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Volumn 18, Issue 14, 2013, Pages 1739-1752

Disruption of endothelial cell mitochondrial bioenergetics in lambs with increased pulmonary blood flow

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CARNITINE ACETYLTRANSFERASE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; HEAT SHOCK PROTEIN 90; MANGANESE SUPEROXIDE DISMUTASE; N(G),N(G) DIMETHYLARGININE; NITRIC OXIDE; UNCOUPLING PROTEIN 2;

EID: 84875939562     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4806     Document Type: Review
Times cited : (35)

References (59)
  • 2
    • 0033971183 scopus 로고    scopus 로고
    • Altered regulation of the ET-1 cascade in lambs with increased pulmonary blood flow and pulmonary hypertension
    • Black SM, Bristow J, Soifer SJ, and Fineman Jr. Altered regulation of the ET-1 cascade in lambs with increased pulmonary blood flow and pulmonary hypertension. Pediatr Res 47: 97-106, 2000.
    • (2000) Pediatr Res , vol.47 , pp. 97-106
    • Black, S.M.1    Bristow, J.2    Soifer, S.J.3    Fineman, J.R.4
  • 3
    • 0031724886 scopus 로고    scopus 로고
    • Increased endothelial NOS in lambs with increased pulmonary blood flow and pulmonary hypertension
    • Black SM, Fineman JR, Steinhorn RH, Bristow J, and Soifer SJ. Increased endothelial NOS in lambs with increased pulmonary blood flow and pulmonary hypertension. Am J Physiol 275: H1643-H1651, 1998.
    • (1998) Am J Physiol , vol.275
    • Black, S.M.1    Fineman, J.R.2    Steinhorn, R.H.3    Bristow, J.4    Soifer, S.J.5
  • 5
    • 0037427445 scopus 로고    scopus 로고
    • Mitochondria and ischemic reperfusion damage in the adult and in the developing brain
    • Blomgren K, Zhu C, Hallin U, and Hagberg H. Mitochondria and ischemic reperfusion damage in the adult and in the developing brain. Biochem Biophys Res Commun 304: 551-559, 2003.
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 551-559
    • Blomgren, K.1    Zhu, C.2    Hallin, U.3    Hagberg, H.4
  • 6
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte S and Cordelieres FP. A guided tour into subcellular colocalization analysis in light microscopy. J Microsc 224: 213-232, 2006.
    • (2006) J Microsc , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2
  • 7
    • 0035834823 scopus 로고    scopus 로고
    • Hsp90 and caveolin are key targets for the proangiogenic nitric oxide-mediated effects of statins
    • Brouet A, Sonveaux P, Dessy C, Moniotte S, Balligand JL, and Feron O. Hsp90 and caveolin are key targets for the proangiogenic nitric oxide-mediated effects of statins. Circ Res 89: 866-873, 2001.
    • (2001) Circ Res , vol.89 , pp. 866-873
    • Brouet, A.1    Sonveaux, P.2    Dessy, C.3    Moniotte, S.4    Balligand, J.L.5    Feron, O.6
  • 8
    • 34249825521 scopus 로고    scopus 로고
    • Nitric oxide and mitochondria
    • Brown GC. Nitric oxide and mitochondria. Front Biosci 12: 1024-1033, 2007.
    • (2007) Front Biosci , vol.12 , pp. 1024-1033
    • Brown, G.C.1
  • 9
    • 28844438030 scopus 로고    scopus 로고
    • Antioxidant effect of L-carnitine and its short chain esters: Relevance for the protection from oxidative stress related cardiovascular damage
    • Calo LA, Pagnin E, Davis PA, Semplicini A, Nicolai R, Calvani M, and Pessina AC. Antioxidant effect of L-carnitine and its short chain esters: relevance for the protection from oxidative stress related cardiovascular damage. Int J Cardiol 107: 54-60, 2006.
