메뉴 건너뛰기




Volumn 290, Issue 5, 2006, Pages

eNOS translocation but not eNOS phosphorylation is dependent on intracellular Ca 2+ in human atrial myocardium

Author keywords

3 adrenoceptor; BRL 37344; Ca 2+ regulation; Cardiomyocyte; Heart

Indexed keywords

4 [2 [[2 (3 CHLOROPHENYL) 2 HYDROXYETHYL]AMINO]PROPYL]PHENOXYACETIC ACID; ADENYLATE CYCLASE ACTIVATOR; BETA 3 ADRENERGIC RECEPTOR STIMULATING AGENT; CALCIUM; CHELATING AGENT; ENDOTHELIAL NITRIC OXIDE SYNTHASE; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; FLUORESCEIN; FORSKOLIN; NITRIC OXIDE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; SERINE;

EID: 33646420374     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00005.2005     Document Type: Article
Times cited : (20)

References (40)
  • 2
    • 0029057806 scopus 로고
    • Nitric oxide-dependent parasympathetic signaling is due to activation of constitutive endothelial (type III) nitric oxide synthase in cardiac myocytes
    • Balligand JL, Kobzik L, Han X, Kaye DM, Belhassen L, O'Hara DS, Kelly RA, Smith TW, and Michel T. Nitric oxide-dependent parasympathetic signaling is due to activation of constitutive endothelial (type III) nitric oxide synthase in cardiac myocytes. J Biol Chem 270: 14582-14586, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 14582-14586
    • Balligand, J.L.1    Kobzik, L.2    Han, X.3    Kaye, D.M.4    Belhassen, L.5    O'Hara, D.S.6    Kelly, R.A.7    Smith, T.W.8    Michel, T.9
  • 3
    • 0037772382 scopus 로고    scopus 로고
    • Compensatory phosphorylation and protein-protein interactions revealed by loss of function and gain of function mutants of multiple serine phosphorylation sites in endothelial nitric-oxide synthase
    • Bauer PM, Fulton D, Boo YC, Sorescu GP, Kemp BE, Jo H, and Sessa WC. Compensatory phosphorylation and protein-protein interactions revealed by loss of function and gain of function mutants of multiple serine phosphorylation sites in endothelial nitric-oxide synthase. J Biol Chem 278: 14841-14849, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 14841-14849
    • Bauer, P.M.1    Fulton, D.2    Boo, Y.C.3    Sorescu, G.P.4    Kemp, B.E.5    Jo, H.6    Sessa, W.C.7
  • 4
    • 0026542534 scopus 로고
    • Intracellular calcium handling in isolated ventricular myocytes from patients with terminal heart failure
    • Beuckelmann DJ, Näbauer M, and Erdmann E. Intracellular calcium handling in isolated ventricular myocytes from patients with terminal heart failure. Circulation 85: 1046-1055, 1992.
    • (1992) Circulation , vol.85 , pp. 1046-1055
    • Beuckelmann, D.J.1    Näbauer, M.2    Erdmann, E.3
  • 9
    • 0025191219 scopus 로고
    • Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme
    • Bredt DS and Snyder SH. Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proc Natl Acad Sci USA 87: 682-685, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 682-685
    • Bredt, D.S.1    Snyder, S.H.2
  • 11
    • 0035980110 scopus 로고    scopus 로고
    • 2+-dependent to the late phosphorylation-dependent activation of the endothelial nitric-oxide synthase in vascular endothelial growth factor-exposed endothelial cells
    • 2+-dependent to the late phosphorylation-dependent activation of the endothelial nitric-oxide synthase in vascular endothelial growth factor-exposed endothelial cells. J Biol Chem 276: 32663-32669, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 32663-32669
    • Brouet, A.1    Sonveaux, P.2    Dessy, C.3    Balligand, J.L.4    Feron, O.5
  • 12
    • 0033542476 scopus 로고    scopus 로고
    • Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
