메뉴 건너뛰기




Volumn 60, Issue 2, 2003, Pages 421-430

Nitric oxide enhances de novo formation of endothelial gap junctions

Author keywords

Cell communication; Endothelial function; Gap junctions; Nitric oxide; Protein kinases

Indexed keywords

ADENOSINE PHOSPHATE; CONNEXIN 37; CONNEXIN 40; CONNEXIN 43; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; CYCLIC GMP; GUANOSINE PHOSPHATE; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; NITRIC OXIDE; NITRIC OXIDE DONOR; PROTEIN KINASE; SYNAPTOSOMAL ASSOCIATED PROTEIN; UNCLASSIFIED DRUG;

EID: 0242627404     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2003.04.001     Document Type: Article
Times cited : (51)

References (51)
  • 1
    • 0029974655 scopus 로고    scopus 로고
    • Connections with connexins: The molecular basis of direct intercellular signaling
    • Bruzzone R., White T.W., Paul D.L. Connections with connexins: the molecular basis of direct intercellular signaling. Eur. J. Biochem. 238:1996;1-27.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 1-27
    • Bruzzone, R.1    White, T.W.2    Paul, D.L.3
  • 2
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • Kumar N.M., Gilula N.B. The gap junction communication channel. Cell. 84:1996;381-388.
    • (1996) Cell , vol.84 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 3
    • 0033544876 scopus 로고    scopus 로고
    • Inhibition of endothelial cell migration, intercellular communication, and vascular tube formation by thromboxane A(2)
    • Ashton A.W., Yokota R., John G., Zhao S., Suadicani S.O., Spray D.C.et al. Inhibition of endothelial cell migration, intercellular communication, and vascular tube formation by thromboxane A(2). J. Biol. Chem. 274:1999;35562- 35570.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35562-35570
    • Ashton, A.W.1    Yokota, R.2    John, G.3    Zhao, S.4    Suadicani, S.O.5    Spray, D.C.6
  • 4
    • 0024852792 scopus 로고
    • Junctional communication is induced in migrating capillary endothelial cells
    • Pepper M.S., Spray D.C., Chanson M., Montesano R., Orci L., Meda P. Junctional communication is induced in migrating capillary endothelial cells. J. Cell Biol. 109:1989;3027-3038.
    • (1989) J. Cell Biol. , vol.109 , pp. 3027-3038
    • Pepper, M.S.1    Spray, D.C.2    Chanson, M.3    Montesano, R.4    Orci, L.5    Meda, P.6
  • 6
    • 0027419412 scopus 로고
    • Connexin40, a component of gap junctions in vascular endothelium, is restricted in its ability to interact with other connexins
    • Bruzzone R., Haefliger J.A., Gimlich R.L., Paul D.L. Connexin40, a component of gap junctions in vascular endothelium, is restricted in its ability to interact with other connexins. Mol. Biol. Cell. 4:1993;7-20.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 7-20
    • Bruzzone, R.1    Haefliger, J.A.2    Gimlich, R.L.3    Paul, D.L.4
  • 7
    • 0028283183 scopus 로고
    • Human connexin43 gap junction channels. Regulation of unitary conductances by phosphorylation
    • Moreno A.P., Saez J.C., Fishman G.I., Spray D.C. Human connexin43 gap junction channels. Regulation of unitary conductances by phosphorylation. Circ. Res. 74:1994;1050-1057.
    • (1994) Circ. Res. , vol.74 , pp. 1050-1057
    • Moreno, A.P.1    Saez, J.C.2    Fishman, G.I.3    Spray, D.C.4
  • 8
    • 0034682799 scopus 로고    scopus 로고
    • Regulation of connexin degradation as a mechanism to increase gap junction assembly and function
    • Musil L.S., Le A.C., VanSlyke J.K., Roberts L.M. Regulation of connexin degradation as a mechanism to increase gap junction assembly and function. J. Biol. Chem. 275:2000;25207-25215.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25207-25215
    • Musil, L.S.1    Le, A.C.2    Vanslyke, J.K.3    Roberts, L.M.4
  • 9
    • 0032555956 scopus 로고    scopus 로고
    • Rapid turnover of connexin43 in the adult rat heart
    • [see comments]
    • Beardslee M.A., Laing J.G., Beyer E.C., Saffitz J.E. Rapid turnover of connexin43 in the adult rat heart. Circ. Res. 83:1998;629-635. [see comments].
