Regulation of epidermal growth factor-induced connexin 43 gap junction communication by big mitogen-activated protein kinase 1/ERK 5 but not ERK1/2 kinase activation. J. Biol. Chem. 278:2003;18682-18688.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18682-18688
    • Cameron, S.J.1    Malik, S.2    Akaibe, M.3
  • 55
    • 0037019966 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase activation mediates downregulation of connexin43 in cardiomyocytes
    • Petrich B.G., Gong X., Lerner D.L.et al. c-Jun N-terminal kinase activation mediates downregulation of connexin43 in cardiomyocytes. Circ. Res. 91:2002;640-647.
    • (2002) Circ. Res. , vol.91 , pp. 640-647
    • Petrich, B.G.1    Gong, X.2    Lerner, D.L.3
  • 56
    • 0037019951 scopus 로고    scopus 로고
    • JNK bond regulation. Why do mammalian hearts invest in connexin43?
    • Barker R.J., Gourdie R.G. JNK bond regulation. Why do mammalian hearts invest in connexin43? Circ. Res. 91:2002;556-558.
    • (2002) Circ. Res. , vol.91 , pp. 556-558
    • Barker, R.J.1    Gourdie, R.G.2
  • 57
    • 0030022421 scopus 로고    scopus 로고
    • Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein
    • Warn-Cramer B.J., Lampe P.D., Kurata W.E.et al. Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein. J. Biol. Chem. 271:1996;3779-3786.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3779-3786
    • Warn-Cramer, B.J.1    Lampe, P.D.2    Kurata, W.E.3
  • 58
    • 0029738476 scopus 로고    scopus 로고
    • Regulation of connexin43 function by activated tyrosine protein kinases
    • Lau A.F., Kurata W.E., Kanemitsu M.Y.et al. Regulation of connexin43 function by activated tyrosine protein kinases. J. Bioenerg. Biomembranes. 28:1996;359-368.
    • (1996) J. Bioenerg. Biomembranes , vol.28 , pp. 359-368
    • Lau, A.F.1    Kurata, W.E.2    Kanemitsu, M.Y.3
  • 59
    • 0037160066 scopus 로고    scopus 로고
    • Casein kinase 1 regulates connexin-43 gap junction assembly
    • Cooper C.D., Lampe P.D. Casein kinase 1 regulates connexin-43 gap junction assembly. J. Biol. Chem. 277:2003;44962-44968.
    • (2003) J. Biol. Chem. , vol.277 , pp. 44962-44968
    • Cooper, C.D.1    Lampe, P.D.2
  • 60
    • 0037286875 scopus 로고    scopus 로고
    • Ischemia-induced dephosphorylation of cardiomyocyte connexin-43 is reduced by okadaic acid and calyculin a but not fostriecin
    • Jeyaraman M., Tanguy S., Fandrich R.A., Lukas A., Kardami E. 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.A.3    Lukas, A.4    Kardami, E.5
  • 64
    • 0034595817 scopus 로고    scopus 로고
    • Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase
    • Sayed M., Kim S.O., Salh B.S., Issinger O.-G., Pelech S.L. Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase. J. Biol. Chem. 275:2000;16569-16573.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16569-16573
    • Sayed, M.1    Kim, S.O.2    Salh, B.S.3    Issinger, O.-G.4    Pelech, S.L.5
  • 65
    • 0033521115 scopus 로고    scopus 로고
    • Transcriptional regulation of endothelial nitric-oxide synthase by an interaction between casein kinase 2 and protein phosphatase 2A
    • Cieslik K., Lee C.-M., Tang J., Wu K.K. Transcriptional regulation of endothelial nitric-oxide synthase by an interaction between casein kinase 2 and protein phosphatase 2A. J. Biol. Chem. 274:1999;34669-34675.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34669-34675
    • Cieslik, K.1    Lee, C.-M.2    Tang, J.3    Wu, K.K.4
  • 66
    • 0034096201 scopus 로고    scopus 로고
    • Protein phosphatases and the regulation of mitogen-activated protein kinase signalling
    • Keyse S.M. Protein phosphatases and the regulation of mitogen-activated protein kinase signalling. Curr. Opin. Cell Biol. 12:2000;186-192.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 186-192
    • Keyse, S.M.1
  • 67
    • 0033991742 scopus 로고    scopus 로고
    • The calcium paradox revisited: An artefact of great heuristic value
    • Piper H.M. The calcium paradox revisited: an artefact of great heuristic value. Cardiovasc. Res. 45:2000;123-127.