    • (2006) Int J Cardiol , vol.107 , pp. 54-60
    • Calo, L.A.1    Pagnin, E.2    Davis, P.A.3    Semplicini, A.4    Nicolai, R.5    Calvani, M.6    Pessina, A.C.7
  • 10
    • 33644971702 scopus 로고    scopus 로고
    • Differences in eNOS activity because of subcellular localization are dictated by phosphor-ylation state rather than the local calcium environment
    • Church JE and Fulton D. Differences in eNOS activity because of subcellular localization are dictated by phosphor-ylation state rather than the local calcium environment. J Biol Chem 281: 1477-1488, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 1477-1488
    • Church, J.E.1    Fulton, D.2
  • 11
    • 0027374638 scopus 로고
    • A new method for the cytofluorimetric analysis of mitochondrial membrane potential using the J-aggregate forming lipophilic cation 5, 5¢, 6, 6¢-tetrachloro-1, 1¢, 3, 3¢-tetraethylbenzimidazolcarbocyanine iodide (JC-1)
    • Cossarizza A, Baccarani-Contri M, Kalashnikova G, and Franceschi C. A new method for the cytofluorimetric analysis of mitochondrial membrane potential using the J-aggregate forming lipophilic cation 5, 5¢, 6, 6¢-tetrachloro-1, 1¢, 3, 3¢-tetraethylbenzimidazolcarbocyanine iodide (JC-1). Biochem Biophys Res Commun 197: 40-45, 1993.
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 40-45
    • Cossarizza, A.1    Baccarani-Contri, M.2    Kalashnikova, G.3    Franceschi, C.4
  • 12
    • 0025561023 scopus 로고
    • Primary and secondary disorders of carnitine metabolism
    • DeVivo Da IT. Primary and secondary disorders of carnitine metabolism. Int J Pediatr 5: 135-141, 1990.
    • (1990) Int J Pediatr , vol.5 , pp. 135-141
    • Devivo Da, I.T.1
  • 13
    • 84862497436 scopus 로고    scopus 로고
    • Arginine attenuates methylglyoxal-and high glucose-induced endothelial dysfunction and oxidative stress by an endothelial nitric-oxide synthase-independent mechanism
    • Dhar I, Dhar A, Wu L, and Desai K. Arginine attenuates methylglyoxal-and high glucose-induced endothelial dysfunction and oxidative stress by an endothelial nitric-oxide synthase-independent mechanism. J Pharmacol Exp Ther 342: 196-204, 2012.
    • (2012) J Pharmacol Exp Ther , vol.342 , pp. 196-204
    • Dhar, I.1    Dhar, A.2    Wu, L.3    Desai, K.4
  • 14
    • 78149409004 scopus 로고    scopus 로고
    • The role of mitochondria in pulmonary vascular remodeling
    • Dromparis P, Sutendra G, and Michelakis ED. The role of mitochondria in pulmonary vascular remodeling. J Mol Med (Berl) 88: 1003-1010, 2010.
    • (2010) J Mol Med (Berl) , vol.88 , pp. 1003-1010
    • Dromparis, P.1    Sutendra, G.2    Michelakis, E.D.3
  • 15
    • 4043086952 scopus 로고    scopus 로고
    • Mitochondria in health and disease: Perspectives on a new mitochondrial biology
    • Duchen MR. Mitochondria in health and disease: perspectives on a new mitochondrial biology. Mol Aspects Med 25: 365-451, 2004.
    • (2004) Mol Aspects Med , vol.25 , pp. 365-451
    • Duchen, M.R.1
  • 16
    • 77954326413 scopus 로고    scopus 로고
    • The NO cascade, eNOS location, and microvascular permeability
    • Duran WN, Breslin JW, and Sanchez FA. The NO cascade, eNOS location, and microvascular permeability. Cardiovasc Res 87: 254-261, 2010.