    • (1998) Circ. Res. , vol.83 , pp. 629-635
    • Beardslee, M.A.1    Laing, J.G.2    Beyer, E.C.3    Saffitz, J.E.4
  • 10
    • 0026541187 scopus 로고
    • Four novel members of the connexin family of gap junction proteins. Molecular cloning, expression, and chromosome mapping
    • Haefliger J.A., Bruzzone R., Jenkins N.A., Gilbert D.J., Copeland N.G., Paul D.L. Four novel members of the connexin family of gap junction proteins. Molecular cloning, expression, and chromosome mapping. J. Biol. Chem. 267:1992;2057-2064.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2057-2064
    • Haefliger, J.A.1    Bruzzone, R.2    Jenkins, N.A.3    Gilbert, D.J.4    Copeland, N.G.5    Paul, D.L.6
  • 12
    • 0026513477 scopus 로고
    • Molecular cloning and expression of rat connexin40, a gap junction protein expressed in vascular smooth muscle
    • Beyer E.C., Reed K.E., Westphale E.M., Kanter H.L., Larson D.M. Molecular cloning and expression of rat connexin40, a gap junction protein expressed in vascular smooth muscle. J. Membr. Biol. 127:1992;69-76.
    • (1992) J. Membr. Biol. , vol.127 , pp. 69-76
    • Beyer, E.C.1    Reed, K.E.2    Westphale, E.M.3    Kanter, H.L.4    Larson, D.M.5
  • 13
    • 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
  • 14
    • 0033952769 scopus 로고    scopus 로고
    • Human connexin40 gap junction channels are modulated by cAMP
    • [see comments]
    • van-Rijen H.V., van-Veen T.A., Hermans M.M., Jongsma H.J. Human connexin40 gap junction channels are modulated by cAMP. Cardiovasc. Res. 45:2000;941-951. [see comments].
    • (2000) Cardiovasc. Res. , vol.45 , pp. 941-951
    • Van-Rijen, H.V.1    Van-Veen, T.A.2    Hermans, M.M.3    Jongsma, H.J.4
  • 15
    • 0033534737 scopus 로고    scopus 로고
    • Role of heterocellular Gap junctional communication in endothelium-dependent smooth muscle hyperpolarization: Inhibition by a connexin-mimetic peptide
    • Dora K.A., Martin P.E.M., Chaytor A.T., Evans W.H., Garland C.J., Griffith T.M. Role of heterocellular Gap junctional communication in endothelium-dependent smooth muscle hyperpolarization: inhibition by a connexin-mimetic peptide. Biochem. Biophys. Res. Commun. 254:1999;27-31.
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 27-31
    • Dora, K.A.1    Martin, P.E.M.2    Chaytor, A.T.3    Evans, W.H.4    Garland, C.J.5    Griffith, T.M.6
  • 16
    • 0033569702 scopus 로고    scopus 로고
    • The endothelial component of cannabinoid-induced relaxation in rabbit mesenteric artery depends on gap junctional communication
    • Chaytor A.T., Martin P.E., Evans W.H., Randall M.D., Griffith T.M. The endothelial component of cannabinoid-induced relaxation in rabbit mesenteric artery depends on gap junctional communication. J. Physiol. Lond. 520:1999;539-550.
    • (1999) J. Physiol. Lond. , vol.520 , pp. 539-550
    • Chaytor, A.T.1    Martin, P.E.2    Evans, W.H.3    Randall, M.D.4    Griffith, T.M.5
  • 17
    • 0024565181 scopus 로고
    • Conduction of vasomotor responses in arterioles: A role for cell-to-cell coupling?
    • Segal S.S., Duling B.R. Conduction of vasomotor responses in arterioles: a role for cell-to-cell coupling? Am. J. Physiol. 256:1989;H838-H845.