    • (2000) Cardiovasc. Res. , vol.45 , pp. 123-127
    • Piper, H.M.1
  • 68
    • 0042330416 scopus 로고    scopus 로고
    • Role of apoptosis-inducing factor in myocardial cell death by ischemia-reperfusion
    • Kim G.-T., Chun Y.-S., Park J.-W., Kim M.-S. Role of apoptosis-inducing factor in myocardial cell death by ischemia-reperfusion. Biochem. Biophys. Res. Commun. 309:2003;619-624.
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 619-624
    • Kim, G.-T.1    Chun, Y.-S.2    Park, J.-W.3    Kim, M.-S.4
  • 72
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium
    • Murry C.E., Jennings R.B., Reimer K.A. 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
  • 74
    • 0031785657 scopus 로고    scopus 로고
    • Ischemic preconditioning attenuates apoptotic cell death associated with ischemia/reperfusion
    • Maulik N., Yoshida T., Engelman R.M.et al. Ischemic preconditioning attenuates apoptotic cell death associated with ischemia/reperfusion. Mol. Cell. Biochem. 186:1998;139-145.
    • (1998) Mol. Cell. Biochem. , vol.186 , pp. 139-145
    • Maulik, N.1    Yoshida, T.2    Engelman, R.M.3
  • 75
    • 0033984623 scopus 로고    scopus 로고
    • Preconditioning decreases Bax expression, PMN accumulation and apoptosis in reperfused rat heart
    • Nakamura M., Wang N.-P., Zhao Z.-Q.et al. Preconditioning decreases Bax expression, PMN accumulation and apoptosis in reperfused rat heart. Cardiovasc. Res. 45:2000;661-670.
    • (2000) Cardiovasc. Res. , vol.45 , pp. 661-670
    • Nakamura, M.1    Wang, N.-P.2    Zhao, Z.-Q.3
  • 76
    • 0033384684 scopus 로고    scopus 로고
    • Reperfusion arrhythmias in the murine heart: Their characteristics and alteration after ischemic preconditioning
    • Sakamoto J., Miura T., Tsuchida A.et al. Reperfusion arrhythmias in the murine heart: their characteristics and alteration after ischemic preconditioning. Basic Res. Cardiol. 94:1999;489-495.
    • (1999) Basic Res. Cardiol. , vol.94 , pp. 489-495
    • Sakamoto, J.1    Miura, T.2    Tsuchida, A.3
  • 77
    • 0001533131 scopus 로고
    • Preconditioning of ischemic myocardium: Reperfusion-induced arrhythmias
    • Shiki K., Hearse D.J. Preconditioning of ischemic myocardium: reperfusion-induced arrhythmias. Am. J. Physiol., Heart Circ. Physiol. 253:1987;H1470-H1476.
    • (1987) Am. J. Physiol., Heart Circ. Physiol. , vol.253 , pp. 1470-H1476
    • Shiki, K.1    Hearse, D.J.2
  • 78
    • 0026057713 scopus 로고
    • Effect of preconditioning ischemia on reperfusion arrhythmias after coronary artery occlusion and reperfusion in the rat
    • Hagar J.M., Hale S.L., Kloner R.A. Effect of preconditioning ischemia on reperfusion arrhythmias after coronary artery occlusion and reperfusion in the rat. Circ. Res. 68:1991;61-68.
    • (1991) Circ. Res. , vol.68 , pp. 61-68
    • Hagar, J.M.1    Hale, S.L.2    Kloner, R.A.3
  • 79
    • 0034997753 scopus 로고    scopus 로고
    • κ-but not δ-opioid receptors mediate effects of ischemic preconditioning on both infarct and arrhythmia in rats
    • Wang G.-Y., Wu S., Pei J.-M., Yu X.C., Wong T.-M. κ-but not δ-opioid receptors mediate effects of ischemic preconditioning on both infarct and arrhythmia in rats. Am. J. Physiol., Heart Circ. Physiol. 280:2001;H384-H391.
