메뉴 건너뛰기




Volumn 37, Issue 5, 2004, Pages 1013-1022

17β-estradiol reduces the effect of metabolic inhibition on gap junction intercellular communication in rat cardiomyocytes via the estrogen receptor

Author keywords

Connexin43; Membrane estrogen receptor; Metabolic inhibition; Non genomic effect; Serine368 phosphorylation; Signaling pathway

Indexed keywords

17ALPHA ESTRADIOL; BOVINE SERUM ALBUMIN; CHELERYTHRINE; ESTRADIOL; ESTRADIOL RECEPTOR; ESTRADIOL RECEPTOR ANTAGONIST; ESTROGEN RECEPTOR; FLUORESCEIN ISOTHIOCYANATE; IODOACETATE SODIUM; LIGAND; LUCIFER YELLOW; POTASSIUM CYANIDE; PROTEIN KINASE C INHIBITOR; RECEPTOR BLOCKING AGENT; SERINE; SODIUM DERIVATIVE; TAMOXIFEN; UNCLASSIFIED DRUG; ALKALOID; ANTIESTROGEN; BENZOPHENANTHRIDINE DERIVATIVE; CONNEXIN 43; ENZYME INHIBITOR; ESTROGEN RECEPTOR ALPHA; FLUORESCENT DYE; ISOQUINOLINE DERIVATIVE; PHENANTHRIDINE DERIVATIVE; PROTEIN KINASE C;

EID: 7444226471     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2004.08.003     Document Type: Article
Times cited : (33)

