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Volumn 580, Issue 26, 2006, Pages 6039-6046

Localization of Kv1.5 channels in rat and canine myocyte sarcolemma

Author keywords

Cardiac myocytes; Caveolin; Kv channel; Lipid rafts

Indexed keywords

ALPHA ACTININ; BETA DYSTROGLYCAN; CAVEOLIN 3; ENDOTHELIAL NITRIC OXIDE SYNTHASE; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 33750530428     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.09.069     Document Type: Article
Times cited : (44)

References (48)
  • 3
    • 0347052880 scopus 로고    scopus 로고
    • Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95
    • Wong W., and Schlichter L.C. Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95. J. Biol. Chem. 279 (2004) 444-452
    • (2004) J. Biol. Chem. , vol.279 , pp. 444-452
    • Wong, W.1    Schlichter, L.C.2
  • 5
    • 0038581115 scopus 로고    scopus 로고
    • Ceramide inhibits the potassium channel Kv1.3 by the formation of membrane platforms
    • Bock J., Szabo I., Gamper N., Adams C., and Gulbins E. Ceramide inhibits the potassium channel Kv1.3 by the formation of membrane platforms. Biochem. Biophys. Res. Commun. 305 (2003) 890-897
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 890-897
    • Bock, J.1    Szabo, I.2    Gamper, N.3    Adams, C.4    Gulbins, E.5
  • 6
    • 0031667962 scopus 로고    scopus 로고
    • Mutational analysis of caveolin-induced vesicle formation. Expression of caveolin-1 recruits caveolin-2 to caveolae membranes
    • Li S., Galbiati F., Volonte D., Sargiacomo M., Engelman J.A., Das K., Scherer P.E., and Lisanti M.P. Mutational analysis of caveolin-induced vesicle formation. Expression of caveolin-1 recruits caveolin-2 to caveolae membranes. FEBS Lett. 434 (1998) 127-134
    • (1998) FEBS Lett. , vol.434 , pp. 127-134
    • Li, S.1    Galbiati, F.2    Volonte, D.3    Sargiacomo, M.4    Engelman, J.A.5    Das, K.6    Scherer, P.E.7    Lisanti, M.P.8
  • 7
    • 0035877753 scopus 로고    scopus 로고
    • Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and T-tubule abnormalities
    • Galbiati F., Engelman J.A., Volonte D., Zhang X.L., Minetti C., Li M., Hou Jr. H., Kneitz B., Edelmann W., and Lisanti M.P. Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and T-tubule abnormalities. J. Biol. Chem. 276 (2001) 21425-21433
    • (2001) J. Biol. Chem. , vol.276 , pp. 21425-21433
    • Galbiati, F.1    Engelman, J.A.2    Volonte, D.3    Zhang, X.L.4    Minetti, C.5    Li, M.6    Hou Jr., H.7    Kneitz, B.8    Edelmann, W.9    Lisanti, M.P.10
  • 10
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • Li S., Couet J., and Lisanti M.P. Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. J. Biol. Chem. 271 (1996) 29182-29190
    • (1996) J. Biol. Chem. , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 11
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains
    • Song K.S., Li S., Okamoto T., Quilliam L.A., Sargiacomo M., and Lisanti M.P. Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains. J. Biol. Chem. 271 (1996) 9690-9697
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 12
    • 0029787241 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase targeting to caveolae. Specific interactions with caveolin isoforms in cardiac myocytes and endothelial cells
    • Feron O., Belhassen L., Kobzik L., Smith T.W., Kelly R.A., and Michel T. Endothelial nitric oxide synthase targeting to caveolae. Specific interactions with caveolin isoforms in cardiac myocytes and endothelial cells. J. Biol. Chem. 271 (1996) 22810-22814