    • (2001) Am. J. Physiol., Heart Circ. Physiol. , vol.280 , pp. 384-H391
    • Wang, G.-Y.1    Wu, S.2    Pei, J.-M.3    Yu, X.C.4    Wong, T.-M.5
  • 80
    • 0028219202 scopus 로고
    • Conscious rabbits become tolerant to multiple episodes of ischemic preconditioning
    • Cohen M.V., Yang X.-M., Downey J.M. Conscious rabbits become tolerant to multiple episodes of ischemic preconditioning. Circ. Res. 74:1994;998-1004.
    • (1994) Circ. Res. , vol.74 , pp. 998-1004
    • Cohen, M.V.1    Yang, X.-M.2    Downey, J.M.3
  • 81
    • 0030272160 scopus 로고    scopus 로고
    • Time course of the protection against ischaemia and reperfusion-induced ventricular arrhythmias resulting from brief periods of cardiac pacing
    • Kaszala K., Vegh A., Papp J.G., Parratt J.R. Time course of the protection against ischaemia and reperfusion-induced ventricular arrhythmias resulting from brief periods of cardiac pacing. J. Mol. Cell. Cardiol. 28:1996;2085-2095.
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 2085-2095
    • Kaszala, K.1    Vegh, A.2    Papp, J.G.3    Parratt, J.R.4
  • 82
    • 0029111591 scopus 로고
    • Preconditioning reduces infarct size but accelerates time to ventricular fibrillation in ischemic pig heart
    • Ovize M., Aupetit J.-F., Rioufol G.et al. Preconditioning reduces infarct size but accelerates time to ventricular fibrillation in ischemic pig heart. Am. J. Physiol., Heart Circ. Physiol. 269:1995;H72-H79.
    • (1995) Am. J. Physiol., Heart Circ. Physiol. , vol.269 , pp. 72-H79
    • Ovize, M.1    Aupetit, J.-F.2    Rioufol, G.3
  • 83
    • 0029885842 scopus 로고    scopus 로고
    • Electrophysiogical characteristics of repetitive ischemic preconditioning in the pig heart
    • Shattock M.J., Lawson C.S., Hearse D.J., Downey J.M. Electrophysiogical characteristics of repetitive ischemic preconditioning in the pig heart. J. Mol. Cell. Cardiol. 28:1996;1339-1347.
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 1339-1347
    • Shattock, M.J.1    Lawson, C.S.2    Hearse, D.J.3    Downey, J.M.4
  • 88
    • 0023236236 scopus 로고
    • Regional myocardial blood flow, function and metabolism using phosphorus-31 nuclear magnetic resonance spectroscopy during ischemia and reperfusion
    • Guth B.D., Martin J.F., Heusch G., Ross J. Jr. Regional myocardial blood flow, function and metabolism using phosphorus-31 nuclear magnetic resonance spectroscopy during ischemia and reperfusion. J. Am. Coll. Cardiol. 10:1987;673-681.
    • (1987) J. Am. Coll. Cardiol. , vol.10 , pp. 673-681
    • Guth, B.D.1    Martin, J.F.2    Heusch, G.3    Ross, J.Jr.4
  • 89
    • 0032167375 scopus 로고    scopus 로고
    • Fostriecin, an inhibitor of protein phosphatase 2A, limits myocardial infarct size even when administered after onset of ischemia
    • Weinbrenner C., Baines C.P., Liu G.-C.et al. Fostriecin, an inhibitor of protein phosphatase 2A, limits myocardial infarct size even when administered after onset of ischemia. Circulation. 98:1998;899-905.
    • (1998) Circulation , vol.98 , pp. 899-905
    • Weinbrenner, C.1    Baines, C.P.2    Liu, G.-C.3
  • 90
    • 0033395842 scopus 로고    scopus 로고
    • Ischemia induced activation of heat shock protein 27 kinases and casein kinase 2 in the preconditioned rabbit heart
    • Kim S.O., Baines C.P., Critz S.D.et al. Ischemia induced activation of heat shock protein 27 kinases and casein kinase 2 in the preconditioned rabbit heart. Biochem. Cell Biol. 77:1999;559-567.