    • (1989) Am. J. Physiol. , vol.256 , pp. 838-H845
    • Segal, S.S.1    Duling, B.R.2
  • 18
    • 0034737654 scopus 로고    scopus 로고
    • Impaired conduction of vasodilation along arterioles in connexin40-deficient mice
    • deWit C., Roos F., Bolz S.S., Kirchhoff S., Kruger O., Willecke K.et al. Impaired conduction of vasodilation along arterioles in connexin40-deficient mice. Circ. Res. 86:2000;649-655.
    • (2000) Circ. Res. , vol.86 , pp. 649-655
    • Dewit, C.1    Roos, F.2    Bolz, S.S.3    Kirchhoff, S.4    Kruger, O.5    Willecke, K.6
  • 19
    • 0036679371 scopus 로고    scopus 로고
    • Regulation of connexin43 by nitric oxide in primary uterine myocytes from term pregnant women
    • Roh C.R., Heo J.H., Yang S.H., Bae D.S. Regulation of connexin43 by nitric oxide in primary uterine myocytes from term pregnant women. Am. J. Obstet. Gynecol. 187:2002;434-440.
    • (2002) Am. J. Obstet. Gynecol. , vol.187 , pp. 434-440
    • Roh, C.R.1    Heo, J.H.2    Yang, S.H.3    Bae, D.S.4
  • 20
    • 0025652890 scopus 로고
    • Arginine blocks gap junctions between retinal horizontal cells
    • Miyachi E., Murakami M., Nakaki T. Arginine blocks gap junctions between retinal horizontal cells. NeuroReport. 1:1990;107-110.
    • (1990) NeuroReport , vol.1 , pp. 107-110
    • Miyachi, E.1    Murakami, M.2    Nakaki, T.3
  • 21
    • 0015822275 scopus 로고
    • Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria
    • Jaffe E.A., Nachman R.L., Becker C.G., Minick C.R. Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria. J. Clin. Invest. 52:1973;2745-2756.
    • (1973) J. Clin. Invest. , vol.52 , pp. 2745-2756
    • Jaffe, E.A.1    Nachman, R.L.2    Becker, C.G.3    Minick, C.R.4
  • 22
    • 0028915946 scopus 로고
    • Specific permeability and selective formation of gap junction channels in connexin-transfected HeLa cells
    • Elfgang C., Eckert R., Lichtenberg F.H., Butterweck A., Traub O., Klein R.A.et al. Specific permeability and selective formation of gap junction channels in connexin-transfected HeLa cells. J. Cell Biol. 129:1995;805-817.
    • (1995) J. Cell Biol. , vol.129 , pp. 805-817
    • Elfgang, C.1    Eckert, R.2    Lichtenberg, F.H.3    Butterweck, A.4    Traub, O.5    Klein, R.A.6
  • 23
    • 0027318152 scopus 로고
    • Specificity of gap junction communication among human mammary cells and connexin transfectants in culture
    • Tomasetto C., Neveu M.J., Daley J., Horan P.K., Sager R. Specificity of gap junction communication among human mammary cells and connexin transfectants in culture. J. Cell Biol. 122:1993;157-167.
    • (1993) J. Cell Biol. , vol.122 , pp. 157-167
    • Tomasetto, C.1    Neveu, M.J.2    Daley, J.3    Horan, P.K.4    Sager, R.5
  • 24
    • 0028819911 scopus 로고
    • Specific motifs in the external loops of connexin proteins can determine gap junction formation between chick heart myocytes
    • Warner A., Clements D.K., Parikh S., Evans W.H., DeHaan R.L. Specific motifs in the external loops of connexin proteins can determine gap junction formation between chick heart myocytes. J. Physiol. Lond. 488:1995;721-728.
    • (1995) J. Physiol. Lond. , vol.488 , pp. 721-728
    • Warner, A.1    Clements, D.K.2    Parikh, S.3    Evans, W.H.4    Dehaan, R.L.5
  • 26
    • 0029937924 scopus 로고    scopus 로고
    • A nitric oxide-sensitive electrode: Requirement of lower oxygen concentration for detecting nitric oxide from the tissue
    • Ishida Y., Hashimoto M., Fukushima S., Masumura S., Sasaki T., Nakayama K.et al. A nitric oxide-sensitive electrode: requirement of lower oxygen concentration for detecting nitric oxide from the tissue. J. Pharmacol. Toxicol. Methods. 35:1996;19-24.