    • (2010) Cardiovasc Res , vol.87 , pp. 254-261
    • Duran, W.N.1    Breslin, J.W.2    Sanchez, F.A.3
  • 17
    • 11144356896 scopus 로고    scopus 로고
    • Docking of endothelial nitric oxide synthase (eNOS) to the mitochondrial outer membrane: A pentabasic amino acid sequence in the autoinhibitory domain of eNOS targets a proteinase K-cleavable peptide on the cytoplasmic face of mitochondria
    • Gao S, Chen J, Brodsky SV, Huang H, Adler S, Lee JH, Dhadwal N, Cohen-Gould L, Gross SS, and Goligorsky MS. Docking of endothelial nitric oxide synthase (eNOS) to the mitochondrial outer membrane: a pentabasic amino acid sequence in the autoinhibitory domain of eNOS targets a proteinase K-cleavable peptide on the cytoplasmic face of mitochondria. J Biol Chem 279: 15968-15974, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 15968-15974
    • Gao, S.1    Chen, J.2    Brodsky, S.V.3    Huang, H.4    Adler, S.5    Lee, J.H.6    Dhadwal, N.7    Cohen-Gould, L.8    Gross, S.S.9    Goligorsky, M.S.10
  • 19
    • 0034698050 scopus 로고    scopus 로고
    • Reconstitution of an endothelial nitric-oxide synthase (eNOS), hsp90, and caveolin-1 complex in vitro. Evidence that hsp90 facilitates calmodulin stimulated displacement of eNOS from caveolin-1
    • Gratton JP, Fontana J, O'Connor DS, Garcia-Cardena G, McCabe TJ, and Sessa WC. Reconstitution of an endothelial nitric-oxide synthase (eNOS), hsp90, and caveolin-1 complex in vitro. Evidence that hsp90 facilitates calmodulin stimulated displacement of eNOS from caveolin-1. J Biol Chem 275: 22268-22272, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 22268-22272
    • Gratton, J.P.1    Fontana, J.2    O'Connor, D.S.3    Garcia-Cardena, G.4    McCabe, T.J.5    Sessa, W.C.6
  • 21
    • 0032997656 scopus 로고    scopus 로고
    • Chimeric forms of neuronal nitric oxide synthase identify different regions of the reductase domain that are essential for dimerization and activity
    • Hallmark OG, Phung YT, and Black SM. Chimeric forms of neuronal nitric oxide synthase identify different regions of the reductase domain that are essential for dimerization and activity. DNA Cell Biol 18: 397-407, 1999.
    • (1999) DNA Cell Biol , vol.18 , pp. 397-407
    • Hallmark, O.G.1    Phung, Y.T.2    Black, S.M.3
  • 23
    • 1542782162 scopus 로고    scopus 로고
    • Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubi-quitin ligase CHIP
    • Jiang J, Cyr D, Babbitt RW, Sessa WC, and Patterson C. Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubi-quitin ligase CHIP. J Biol Chem 278: 49332-49341, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 49332-49341
    • Jiang, J.1    Cyr, D.2    Babbitt, R.W.3    Sessa, W.C.4    Patterson, C.5
  • 24
    • 1942485280 scopus 로고    scopus 로고
    • Nitric oxide decreases endothelin-1 secretion through the activation of soluble guanylate cyclase
    • Kelly LK, Wedgwood S, Steinhorn RH, and Black SM. Nitric oxide decreases endothelin-1 secretion through the activation of soluble guanylate cyclase. Am J Physiol Lung Cell Mol Physiol 286: L984-L991, 2004.
    • (2004) Am J Physiol Lung Cell Mol Physiol , vol.286
    • Kelly, L.K.1    Wedgwood, S.2    Steinhorn, R.H.3    Black, S.M.4
  • 25
    • 0034717940 scopus 로고    scopus 로고
    • Fatty acid import into mitochondria
    • Kerner J and Hoppel C. Fatty acid import into mitochondria. Biochim Biophys Acta 1486: 1-17, 2000.