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 559-567
    • Kim, S.O.1    Baines, C.P.2    Critz, S.D.3
  • 91
    • 0033621128 scopus 로고    scopus 로고
    • Ischemic preconditioning and the β-adrenergic signal transduction pathway
    • Lochner A., Genade S., Tromp E., Podzuweit T., Moolman J.A. Ischemic preconditioning and the β-adrenergic signal transduction pathway. Circulation. 100:1999;958-966.
    • (1999) Circulation , vol.100 , pp. 958-966
    • Lochner, A.1    Genade, S.2    Tromp, E.3    Podzuweit, T.4    Moolman, J.A.5
  • 92
    • 0032987732 scopus 로고    scopus 로고
    • Protein kinase C translocation and PKC-dependent protein phosphorylation during myocardial ischemia
    • Albert C.J., Ford D.A. Protein kinase C translocation and PKC-dependent protein phosphorylation during myocardial ischemia. Am. J. Physiol., Heart Circ. Physiol. 276:1999;H642-H650.
    • (1999) Am. J. Physiol., Heart Circ. Physiol. , vol.276 , pp. 642-H650
    • Albert, C.J.1    Ford, D.A.2
  • 93
    • 0037345609 scopus 로고    scopus 로고
    • Ischemic preconditioning promotes a transient, but not sustained translocation of protein kinase C and sensitization of adenyl cyclase
    • Simonis G., Weinbrenner C., Strasser R.H. Ischemic preconditioning promotes a transient, but not sustained translocation of protein kinase C and sensitization of adenyl cyclase. Basic Res. Cardiol. 98:2003;104-118.
    • (2003) Basic Res. Cardiol. , vol.98 , pp. 104-118
    • Simonis, G.1    Weinbrenner, C.2    Strasser, R.H.3
  • 94
    • 0035200336 scopus 로고    scopus 로고
    • Src family kinase and adenosine differentially regulate multiple MAP kinases in ischemic myocardium: Modulation of MAP kinases activation by ischemic preconditioning
    • Takeishi Y., Huang Q., Wang T.et al. Src family kinase and adenosine differentially regulate multiple MAP kinases in ischemic myocardium: modulation of MAP kinases activation by ischemic preconditioning. J. Mol. Cell. Cardiol. 33:2001;1989-2005.
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 1989-2005
    • Takeishi, Y.1    Huang, Q.2    Wang, T.3
  • 96
    • 0029970021 scopus 로고    scopus 로고
    • Rapid adaptation of myocardial calcium homeostasis to short episodes of ischemia in isolated rat hearts
    • Smith G.B., Stefenelli T., Wu S.T.et al. Rapid adaptation of myocardial calcium homeostasis to short episodes of ischemia in isolated rat hearts. Am. Heart j. 131:1996;1106-1112.
    • (1996) Am. Heart J. , vol.131 , pp. 1106-1112
    • Smith, G.B.1    Stefenelli, T.2    Wu, S.T.3
  • 97
    • 0033840404 scopus 로고    scopus 로고
    • Intracellular free calcium and mitochondrial membrane potential in ischemia/reperfusion and preconditioning
    • Ylitalo K.V., Ala-Rami A., Liimatta E.V., Peuhkurine K.J., Hassinen I.E. Intracellular free calcium and mitochondrial membrane potential in ischemia/reperfusion and preconditioning. J. Mol. Cell. Cardiol. 32:2000;1223-1238.
    • (2000) J. Mol. Cell. Cardiol. , vol.32 , pp. 1223-1238
    • Ylitalo, K.V.1    Ala-Rami, A.2    Liimatta, E.V.3    Peuhkurine, K.J.4    Hassinen, I.E.5
  • 99
    • 0034644635 scopus 로고    scopus 로고
    • Dephosphorylation and intracellular redistributoin of ventricular connexin43 during electrical uncoupling induced by ischemia
    • Beardslee M.A., Lerner D.L., Tadros P.N.et al. Dephosphorylation and intracellular redistributoin of ventricular connexin43 during electrical uncoupling induced by ischemia. Circ. Res. 87:2000;656-662.