    • (1996) J. Pharmacol. Toxicol. Methods , vol.35 , pp. 19-24
    • Ishida, Y.1    Hashimoto, M.2    Fukushima, S.3    Masumura, S.4    Sasaki, T.5    Nakayama, K.6
  • 27
    • 0029811304 scopus 로고    scopus 로고
    • Nitric oxide and superoxide anion production during endothelial cell proliferation
    • Arnal J.F., Tack I., Besombes J.P., Pipy B., Negre S.A. Nitric oxide and superoxide anion production during endothelial cell proliferation. Am. J. Physiol. 271:1996;C1521-C1526.
    • (1996) Am. J. Physiol. , vol.271 , pp. 1521-C1526
    • Arnal, J.F.1    Tack, I.2    Besombes, J.P.3    Pipy, B.4    Negre, S.A.5
  • 28
    • 0032813952 scopus 로고    scopus 로고
    • S-nitrosylation of proteins
    • Broillet M.C. S-nitrosylation of proteins. Cell. Mol. Life Sci. 55:1999;1036-1042.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 1036-1042
    • Broillet, M.C.1
  • 29
    • 0026340016 scopus 로고
    • Cytoprotective function of nitric oxide: Inactivation of superoxide radicals produced by human leukocytes
    • Rubanyi G.M., Ho E.H., Cantor E.H., Lumma W.C., Botelho L.H. Cytoprotective function of nitric oxide: inactivation of superoxide radicals produced by human leukocytes. Biochem. Biophys. Res. Commun. 181:1991;1392-1397.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 1392-1397
    • Rubanyi, G.M.1    Ho, E.H.2    Cantor, E.H.3    Lumma, W.C.4    Botelho, L.H.5
  • 30
    • 0032601592 scopus 로고    scopus 로고
    • Signal transduction by cGMP-dependent protein kinases and their emerging roles in the regulation of cell adhesion and gene expression
    • Eigenthaler M., Lohmann S.M., Walter U., Pilz R.B. Signal transduction by cGMP-dependent protein kinases and their emerging roles in the regulation of cell adhesion and gene expression. Rev. Physiol., Biochem. Pharmacol. 135:1999;173-209.
    • (1999) Rev. Physiol., Biochem. Pharmacol. , vol.135 , pp. 173-209
    • Eigenthaler, M.1    Lohmann, S.M.2    Walter, U.3    Pilz, R.B.4
  • 31
  • 32
    • 0033524751 scopus 로고    scopus 로고
    • Nitric oxide/cAMP interactions in the control of rat renal vascular resistance
    • Sandner P., Kornfeld M., Ruan X., Arendshorst W.J., Kurtz A. Nitric oxide/cAMP interactions in the control of rat renal vascular resistance. Circ. Res. 84:1999;186-192.
    • (1999) Circ. Res. , vol.84 , pp. 186-192
    • Sandner, P.1    Kornfeld, M.2    Ruan, X.3    Arendshorst, W.J.4    Kurtz, A.5
  • 33
    • 0025314048 scopus 로고
    • Molecular basis of the synergistic inhibition of platelet function by nitrovasodilators and activators of adenylate cyclase: Inhibition of cyclic AMP breakdown by cyclic GMP
    • Maurice D.H., Haslam R.J. Molecular basis of the synergistic inhibition of platelet function by nitrovasodilators and activators of adenylate cyclase: inhibition of cyclic AMP breakdown by cyclic GMP. Mol. Pharmacol. 37:1990;671-681.
    • (1990) Mol. Pharmacol. , vol.37 , pp. 671-681
    • Maurice, D.H.1    Haslam, R.J.2
  • 34
    • 85047678280 scopus 로고
    • Synergistic action of vasodilators that increase cGMP and cAMP in the hamster cremaster microcirculation
    • deWit C., von-Bismarck P., Pohl U. Synergistic action of vasodilators that increase cGMP and cAMP in the hamster cremaster microcirculation. Cardiovasc. Res. 28:1994;1513-1518.
    • (1994) Cardiovasc. Res. , vol.28 , pp. 1513-1518
    • Dewit, C.1    Von-Bismarck, P.2    Pohl, U.3
  • 35
    • 0027986509 scopus 로고
    • Inhibition of smooth muscle cell growth by nitric oxide and activation of cAMP-dependent protein kinase by cGMP
    • Cornwell T.L., Arnold E., Boerth N.J., Lincoln T.M. Inhibition of smooth muscle cell growth by nitric oxide and activation of cAMP-dependent protein kinase by cGMP. Am. J. Physiol. 267:1994;C1405-C1413.