    • (1996) J. Biol. Chem. , vol.271 , pp. 22810-22814
    • Feron, O.1    Belhassen, L.2    Kobzik, L.3    Smith, T.W.4    Kelly, R.A.5    Michel, T.6
  • 13
    • 0034635437 scopus 로고    scopus 로고
    • Activated cardiac adenosine A(1) receptors translocate out of caveolae
    • Lasley R.D., Narayan P., Uittenbogaard A., and Smart E.J. Activated cardiac adenosine A(1) receptors translocate out of caveolae. J. Biol. Chem. 275 (2000) 4417-4421
    • (2000) J. Biol. Chem. , vol.275 , pp. 4417-4421
    • Lasley, R.D.1    Narayan, P.2    Uittenbogaard, A.3    Smart, E.J.4
  • 14
    • 0034869686 scopus 로고    scopus 로고
    • Accumulation of molecules involved in alpha1-adrenergic signal within caveolae: caveolin expression and the development of cardiac hypertrophy
    • Fujita T., Toya Y., Iwatsubo K., Onda T., Kimura K., Umemura S., and Ishikawa Y. Accumulation of molecules involved in alpha1-adrenergic signal within caveolae: caveolin expression and the development of cardiac hypertrophy. Cardiovasc. Res. 51 (2001) 709-716
    • (2001) Cardiovasc. Res. , vol.51 , pp. 709-716
    • Fujita, T.1    Toya, Y.2    Iwatsubo, K.3    Onda, T.4    Kimura, K.5    Umemura, S.6    Ishikawa, Y.7
  • 15
    • 0037072884 scopus 로고    scopus 로고
    • Caveolar localization dictates physiologic signaling of beta 2-adrenoceptors in neonatal cardiac myocytes
    • Xiang Y., Rybin V.O., Steinberg S.F., and Kobilka B. Caveolar localization dictates physiologic signaling of beta 2-adrenoceptors in neonatal cardiac myocytes. J. Biol. Chem. 277 (2002) 34280-34286
    • (2002) J. Biol. Chem. , vol.277 , pp. 34280-34286
    • Xiang, Y.1    Rybin, V.O.2    Steinberg, S.F.3    Kobilka, B.4
  • 16
    • 0035163568 scopus 로고    scopus 로고
    • Cardiac myocyte adenosine receptors and caveolae
    • Lasley R.D., and Smart E.J. Cardiac myocyte adenosine receptors and caveolae. Trends Cardiovasc. Med. 11 (2001) 259-263
    • (2001) Trends Cardiovasc. Med. , vol.11 , pp. 259-263
    • Lasley, R.D.1    Smart, E.J.2
  • 18
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • Nabi I.R., and Le P.U. Caveolae/raft-dependent endocytosis. J. Cell Biol. 161 (2003) 673-677
    • (2003) J. Cell Biol. , vol.161 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 19
    • 0242363240 scopus 로고    scopus 로고
    • 2+-dependent signal transduction
    • 2+-dependent signal transduction. Traffic 4 (2003) 717-723
    • (2003) Traffic , vol.4 , pp. 717-723
    • Isshiki, M.1    Anderson, R.G.2
  • 22
    • 0033744507 scopus 로고    scopus 로고
    • + channel remodeling in atrial fibrillation
    • + channel remodeling in atrial fibrillation. J. Mol. Cell. Cardiol. 32 (2000) 1763-1766
    • (2000) J. Mol. Cell. Cardiol. , vol.32 , pp. 1763-1766
    • Van Wagoner, D.R.1
  • 24
    • 0037107183 scopus 로고    scopus 로고
    • Phosphorylation-dependent and phosphorylation-independent modes of modulation of Shaker family voltage-gated potassium channels by Src family protein tyrosine kinases
    • Nitabach M.N., Llamas D.A., Thompson I.J., Collins K.A., and Holmes T.C. Phosphorylation-dependent and phosphorylation-independent modes of modulation of Shaker family voltage-gated potassium channels by Src family protein tyrosine kinases. J. Neurosci. 22 (2002) 7913-7922
    • (2002) J. Neurosci. , vol.22 , pp. 7913-7922