References (40)
  • 3
    • 0025155347 scopus 로고
    • Differential phosphorylation of the 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 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
  • 4
    • 0028168365 scopus 로고
    • Changes in gap-junction permeability, phosphorylation, and number mediated by phorbol ester and non-phorbol-ester tumor promoters in rat liver epithelial cells
    • D.F. Matesic, H.L. Rupp, W.J. Bonney, R.J. Ruch, and J.E. Trosko Changes in gap-junction permeability, phosphorylation, and number mediated by phorbol ester and non-phorbol-ester tumor promoters in rat liver epithelial cells Mol. Carcinog. 10 1994 226 236
    • (1994) Mol. Carcinog. , vol.10 , pp. 226-236
    • Matesic, D.F.1    Rupp, H.L.2    Bonney, W.J.3    Ruch, R.J.4    Trosko, J.E.5
  • 5
    • 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 Pt 1 1991 67 72
    • (1991) Biochem. J. , vol.273 , Issue.1 , pp. 67-72
    • Laird, D.W.1    Puranam, K.L.2    Revel, J.P.3
  • 6
    • 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
  • 7
    • 85047678630 scopus 로고
    • Assessment of techniques for preventing glycolysis in cardiac muscle
    • J.S. Pirolo, and D.G. Allen Assessment of techniques for preventing glycolysis in cardiac muscle Cardiovasc. Res. 20 1986 837 844
    • (1986) Cardiovasc. Res. , vol.20 , pp. 837-844
    • Pirolo, J.S.1    Allen, D.G.2
  • 8
    • 0024642593 scopus 로고
    • The effects of metabolic inhibition on intracellular calcium and pH in isolated rat ventricular cells
    • D.A. Eisner, C.G. Nichols, S.C. O'Neill, G.L. Smith, and M. Valdeolmillos The effects of metabolic inhibition on intracellular calcium and pH in isolated rat ventricular cells J. Physiol. 411 1989 393 418
    • (1989) J. Physiol. , vol.411 , pp. 393-418
    • Eisner, D.A.1    Nichols, C.G.2    O'Neill, S.C.3    Smith, G.L.4    Valdeolmillos, M.5
  • 9
    • 0031898246 scopus 로고    scopus 로고
    • Metabolic inhibition in the perfused rat heart: Evidence for glycolytic requirement for normal sodium homeostasis
    • J. Dizon, D. Burkhoff, J. Tauskela, J. Whang, P. Cannon, and J. Katz Metabolic inhibition in the perfused rat heart: evidence for glycolytic requirement for normal sodium homeostasis Am. J. Physiol. 274 1998 H1082 H1089
    • (1998) Am. J. Physiol. , vol.274
    • Dizon, J.1    Burkhoff, D.2    Tauskela, J.3    Whang, J.4    Cannon, P.5    Katz, J.6
  • 10
    • 0029989004 scopus 로고    scopus 로고
    • Characterization of the calcium overload in cultured neonatal rat cardiomyocytes under metabolic inhibition
    • S. Barrigon, S.Y. Wang, X. Ji, and G.A. Langer Characterization of the calcium overload in cultured neonatal rat cardiomyocytes under metabolic inhibition J. Mol. Cell. Cardiol. 28 1996 1329 1337
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 1329-1337
    • Barrigon, S.1    Wang, S.Y.2    Ji, X.3    Langer, G.A.4
  • 11
    • 0034644635 scopus 로고    scopus 로고
    • Dephosphorylation and intracellular redistribution of ventricular connexin43 during electrical uncoupling induced by ischemia
    • M.A. Beardslee, D.L. Lerner, P.N. Tadros, J.G. Laing, E.C. Beyer, and K.A. Yamada Dephosphorylation and intracellular redistribution 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    Laing, J.G.4    Beyer, E.C.5    Yamada, K.A.6
  • 12
    • 0025805333 scopus 로고
    • The role of ligand in estrogen receptor regulation of gene expression
    • F.E. Murdoch, and J. Gorski The role of ligand in estrogen receptor regulation of gene expression Mol. Cell. Endocrinol. 78 1991 C103 C108
    • (1991) Mol. Cell. Endocrinol. , vol.78
    • Murdoch, F.E.1    Gorski, J.2
  • 15
    • 0029862386 scopus 로고    scopus 로고
    • Gender differences in coronary artery diameter involve estrogen, nitric oxide, and Ca(2+)-dependent K+ channels