    • (1994) Am. J. Physiol. , vol.267 , pp. 1405-C1413
    • Cornwell, T.L.1    Arnold, E.2    Boerth, N.J.3    Lincoln, T.M.4
  • 36
    • 0032559678 scopus 로고    scopus 로고
    • Modulation of Ca2+ channels by cyclic nucleotide cross activation of opposing protein kinases in rabbit portal vein
    • Ruiz-Velasco V., Zhong J., Hume J.R., Keef K.D. Modulation of Ca2+ channels by cyclic nucleotide cross activation of opposing protein kinases in rabbit portal vein. Circ. Res. 82:1998;557-565.
    • (1998) Circ. Res. , vol.82 , pp. 557-565
    • Ruiz-Velasco, V.1    Zhong, J.2    Hume, J.R.3    Keef, K.D.4
  • 37
    • 0025789648 scopus 로고
    • Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques
    • Musil L.S., Goodenough D.A. Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques. J. Cell Biol. 115:1991;1357-1374.
    • (1991) J. Cell Biol. , vol.115 , pp. 1357-1374
    • Musil, L.S.1    Goodenough, D.A.2
  • 38
    • 0034646872 scopus 로고    scopus 로고
    • Connexin expression and turnover: Implications for cardiac excitability
    • Saffitz J.E., Laing J.G., Yamada K.A. Connexin expression and turnover: implications for cardiac excitability. Circ. Res. 86:2000;723-728.
    • (2000) Circ. Res. , vol.86 , pp. 723-728
    • Saffitz, J.E.1    Laing, J.G.2    Yamada, K.A.3
  • 39
    • 0033012698 scopus 로고    scopus 로고
    • Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells
    • Jordan K., Solan J.L., Dominguez M., Sia M., Hand A., Lampe P.D.et al. Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells. Mol. Biol. Cell. 10:1999;2033-2050.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2033-2050
    • Jordan, K.1    Solan, J.L.2    Dominguez, M.3    Sia, M.4    Hand, A.5    Lampe, P.D.6
  • 40
    • 0031474609 scopus 로고    scopus 로고
    • Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network
    • Muniz M., Martin M.E., Hidalgo J., Velasco A. Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network. Proc. Natl. Acad. Sci. U. S. A. 94:1997;14461-14466.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 14461-14466
    • Muniz, M.1    Martin, M.E.2    Hidalgo, J.3    Velasco, A.4
  • 41
    • 0033551741 scopus 로고    scopus 로고
    • Presence of a complex containing vesicle-associated membrane protein 2 in rat parotid acinar cells and its disassembly upon activation of cAMP-dependent protein kinase
    • Fujita Y.J., Dohke Y., Hara Y.M., Furuyama S., Sugiya H. Presence of a complex containing vesicle-associated membrane protein 2 in rat parotid acinar cells and its disassembly upon activation of cAMP-dependent protein kinase. J. Biol. Chem. 274:1999;23642-23646.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23642-23646
    • Fujita, Y.J.1    Dohke, Y.2    Hara, Y.M.3    Furuyama, S.4    Sugiya, H.5
  • 42
    • 0030772349 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells
    • Katsura T., Gustafson C.E., Ausiello D.A., Brown D. Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells. Am. J. Physiol. 272:1997;F817-F822.
    • (1997) Am. J. Physiol. , vol.272 , pp. 817-F822
    • Katsura, T.1    Gustafson, C.E.2    Ausiello, D.A.3    Brown, D.4
  • 43
    • 0025838007 scopus 로고
    • Mouse connexin37: Cloning and functional expression of a gap junction gene highly expressed in lung
    • Willecke K., Heynkes R., Dahl E., Stutenkemper R., Hennemann H., Jungbluth S.et al. Mouse connexin37: cloning and functional expression of a gap junction gene highly expressed in lung. J. Cell Biol. 114:1991;1049-1057.