    • Dimmeler S, Fleming I, Fisslthaler B, Hermann C, Busse R, and Zeiher AM. Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation. Nature 399: 601-605, 1999.
    • (1999) Nature , vol.399 , pp. 601-605
    • Dimmeler, S.1    Fleming, I.2    Fisslthaler, B.3    Hermann, C.4    Busse, R.5    Zeiher, A.M.6
  • 13
    • 2342476366 scopus 로고    scopus 로고
    • High-density lipoprotein and apolipoprotein AI increase endothelial NO synthase activity by protein association and multisite phosphorylation
    • Drew BG, Fidge NH, Gallon-Beaumier G, Kemp BE, and Kingwell BA. High-density lipoprotein and apolipoprotein AI increase endothelial NO synthase activity by protein association and multisite phosphorylation. Proc Natl Acad Sci USA 101: 6999-7004, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6999-7004
    • Drew, B.G.1    Fidge, N.H.2    Gallon-Beaumier, G.3    Kemp, B.E.4    Kingwell, B.A.5
  • 14
    • 0030990083 scopus 로고    scopus 로고
    • Calcium-dependent and calciumindependent activation of the endothelial NO synthase
    • Fleming I, Bauersachs J, and Busse R. Calcium-dependent and calciumindependent activation of the endothelial NO synthase. J Vasc Res 34: 165-174, 1997.
    • (1997) J Vasc Res , vol.34 , pp. 165-174
    • Fleming, I.1    Bauersachs, J.2    Busse, R.3
  • 17
    • 0032189129 scopus 로고    scopus 로고
    • The negative inotropic effect of β3-adrenoceptor stimulation is mediated by activation of a nitric oxide synthase pathway in human ventricle
    • Gauthier C, Leblais V, Kobzik L, Trochu JN, Khandoudi N, Bril A, Balligand JL, and Le Marec H. The negative inotropic effect of β3-adrenoceptor stimulation is mediated by activation of a nitric oxide synthase pathway in human ventricle. J Clin Invest 102: 1377-1384, 1998.
    • (1998) J Clin Invest , vol.102 , pp. 1377-1384
    • Gauthier, C.1    Leblais, V.2    Kobzik, L.3    Trochu, J.N.4    Khandoudi, N.5    Bril, A.6    Balligand, J.L.7    Le Marec, H.8
  • 19
    • 0033564442 scopus 로고    scopus 로고
    • Endomyocardial nitric oxide synthase and left ventricular preload reserve in dilated cardiomyopathy
    • Heymes C, Vanderheyden M, Bronzwaer JGF, Shah AM, and Paulus WJ. Endomyocardial nitric oxide synthase and left ventricular preload reserve in dilated cardiomyopathy. Circulation 99: 3009-3016, 1999.
    • (1999) Circulation , vol.99 , pp. 3009-3016
    • Heymes, C.1    Vanderheyden, M.2    Bronzwaer, J.G.F.3    Shah, A.M.4    Paulus, W.J.5
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0030271193 scopus 로고    scopus 로고
    • The role of nitric oxide and cell adhesion molecules on the microcirculation in ischaemia-reperfusion
    • Lefer AM and Lefer DJ. The role of nitric oxide and cell adhesion molecules on the microcirculation in ischaemia-reperfusion. Cardiovasc Res 32: 743-751, 1996.
    • (1996) Cardiovasc Res , vol.32 , pp. 743-751
    • Lefer, A.M.1    Lefer, D.J.2
  • 27
    • 0036511697 scopus 로고    scopus 로고
    • L-NAME enhances microcirculatory congestion and cardiomyocyte apoptosis during myocardial ischemia-reperfusion in rats
    • Liu P, Xu B, Forman LJ, Carsia R, and Hock CE. L-NAME enhances microcirculatory congestion and cardiomyocyte apoptosis during myocardial ischemia-reperfusion in rats. Shock 17: 185-192, 2002.
    • (2002) Shock , vol.17 , pp. 185-192
    • Liu, P.1    Xu, B.2    Forman, L.J.3    Carsia, R.4    Hock, C.E.5
  • 29
    • 0042917516 scopus 로고    scopus 로고
    • Nitric oxide and cardiac function: Ten years after, and continuing
    • Massion PB, Feron O, Dessy C, and Balligand JL. Nitric oxide and cardiac function: ten years after, and continuing. Circ Res 93: 388-398, 2003.