    • (2000) Circ. Res. , vol.87 , pp. 656-662
    • Beardslee, M.A.1    Lerner, D.L.2    Tadros, P.N.3
  • 100
    • 0038727330 scopus 로고    scopus 로고
    • Mechanisms of delayed electrical uncoupling induced by ischemic preconditioning
    • Jain S.K., Schuessler R.B., Saffitz J.E. 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
  • 103
    • 0033745550 scopus 로고    scopus 로고
    • Metabolic inhibition activates a non-selective current through connexin hemichannels in isolated ventricular myocytes
    • Kondo R.P., Wang S.Y., John S.A., Weiss J.N., Goldhaber J.I. Metabolic inhibition activates a non-selective current through connexin hemichannels in isolated ventricular myocytes. J. Mol. Cell. Cardiol. 32:2000;1859-1872.
    • (2000) J. Mol. Cell. Cardiol. , vol.32 , pp. 1859-1872
    • Kondo, R.P.1    Wang, S.Y.2    John, S.A.3    Weiss, J.N.4    Goldhaber, J.I.5
  • 105
    • 0032586953 scopus 로고    scopus 로고
    • 23Na NMR demonstrates prolonged increase of intracellular sodium following transient regional ischemia in the in situ pig heart
    • 23Na NMR demonstrates prolonged increase of intracellular sodium following transient regional ischemia in the in situ pig heart. Basic Res. Cardiol. 94:1999;60-69.
    • (1999) Basic Res. Cardiol. , vol.94 , pp. 60-69
    • Balschi, J.A.1
  • 108
    • 0030780568 scopus 로고    scopus 로고
    • Gap junction uncoupler heptanol prevents cell-to-cell progression of hypercontracture and limits necrosis during myocardial reperfusion
    • Garcia-Dorado D., Inserte J., Ruiz-Meana M.et al. Gap junction uncoupler heptanol prevents cell-to-cell progression of hypercontracture and limits necrosis during myocardial reperfusion. Circulation. 96:1997;3579-3586.
    • (1997) Circulation , vol.96 , pp. 3579-3586
    • Garcia-Dorado, D.1    Inserte, J.2    Ruiz-Meana, M.3
  • 109
    • 0034570579 scopus 로고    scopus 로고
    • Dephosphorylation agents depress gap junctional communication between rat cardiac cells without modifying the connexin43 phosphorylation degree
    • Duthe F., DuPont E., Verrechia F.et al. Dephosphorylation agents depress gap junctional communication between rat cardiac cells without modifying the connexin43 phosphorylation degree. Gen. Physiol. Biophys. 19:2000;441-449.
    • (2000) Gen. Physiol. Biophys. , vol.19 , pp. 441-449
    • Duthe, F.1    Dupont, E.2    Verrechia, F.3
  • 110
    • 0026499874 scopus 로고
    • Selective inhibition of the contractile apparatus. A new approach to modification of infarct size, infarct composition, and infarct geometry during coronary artery occlusion and reperfusion
    • Garcia-Dorado D., Théroux P., Duran J.M.et al. Selective inhibition of the contractile apparatus. A new approach to modification of infarct size, infarct composition, and infarct geometry during coronary artery occlusion and reperfusion. Circulation. 85:1992;1160-1174.
    • (1992) Circulation , vol.85 , pp. 1160-1174
    • Garcia-Dorado, D.1    Théroux, P.2    Duran, J.M.3
  • 112
    • 0035140850 scopus 로고    scopus 로고
    • Sarcolemmal blebs and osmotic fragility as correlates of irreversible ischemic injury in preconditioned isolated rabbit cardiomycytes
    • Armstrong S.C., Shivell C., Ganote C.E. Sarcolemmal blebs and osmotic fragility as correlates of irreversible ischemic injury in preconditioned isolated rabbit cardiomycytes. J. Mol. Cell. Cardiol. 33:2001;149-160.
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 149-160
    • Armstrong, S.C.1    Shivell, C.2    Ganote, C.E.3
  • 113
    • 0036081556 scopus 로고    scopus 로고
    • Acute protection of ischemic heart by FGF-2: Involvement of FGF-2 receptors and protein kinase C
    • Jiang Z.-S., Padua R.R., Ju H.et al. Acute protection of ischemic heart by FGF-2: involvement of FGF-2 receptors and protein kinase C. Am. J. Physiol., Heart Circ. Physiol. 282:2002;H1071-H1080.