    • (1991) J. Cell Biol. , vol.114 , pp. 1049-1057
    • Willecke, K.1    Heynkes, R.2    Dahl, E.3    Stutenkemper, R.4    Hennemann, H.5    Jungbluth, S.6
  • 44
    • 0032761330 scopus 로고    scopus 로고
    • Sporadic cases of dilated cardiomyopathies associated with atrioventricular conduction defects are not linked to mutation within the connexins 40 and 43 genes
    • [letter]
    • Haefliger J.A., Goy J.J., Waeber G. Sporadic cases of dilated cardiomyopathies associated with atrioventricular conduction defects are not linked to mutation within the connexins 40 and 43 genes. Eur. Heart J. 20:1999;1843. [letter].
    • (1999) Eur. Heart J. , vol.20 , pp. 1843
    • Haefliger, J.A.1    Goy, J.J.2    Waeber, G.3
  • 45
    • 0025158107 scopus 로고
    • Protein kinase recognition sequence motifs
    • Kemp B.E., Pearson R.B. Protein kinase recognition sequence motifs. Trends Biochem. Sci. 15:1990;342-346.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 342-346
    • Kemp, B.E.1    Pearson, R.B.2
  • 46
    • 0027986578 scopus 로고
    • Phosphorylation and expression of connexin-43 ovarian gap junction protein are regulated by luteinizing hormone
    • Granot I., Dekel N. 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
  • 47
    • 0026527868 scopus 로고
    • Connexin43 in MDCK cells: Regulation by a tumor-promoting phorbol ester and Ca2+
    • Berthoud V.M., Ledbetter M.L., Hertzberg E.L., Saez J.C. Connexin43 in MDCK cells: regulation by a tumor-promoting phorbol ester and Ca2+. 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.2    Hertzberg, E.L.3    Saez, J.C.4
  • 48
    • 0028882497 scopus 로고
    • Differential regulation of distinct types of gap junction channels by similar phosphorylating conditions
    • Kwak B.R., Hermans M.M., De-Jonge H.R., Lohmann S.M., Jongsma H.J., Chanson M. Differential regulation of distinct types of gap junction channels by similar phosphorylating conditions. Mol. Biol. Cell. 6:1995;1707-1719.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1707-1719
    • Kwak, B.R.1    Hermans, M.M.2    De-Jonge, H.R.3    Lohmann, S.M.4    Jongsma, H.J.5    Chanson, M.6
  • 49
    • 0033828666 scopus 로고    scopus 로고
    • Cyclic AMP and LDL trigger a rapid enhancement in gap junction assembly through a stimulation of connexin trafficking
    • Paulson A.F., Lampe P.D., Meyer R.A., TenBroek E., Atkinson M.M., Walseth T.F.et al. Cyclic AMP and LDL trigger a rapid enhancement in gap junction assembly through a stimulation of connexin trafficking. J. Cell. Sci. 113:2000;3037-3049.
    • (2000) J. Cell. Sci. , vol.113 , pp. 3037-3049
    • Paulson, A.F.1    Lampe, P.D.2    Meyer, R.A.3    Tenbroek, E.4    Atkinson, M.M.5    Walseth, T.F.6
  • 50
    • 0036343776 scopus 로고    scopus 로고
    • Gap junctions assemble in the presence of cytoskeletal inhibitors, but enhanced assembly requires microtubules
    • Johnson R.G., Meyer R.A., Li X.R., Preus D.M., Tan L., Grunenwald H.et al. Gap junctions assemble in the presence of cytoskeletal inhibitors, but enhanced assembly requires microtubules. Exp. Cell Res. 275:2002;67-80.
    • (2002) Exp. Cell Res. , vol.275 , pp. 67-80
    • Johnson, R.G.1    Meyer, R.A.2    Li, X.R.3    Preus, D.M.4    Tan, L.5    Grunenwald, H.6
  • 51
    • 0036677449 scopus 로고    scopus 로고
    • Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells
    • Lauf U., Giepmans B.N., Lopez P., Braconnot S., Chen S.C., Falk M.M. Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc. Natl. Acad. Sci. U. S. A. 99:2002;10446-10451.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10446-10451
    • Lauf, U.1    Giepmans, B.N.2    Lopez, P.3    Braconnot, S.4    Chen, S.C.5    Falk, M.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.