    • G.C. Wellman, A.D. Bonev, M.T. Nelson, and J.E. Brayden Gender differences in coronary artery diameter involve estrogen, nitric oxide, and Ca(2+)-dependent K+ channels Circ. Res. 79 1996 1024 1030
    • (1996) Circ. Res. , vol.79 , pp. 1024-1030
    • Wellman, G.C.1    Bonev, A.D.2    Nelson, M.T.3    Brayden, J.E.4
  • 16
    • 0032587165 scopus 로고    scopus 로고
    • Differential effects of 17beta-estradiol on mitogen-activated protein kinase pathways in rat cardiomyocytes
    • S. Nuedling, S. Kahlert, K. Loebbert, R. Meyer, H. Vetter, and C. Grohe Differential effects of 17beta-estradiol on mitogen-activated protein kinase pathways in rat cardiomyocytes FEBS Lett. 454 1999 271 276
    • (1999) FEBS Lett. , vol.454 , pp. 271-276
    • Nuedling, S.1    Kahlert, S.2    Loebbert, K.3    Meyer, R.4    Vetter, H.5    Grohe, C.6
  • 17
    • 0037350002 scopus 로고    scopus 로고
    • Anti-oxidant effects of estrogen reduce [Ca(2+)](i) during metabolic inhibition
    • K. Sugishita, F. Li, Z. Su, and W.H. Barry Anti-oxidant effects of estrogen reduce [Ca(2+)](i) during metabolic inhibition J. Mol. Cell. Cardiol. 35 2003 331 336
    • (2003) J. Mol. Cell. Cardiol. , vol.35 , pp. 331-336
    • Sugishita, K.1    Li, F.2    Su, Z.3    Barry, W.H.4
  • 18
    • 0030819430 scopus 로고    scopus 로고
    • Amelioration of ischemia- and reperfusion-induced myocardial injury by 17beta-estradiol: Role of nitric oxide and calcium-activated potassium channels
    • K. Node, M. Kitakaze, H. Kosaka, T. Minamino, H. Funaya, and M. Hori Amelioration of ischemia- and reperfusion-induced myocardial injury by 17beta-estradiol: role of nitric oxide and calcium-activated potassium channels Circulation 96 1997 1953 1963
    • (1997) Circulation , vol.96 , pp. 1953-1963
    • Node, K.1    Kitakaze, M.2    Kosaka, H.3    Minamino, T.4    Funaya, H.5    Hori, M.6
  • 19
    • 0037371343 scopus 로고    scopus 로고
    • Role of catenins in the development of gap junctions in rat cardiomyocytes
    • J.C. Wu, R.Y. Tsai, and T.H. Chung Role of catenins in the development of gap junctions in rat cardiomyocytes J. Cell Biochem. 88 2003 823 835
    • (2003) J. Cell Biochem. , vol.88 , pp. 823-835
    • Wu, J.C.1    Tsai, R.Y.2    Chung, T.H.3
  • 20
    • 0029919106 scopus 로고    scopus 로고
    • Mechanism of hydrogen peroxide and hydroxyl free radical-induced intracellular acidification in cultured rat cardiac myoblasts
    • M.L. Wu, K.L. Tsai, S.M. Wang, J.C. Wu, B.S. Wang, and Y.T. Lee Mechanism of hydrogen peroxide and hydroxyl free radical-induced intracellular acidification in cultured rat cardiac myoblasts Circ. Res. 78 1996 564 572
    • (1996) Circ. Res. , vol.78 , pp. 564-572
    • Wu, M.L.1    Tsai, K.L.2    Wang, S.M.3    Wu, J.C.4    Wang, B.S.5    Lee, Y.T.6
  • 21
    • 0033213803 scopus 로고    scopus 로고
    • N-cadherin/catenin-based costameres in cultured chicken cardiomyocytes
    • J.C. Wu, T.H. Chung, Y.Z. Tseng, and S.M. Wang N-cadherin/catenin-based costameres in cultured chicken cardiomyocytes J. Cell. Biochem. 75 1999 93 104
    • (1999) J. Cell. Biochem. , vol.75 , pp. 93-104
    • Wu, J.C.1    Chung, T.H.2    Tseng, Y.Z.3    Wang, S.M.4
  • 22
    • 0020369986 scopus 로고
    • Permeability and structural studies of heart cell gap junctions under normal and altered ionic conditions
    • J.M. Burt, J.S. Frank, and M.W. Berns Permeability and structural studies of heart cell gap junctions under normal and altered ionic conditions J. Membr. Biol. 68 1982 227 238
    • (1982) J. Membr. Biol. , vol.68 , pp. 227-238
    • Burt, J.M.1    Frank, J.S.2    Berns, M.W.3
  • 23
    • 0036586486 scopus 로고    scopus 로고
    • Dinitrophenol pretreatment of rat ventricular myocytes protects against damage by metabolic inhibition and reperfusion
    • G.C. Rodrigo, C.L. Lawrence, and N.B. Standen Dinitrophenol pretreatment of rat ventricular myocytes protects against damage by metabolic inhibition and reperfusion J. Mol. Cell Cardiol. 34 2002 555 569