    • (2002) Am. J. Physiol., Heart Circ. Physiol. , vol.282 , pp. 1071-H1080
    • Jiang, Z.-S.1    Padua, R.R.2    Ju, H.3
  • 114
    • 0032054071 scopus 로고    scopus 로고
    • Intramyocardial infusion of FGF-1 mimics ischemic preconditioning in pig myocardium
    • Htun P., Ito W.D., Hoefer I.E., Schaper J., Schaper W. Intramyocardial infusion of FGF-1 mimics ischemic preconditioning in pig myocardium. J. Mol. Cell. Cardiol. 30:1998;867-877.
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 867-877
    • Htun, P.1    Ito, W.D.2    Hoefer, I.E.3    Schaper, J.4    Schaper, W.5
  • 115
    • 0037216633 scopus 로고    scopus 로고
    • Biological activities of fibroblast growth factor-2 in the adult myocardium
    • Detillieux K.A., Sheikh F., Kardami E., Cattini P.A. Biological activities of fibroblast growth factor-2 in the adult myocardium. Cardiovasc. Res. 57:2003;8-19.
    • (2003) Cardiovasc. Res. , vol.57 , pp. 8-19
    • Detillieux, K.A.1    Sheikh, F.2    Kardami, E.3    Cattini, P.A.4
  • 116
    • 0035895240 scopus 로고    scopus 로고
    • Direct evidence for the participation of gap junction-mediated intercellular communication in the transmission of damage signals from alpha-particle irradiated to nonirradiated cells
    • Azzam E.I., de Toledo S.M., Little J.B. Direct evidence for the participation of gap junction-mediated intercellular communication in the transmission of damage signals from alpha-particle irradiated to nonirradiated cells. Proc. Natl. Acad. Sci. U. S. A. 98:2001;473-478.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 473-478
    • Azzam, E.I.1    De Toledo, S.M.2    Little, J.B.3
  • 117
    • 0036101594 scopus 로고    scopus 로고
    • The gap junction uncoupler heptanol abrogates infarct size reduction with preconditioning in mouse hearts
    • Li G., Whittaker P., Yao M., Kloner R.A., Przyklenk K. The gap junction uncoupler heptanol abrogates infarct size reduction with preconditioning in mouse hearts. Cardiovasc. Pathol. 11:2002;158-165.
    • (2002) Cardiovasc. Pathol. , vol.11 , pp. 158-165
    • Li, G.1    Whittaker, P.2    Yao, M.3    Kloner, R.A.4    Przyklenk, K.5
  • 118
  • 119
    • 0038407350 scopus 로고    scopus 로고
    • No ischemic preconditioning in heterozygous connexin 43-deficient mice: A further in vivo study
    • Schwanke U., Li X., Schulz R., Heusch G. 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
  • 120
    • 0142200955 scopus 로고    scopus 로고
    • Protection afforded by ischemic preconditioning is not mediated by effects on cell-to-cell electrical coupling during myocardial ischemia-reperfusion
    • Padilla F., Garcia-Dorado D., Rodriguez-Sinovas A.et al. Protection afforded by ischemic preconditioning is not mediated by effects on cell-to-cell electrical coupling during myocardial ischemia-reperfusion. Am. J. Physiol., Heart Circ. Physiol. 285:2003;H1909-H1916.
    • (2003) Am. J. Physiol., Heart Circ. Physiol. , vol.285 , pp. 1909-H1916
    • Padilla, F.1    Garcia-Dorado, D.2    Rodriguez-Sinovas, A.3
  • 121
    • 1942526389 scopus 로고    scopus 로고
    • No ischemic preconditioning of isolated cardiomyocytes from connexin 43-deficient mice
    • [in press]
    • Li X., Heinzel F.R., Boengler K., Schulz R., Heusch G. No ischemic preconditioning of isolated cardiomyocytes from connexin 43-deficient mice. J. Mol. Cell. Cardiol. 2004;. [in press].
    • (2004) J. Mol. Cell. Cardiol.
    • Li, X.1    Heinzel, F.R.2    Boengler, K.3    Schulz, R.4    Heusch, G.5
  • 122
    • 0036088319 scopus 로고    scopus 로고
    • Paradoxical overexpression and translocation of connexin 43 in homocysteine-treated endothelial cells
    • Li H., Brodsky S., Kumari S.et al. Paradoxical overexpression and translocation of connexin 43 in homocysteine-treated endothelial cells. Am. J. Physiol., Heart Circ. Physiol. 282:2001;H2124-H2133.