    • Nitabach, M.N.1    Llamas, D.A.2    Thompson, I.J.3    Collins, K.A.4    Holmes, T.C.5
  • 25
    • 0036156336 scopus 로고    scopus 로고
    • Modulation of Kv1.5 currents by protein kinase A, tyrosine kinase, and protein tyrosine phosphatase requires an intact cytoskeleton
    • Mason H.S., Latten M.J., Godoy L.D., Horowitz B., and Kenyon J.L. Modulation of Kv1.5 currents by protein kinase A, tyrosine kinase, and protein tyrosine phosphatase requires an intact cytoskeleton. Mol. Pharmacol. 61 (2002) 285-293
    • (2002) Mol. Pharmacol. , vol.61 , pp. 285-293
    • Mason, H.S.1    Latten, M.J.2    Godoy, L.D.3    Horowitz, B.4    Kenyon, J.L.5
  • 27
    • 0027414646 scopus 로고
    • Caveolae and sorting in the trans-Golgi network of epithelial cells
    • Dupree P., Parton R.G., Raposo G., Kurzchalia T.V., and Simons K. Caveolae and sorting in the trans-Golgi network of epithelial cells. EMBO J. 12 (1993) 1597-1605
    • (1993) EMBO J. , vol.12 , pp. 1597-1605
    • Dupree, P.1    Parton, R.G.2    Raposo, G.3    Kurzchalia, T.V.4    Simons, K.5
  • 28
    • 0030873019 scopus 로고    scopus 로고
    • Dynamic targeting of the agonist-stimulated m2 muscarinic acetylcholine receptor to caveolae in cardiac myocytes
    • Feron O., Smith T.W., Michel T., and Kelly R.A. Dynamic targeting of the agonist-stimulated m2 muscarinic acetylcholine receptor to caveolae in cardiac myocytes. J. Biol. Chem. 272 (1997) 17744-17748
    • (1997) J. Biol. Chem. , vol.272 , pp. 17744-17748
    • Feron, O.1    Smith, T.W.2    Michel, T.3    Kelly, R.A.4
  • 29
    • 0346121432 scopus 로고    scopus 로고
    • A caveolin-3 mutant that causes limb girdle muscular dystrophy type 1C disrupts Src localization and activity and induces apoptosis in skeletal myotubes
    • Smythe G.M., Eby J.C., Disatnik M.H., and Rando T.A. A caveolin-3 mutant that causes limb girdle muscular dystrophy type 1C disrupts Src localization and activity and induces apoptosis in skeletal myotubes. J. Cell Sci. 116 (2003) 4739-4749
    • (2003) J. Cell Sci. , vol.116 , pp. 4739-4749
    • Smythe, G.M.1    Eby, J.C.2    Disatnik, M.H.3    Rando, T.A.4
  • 30
    • 0037966553 scopus 로고    scopus 로고
    • SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism
    • Eldstrom J., Choi W.S., Steele D.F., and Fedida D. SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism. FEBS Lett. 547 (2003) 205-211
    • (2003) FEBS Lett. , vol.547 , pp. 205-211
    • Eldstrom, J.1    Choi, W.S.2    Steele, D.F.3    Fedida, D.4
  • 31
    • 0033729848 scopus 로고    scopus 로고
    • Distribution of proteins implicated in excitation-contraction coupling in rat ventricular myocytes
    • Scriven D.R., Dan P., and Moore E.D. Distribution of proteins implicated in excitation-contraction coupling in rat ventricular myocytes. Biophys. J. 79 (2000) 2682-2691
    • (2000) Biophys. J. , vol.79 , pp. 2682-2691
    • Scriven, D.R.1    Dan, P.2    Moore, E.D.3
  • 32
    • 0025857418 scopus 로고
    • Response of isolated adult canine cardiac myocytes to prolonged hypoxia and reoxygenation
    • Hohl C.M., and Altschuld R.A. Response of isolated adult canine cardiac myocytes to prolonged hypoxia and reoxygenation. Am. J. Physiol. 260 (1991) C383-C391
    • (1991) Am. J. Physiol. , vol.260
    • Hohl, C.M.1    Altschuld, R.A.2
  • 35
    • 0034640199 scopus 로고    scopus 로고
    • α-Actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells
    • Maruoka N.D., Steele D.F., Au B.P.Y., Dan P., Zhang X., Moore E.D.W., and Fedida D. α-Actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. FEBS Lett. 473 (2000) 188-194
    • (2000) FEBS Lett. , vol.473 , pp. 188-194
    • Maruoka, N.D.1    Steele, D.F.2    Au, B.P.Y.3    Dan, P.4    Zhang, X.5    Moore, E.D.W.6    Fedida, D.7
  • 37
    • 0027275642 scopus 로고
    • Signal-transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in Mdck cells
    • Sargiacomo M., Sudol M., Tang Z.L., and Lisanti M.P. Signal-transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in Mdck cells. J. Cell Biol. 122 (1993) 789-807
    • (1993) J. Cell Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.L.3    Lisanti, M.P.4
  • 38
    • 3242710394 scopus 로고    scopus 로고
    • Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the voltage-gated potassium channel Kv1.5
    • Folco E.J., Liu G.X., and Koren G. Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the voltage-gated potassium channel Kv1.5. Am. J. Physiol. - Heart Circ. Physiol. 287 (2004) H681-H690
    • (2004) Am. J. Physiol. - Heart Circ. Physiol. , vol.287
    • Folco, E.J.1    Liu, G.X.2    Koren, G.3
  • 39
    • 0037145814 scopus 로고    scopus 로고
    • N-terminal PDZ-binding domain in Kv1 potassium channels
    • Eldstrom J., Doerksen K.W., Steele D.F., and Fedida D. N-terminal PDZ-binding domain in Kv1 potassium channels. FEBS Lett. 531 (2002) 529-537
    • (2002) FEBS Lett. , vol.531 , pp. 529-537
    • Eldstrom, J.1    Doerksen, K.W.2    Steele, D.F.3    Fedida, D.4
  • 42
    • 0035980173 scopus 로고    scopus 로고
    • Gender-based differences in cardiac repolarization in mouse ventricle
    • Trepanier-Boulay V., St Michel C., Tremblay A., and Fiset C. Gender-based differences in cardiac repolarization in mouse ventricle. Circ. Res. 89 (2001) 437-444
    • (2001) Circ. Res. , vol.89 , pp. 437-444
    • Trepanier-Boulay, V.1    St Michel, C.2    Tremblay, A.3    Fiset, C.4
  • 44
    • 0036945719 scopus 로고    scopus 로고
    • Localization of sodium channels in intercalated disks modulates cardiac conduction
    • Kucera J.P., Rohr S., and Rudy Y. Localization of sodium channels in intercalated disks modulates cardiac conduction. Circ. Res. 91 (2002) 1176-1182
    • (2002) Circ. Res. , vol.91 , pp. 1176-1182
    • Kucera, J.P.1    Rohr, S.2    Rudy, Y.3
  • 45
    • 0037133689 scopus 로고    scopus 로고
    • An unexpected role for brain-type sodium channels in coupling of cell surface depolarization to contraction in the heart
    • Maier S.K., Westenbroek R.E., Schenkman K.A., Feigl E.O., Scheuer T., and Catterall W.A. An unexpected role for brain-type sodium channels in coupling of cell surface depolarization to contraction in the heart. Proc. Natl. Acad. Sci. USA 99 (2002) 4073-4078
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4073-4078
    • Maier, S.K.1    Westenbroek, R.E.2    Schenkman, K.A.3    Feigl, E.O.4    Scheuer, T.5    Catterall, W.A.6
  • 48
    • 0037113074 scopus 로고    scopus 로고
    • Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton
    • Mundy D.I., Machleidt T., Ying Y.S., Anderson R.G., and Bloom G.S. Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton. J. Cell Sci. 115 (2002) 4327-4339
    • (2002) J. Cell Sci. , vol.115 , pp. 4327-4339
    • Mundy, D.I.1    Machleidt, T.2    Ying, Y.S.3    Anderson, R.G.4    Bloom, G.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.