    • (2002) J. Mol. Cell Cardiol. , vol.34 , pp. 555-569
    • Rodrigo, G.C.1    Lawrence, C.L.2    Standen, N.B.3
  • 26
    • 0033624571 scopus 로고    scopus 로고
    • Low concentrations of 17beta-estradiol protect single cardiac cells against metabolic stress-induced Ca2+ loading
    • S. Jovanovic, A. Jovanovic, W.K. Shen, and A. Terzic Low concentrations of 17beta-estradiol protect single cardiac cells against metabolic stress-induced Ca2+ loading J. Am. Coll. Cardiol. 36 2000 948 952
    • (2000) J. Am. Coll. Cardiol. , vol.36 , pp. 948-952
    • Jovanovic, S.1    Jovanovic, A.2    Shen, W.K.3    Terzic, A.4
  • 27
    • 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
  • 28
    • 0029757386 scopus 로고    scopus 로고
    • Gap-junction disassembly and connexin 43 dephosphorylation induced by 18 beta-glycyrrhetinic acid
    • X. Guan, S. Wilson, S.K.K. Wilson, and K.K.R.J. Schlender Gap-junction disassembly and connexin 43 dephosphorylation induced by 18 beta-glycyrrhetinic acid Mol. Carcinog. 16 1996 157 164
    • (1996) Mol. Carcinog. , vol.16 , pp. 157-164
    • Guan, X.1    Wilson, S.2    Wilson, S.K.K.3    Schlender, K.K.R.J.4
  • 29
    • 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
  • 30
    • 0031595599 scopus 로고    scopus 로고
    • 17beta-estradiol regulation of protein kinase C activity in chondrocytes is sex-dependent and involves nongenomic mechanisms
    • V.L. Sylvia, T. Hughes, D.D. Dean, B.D. Boyan, and Z. Schwartz 17beta-estradiol regulation of protein kinase C activity in chondrocytes is sex-dependent and involves nongenomic mechanisms J. Cell. Physiol. 176 1998 435 444
    • (1998) J. Cell. Physiol. , vol.176 , pp. 435-444
    • Sylvia, V.L.1    Hughes, T.2    Dean, D.D.3    Boyan, B.D.4    Schwartz, Z.5
  • 31
    • 0034538386 scopus 로고    scopus 로고
    • Calpain-mediated proteolytic cleavage of troponin I induced by hypoxia or metabolic inhibition in cultured neonatal cardiomyocytes
    • C. Kositprapa, B. Zhang, S. Berger, J.M. Canty Jr., and T.C. Lee Calpain-mediated proteolytic cleavage of troponin I induced by hypoxia or metabolic inhibition in cultured neonatal cardiomyocytes Mol. Cell Biochem. 214 2000 47 55
    • (2000) Mol. Cell Biochem. , vol.214 , pp. 47-55
    • Kositprapa, C.1    Zhang, B.2    Berger, S.3    Canty Jr., J.M.4    Lee, T.C.5
  • 32
    • 0037590100 scopus 로고    scopus 로고
    • Ischemic preconditioning preserves connexin43 phosphorylation during sustained ischemia in pig hearts in vivo
    • R. Schulz, P. Gres, A. Skyschally, A. Duschin, S. Belosjorow, and I. Konietzka Ischemic preconditioning preserves connexin43 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
  • 33
    • 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
  • 34
    • 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. 149 2000 1503 1512
    • (2000) J. Cell Biol. , vol.149 , 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
  • 37
    • 0035920110 scopus 로고    scopus 로고
    • Plasma membrane estrogen receptors are coupled to endothelial nitric-oxide synthase through Galpha(i)
    • M.H. Wyckoff, K.L. Chambliss, C. Mineo, I.S. Yuhanna, M.E. Mendelsohn, and S.M. Mumby Plasma membrane estrogen receptors are coupled to endothelial nitric-oxide synthase through Galpha(i) J. Biol. Chem. 276 2001 27071 27076
    • (2001) J. Biol. Chem. , vol.276 , pp. 27071-27076
    • Wyckoff, M.H.1    Chambliss, K.L.2    Mineo, C.3    Yuhanna, I.S.4    Mendelsohn, M.E.5    Mumby, S.M.6
  • 38
  • 40
    • 0033601863 scopus 로고    scopus 로고
    • Characterization of membrane estrogen binding proteins from rabbit uterus
    • P. Monje, and R. Boland Characterization of membrane estrogen binding proteins from rabbit uterus Mol. Cell. Endocrinol. 147 1999 75 84
    • (1999) Mol. Cell. Endocrinol. , vol.147 , pp. 75-84
    • Monje, P.1    Boland, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.