    • (2003) Circ Res , vol.93 , pp. 388-398
    • Massion, P.B.1    Feron, O.2    Dessy, C.3    Balligand, J.L.4
  • 30
    • 0030770629 scopus 로고    scopus 로고
    • Caveolin versus calmodulin: Counterbalancing allosteric modulators of endothelial nitric oxide synthase
    • Michel JB, Feron O, Sase K, Prabhakar P, and Michel T. Caveolin versus calmodulin: counterbalancing allosteric modulators of endothelial nitric oxide synthase. J Biol Chem 272: 25907-25912, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 25907-25912
    • Michel, J.B.1    Feron, O.2    Sase, K.3    Prabhakar, P.4    Michel, T.5
  • 31
    • 0036829884 scopus 로고    scopus 로고
    • Identification of regulatory sites of phosphorylation of the bovine endothelial nitric-oxide synthase at serine 617 and serine 635
    • Michell BJ, Harris MB, Chen Z, Ju H, Venema VJ, Blackstone MA, Huang W, Venema RC, and Kemp BE. Identification of regulatory sites of phosphorylation of the bovine endothelial nitric-oxide synthase at serine 617 and serine 635. J Biol Chem 277: 42344-42351, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 42344-42351
    • Michell, B.J.1    Harris, M.B.2    Chen, Z.3    Ju, H.4    Venema, V.J.5    Blackstone, M.A.6    Huang, W.7    Venema, R.C.8    Kemp, B.E.9
  • 35
    • 0035697136 scopus 로고    scopus 로고
    • Functional interaction of caveolin-1 and eNOS in myocardial capillary endothelium revealed by immunoelectron microscopy
    • Reiner M, Bloch W, and Addicks K. Functional interaction of caveolin-1 and eNOS in myocardial capillary endothelium revealed by immunoelectron microscopy. J Histochem Cytochem 49: 1605-1610, 2001.
    • (2001) J Histochem Cytochem , vol.49 , pp. 1605-1610
    • Reiner, M.1    Bloch, W.2    Addicks, K.3
  • 36
    • 0025273198 scopus 로고
    • Evidence against spare or uncoupled β-adrenoceptors in the human heart
    • Schwinger RH, Böhm M, and Erdmann E. Evidence against spare or uncoupled β-adrenoceptors in the human heart. Am Heart J 119: 899-904, 1990.
    • (1990) Am Heart J , vol.119 , pp. 899-904
    • Schwinger, R.H.1    Böhm, M.2    Erdmann, E.3
  • 37
    • 0025832167 scopus 로고
    • Different β-adrenoceptor-effector coupling in human ventricular and atrial myocardium
    • Schwinger RH, Böhm M, Pieske B, and Erdmann E. Different β-adrenoceptor-effector coupling in human ventricular and atrial myocardium. Eur J Clin Invest 21: 443-451, 1991.
    • (1991) Eur J Clin Invest , vol.21 , pp. 443-451
    • Schwinger, R.H.1    Böhm, M.2    Pieske, B.3    Erdmann, E.4
  • 39
    • 0028838821 scopus 로고
    • The calmodulin-nitric oxide synthase interaction: Critical role of the calmodulin latch domain in enzyme activation
    • Su Z, Blazing MA, Fan D, and George SE. The calmodulin-nitric oxide synthase interaction: critical role of the calmodulin latch domain in enzyme activation. J Biol Chem 270: 29117-29122, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 29117-29122
    • Su, Z.1    Blazing, M.A.2    Fan, D.3    George, S.E.4
  • 40
    • 0043234527 scopus 로고    scopus 로고
    • Synergistic activation of endothelial nitric-oxide synthase (eNOS) by HSP90 and Akt: Calcium-independent eNOS activation involves formation of an HSP90-Akt-CaM-bound eNOS complex
    • Takahashi S and Mendelsohn ME. Synergistic activation of endothelial nitric-oxide synthase (eNOS) by HSP90 and Akt: calcium-independent eNOS activation involves formation of an HSP90-Akt-CaM-bound eNOS complex. J Biol Chem 278: 30821-30827, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 30821-30827
    • Takahashi, S.1    Mendelsohn, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.