    • (2001) Am. J. Physiol., Heart Circ. Physiol. , vol.282 , pp. 2124-H2133
    • Li, H.1    Brodsky, S.2    Kumari, S.3
  • 123
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G., Reed J.C. Mitochondrial control of cell death. Nat. Med. 6:2000;513-519.
    • (2000) Nat. Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 124
    • 0037961037 scopus 로고    scopus 로고
    • Mitochondria and their role in preconditioning's trigger phase
    • Krieg T., Cohen M.V., Downey J.M. Mitochondria and their role in preconditioning's trigger phase. Basic Res. Cardiol. 98:2003;228-234.
    • (2003) Basic Res. Cardiol. , vol.98 , pp. 228-234
    • Krieg, T.1    Cohen, M.V.2    Downey, J.M.3
  • 125
    • 0142090601 scopus 로고    scopus 로고
    • Mitochondria as common endpoints in early and late preconditioning
    • Taimor G. Mitochondria as common endpoints in early and late preconditioning. Cardiovasc. Res. 59:2003;266-267.
    • (2003) Cardiovasc. Res. , vol.59 , pp. 266-267
    • Taimor, G.1
  • 126
    • 0037281030 scopus 로고    scopus 로고
    • The carboxy-tail of connexin-43 localizes to the nucleus and inhibits cell growth
    • Dang X., Doble B.W., Kardami E. The carboxy-tail of connexin-43 localizes to the nucleus and inhibits cell growth. Mol. Cell. Biochem. 242:2003;35-38.
    • (2003) Mol. Cell. Biochem. , vol.242 , pp. 35-38
    • Dang, X.1    Doble, B.W.2    Kardami, E.3
  • 127
    • 0034711508 scopus 로고    scopus 로고
    • The late phase of preconditioning
    • Bolli R. The late phase of preconditioning. Circ. Res. 87:2000;972-983.
    • (2000) Circ. Res. , vol.87 , pp. 972-983
    • Bolli, R.1
  • 128
    • 0037454041 scopus 로고    scopus 로고
    • Connexin 43 as a determinant of myocardial infarct size following coronary occlusion in mice
    • Kanno S., Kovacs A., Yamada K., Saffitz J. Connexin 43 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.3    Saffitz, J.4
  • 130
    • 0023161934 scopus 로고
    • Dependence of junctional conductance on proton, calcium and magnesium ions in cardiac paired cells of guinea-pig
    • Noma A., Tsuboi N. Dependence of junctional conductance on proton, calcium and magnesium ions in cardiac paired cells of guinea-pig. J. Physiol. 382:1987;193-211.
    • (1987) J. Physiol. , vol.382 , pp. 193-211
    • Noma, A.1    Tsuboi, N.2
  • 132
    • 0028170137 scopus 로고
    • (2+)-calmodulin mediated modulation of the electrical coupling of ventricular myocytes isolated from guinea pig heart
    • (2+)-calmodulin mediated modulation of the electrical coupling of ventricular myocytes isolated from guinea pig heart. J. Mol. Cell. Cardiol. 26:1994;1007-1015.
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 1007-1015
    • Toyama, J.1    Sugiura, H.2    Kamiya, K.3
  • 133
    • 0029099406 scopus 로고
    • Modification of gap junction conductance by divalent cations and protons in neonatal rat heart cells
    • Firek L., Weingart R. Modification of gap junction conductance by divalent cations and protons in neonatal rat heart cells. J. Mol. Cell. Cardiol. 27:1995;1633-1643.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 1633-1643
    • Firek, L.1    Weingart, R.2
  • 134
    • 0142024747 scopus 로고    scopus 로고
    • Proton permeation through the myocardial gap junction
    • Zaniboni M., Rossini A., Swietach P.et al. Proton permeation through the myocardial gap junction. Circ. Res. 93:2003;726-735.
    • (2003) Circ. Res. , vol.93 , pp. 726-735
    • Zaniboni, M.1    Rossini, A.2    Swietach, P.3
  • 135
    • 0025219686 scopus 로고
    • ATP directly affects junctional conductance between paired ventricular myocytes isolated from guinea pig heart
    • Sugiura H., Toyama J., Tsuboi N., Kamiya K., Kodama I. ATP directly affects junctional conductance between paired ventricular myocytes isolated from guinea pig heart. Circ. Res. 66:1990;1095-1102.
    • (1990) Circ. Res. , vol.66 , pp. 1095-1102
    • Sugiura, H.1    Toyama, J.2    Tsuboi, N.3    Kamiya, K.4    Kodama, I.5
  • 136
    • 0035195959 scopus 로고    scopus 로고
    • Endogenous protein phosphatase 1 runs down gap junctional communication of rat ventricular myocytes
    • Duthe F., Plaisance I., Sarrouilhe D., Hervé J.-C. Endogenous protein phosphatase 1 runs down gap junctional communication of rat ventricular myocytes. Am. J. Physiol., Cell Physiol. 281:2001;C1648-C1656.
    • (2001) Am. J. Physiol., Cell Physiol. , vol.281 , pp. 1648-C1656
    • Duthe, F.1    Plaisance, I.2    Sarrouilhe, D.3    Hervé, J.-C.4
  • 137
    • 0027322790 scopus 로고
    • Effects of phorbol ester on gap junctions of neonatal rat heart cells
    • Munster P.N., Weingart R. Effects of phorbol ester on gap junctions of neonatal rat heart cells. Pflügers Arch.-Eur. J. Physiol. 423:1993;181-188.
    • (1993) Pflügers Arch.-Eur. J. Physiol. , vol.423 , pp. 181-188
    • Munster, P.N.1    Weingart, R.2
  • 138
    • 0029913029 scopus 로고    scopus 로고
    • Effect of antipeptide antibodies directed against three domains of connexin43 on the gap junctional permeability of cultured cells
    • Bastide B., Jarry-Guichard T., Briand J.P., Délèze J., Gros D. Effect of antipeptide antibodies directed against three domains of connexin43 on the gap junctional permeability of cultured cells. J. Membr. Biol. 150:1996;243-253.
    • (1996) J. Membr. Biol. , vol.150 , pp. 243-253
    • Bastide, B.1    Jarry-Guichard, T.2    Briand, J.P.3    Délèze, J.4    Gros, D.5
  • 140
    • 0029781699 scopus 로고    scopus 로고
    • PH regulation of connexin43: Molecular analysis of the gating particle
    • Ek-Vitorin J.F., Calero G., Morley G.E.et al. pH regulation of connexin43: molecular analysis of the gating particle. Biophys. J. 71:1996;1273-1284.
    • (1996) Biophys. J. , vol.71 , pp. 1273-1284
    • Ek-Vitorin, J.F.1    Calero, G.2    Morley, G.E.3
  • 141
    • 0035881556 scopus 로고    scopus 로고
    • Pharmacological evidence for system-dependent involvement of protein kinase C isoenzymes in phorbol ester-suppressed gap junctional communication
    • Cruciani V., Husoy T., Mikalsen S.O. Pharmacological evidence for system-dependent involvement of protein kinase C isoenzymes in phorbol ester-suppressed gap junctional communication. Exp. Cell Res. 268:2001;150-161.
    • (2001) Exp. Cell Res. , vol.268 , pp. 150-161
    • Cruciani, V.1    Husoy, T.2    Mikalsen, S.O.3
  • 142
    • 0034838872 scopus 로고    scopus 로고
    • Inhibition of connexin43 gap junctional intercellular communication by TPA requires ERK activation
    • Ruch R.J., Trosko J.E., Madhukar B.V. Inhibition of connexin43 gap junctional intercellular communication by TPA requires ERK activation. J. Cell. Biochem. 83:2001;163-169.
    • (2001) J. Cell. Biochem. , vol.83 , pp. 163-169
    • Ruch, R.J.1    Trosko, J.E.2    Madhukar, B.V.3
  • 143
    • 0032498851 scopus 로고    scopus 로고
    • Acute loss of cell-cell communication caused by G protein-coupled receptors: A critical role for c-Src
    • Postma F.R., Hengeveld T., Alblas J.et al. Acute loss of cell-cell communication caused by G protein-coupled receptors: A critical role for c-Src. J. Cell Biol. 140:1998;1199-1209.
    • (1998) J. Cell Biol. , vol.140 , pp. 1199-1209
    • Postma, F.R.1    Hengeveld, T.2    Alblas, J.3


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