    • (2000) Biochim Biophys Acta , vol.1486 , pp. 1-17
    • Kerner, J.1    Hoppel, C.2
  • 26
    • 0029093341 scopus 로고
    • High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5¢-AMP-activated protein kinase inhibition of acetyl-CoA carboxylase
    • Kudo N, Barr AJ, Barr RL, Desai S, and Lopaschuk GD. High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5¢-AMP-activated protein kinase inhibition of acetyl-CoA carboxylase. J Biol Chem 270: 17513-17520, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 17513-17520
    • Kudo, N.1    Barr, A.J.2    Barr, R.L.3    Desai, S.4    Lopaschuk, G.D.5
  • 27
    • 0022507106 scopus 로고
    • A spectro-photometric assay for superoxide dismutase activities in crude tissue fractions
    • Kuthan H, Haussmann HJ, and Werringloer J. A spectro-photometric assay for superoxide dismutase activities in crude tissue fractions. Biochem J 237: 175-180, 1986.
    • (1986) Biochem J , vol.237 , pp. 175-180
    • Kuthan, H.1    Haussmann, H.J.2    Werringloer, J.3
  • 28
    • 77949813688 scopus 로고    scopus 로고
    • Inhibition of L-arginine metabolizing enzymes by L-arginine-derived advanced glycation end products
    • Lai YL, Aoyama S, Nagai R, Miyoshi N, and Ohshima H. Inhibition of L-arginine metabolizing enzymes by L-arginine-derived advanced glycation end products. J Clin Biochem Nutr 46: 177-185, 2010.
    • (2010) J Clin Biochem Nutr , vol.46 , pp. 177-185
    • Lai, Y.L.1    Aoyama, S.2    Nagai, R.3    Miyoshi, N.4    Ohshima, H.5
  • 29
    • 0037133283 scopus 로고    scopus 로고
    • Memory loss in old rats is associated with brain mitochondrial decay and RNA/DNA oxidation: Partial reversal by feeding acetyl-L-carnitine and/or R-alpha-lipoic acid
    • Liu J, Head E, Gharib AM, Yuan W, Ingersoll RT, Hagen TM, Cotman CW, and Ames BN. Memory loss in old rats is associated with brain mitochondrial decay and RNA/DNA oxidation: partial reversal by feeding acetyl-L-carnitine and/or R-alpha-lipoic acid. Proc Natl Acad Sci USA 99: 2356-2361, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2356-2361
    • Liu, J.1    Head, E.2    Gharib, A.M.3    Yuan, W.4    Ingersoll, R.T.5    Hagen, T.M.6    Cotman, C.W.7    Ames, B.N.8
  • 30
    • 0037133319 scopus 로고    scopus 로고
    • Age-associated mito-chondrial oxidative decay: Improvement of carnitine acet-yltransferase substrate-binding affinity and activity in brain by feeding old rats acetyl-L-carnitine and/or R-alpha-lipoic acid
    • Liu J, Killilea DW, and Ames BN. Age-associated mito-chondrial oxidative decay: improvement of carnitine acet-yltransferase substrate-binding affinity and activity in brain by feeding old rats acetyl-L-carnitine and/or R-alpha-lipoic acid. Proc Natl Acad Sci USA 99: 1876-1881, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1876-1881
    • Liu, J.1    Killilea, D.W.2    Ames, B.N.3
  • 31
    • 0030938190 scopus 로고    scopus 로고
    • Upregula-tion of 5¢-AMP-activated protein kinase is responsible for the increase in myocardial fatty acid oxidation rates following birth in the newborn rabbit
    • Makinde AO, Gamble J, and Lopaschuk GD. Upregula-tion of 5¢-AMP-activated protein kinase is responsible for the increase in myocardial fatty acid oxidation rates following birth in the newborn rabbit. Circ Res 80: 482-489, 1997.
    • (1997) Circ Res , vol.80 , pp. 482-489
    • Makinde, A.O.1    Gamble, J.2    Lopaschuk, G.D.3
  • 32
    • 0038651033 scopus 로고    scopus 로고
    • Alterations in TGF-b1 expression in lambs with increased pulmonary blood flow and pulmonary hypertension
    • Mata-Greenwood E, Meyrick B, Fineman JR, and Black SM. Alterations in TGF-b1 expression in lambs with increased pulmonary blood flow and pulmonary hypertension. Am J Physiol 285: L209-L221, 2003.
    • (2003) Am J Physiol , vol.285
    • Mata-Greenwood, E.1    Meyrick, B.2    Fineman, J.R.3    Black, S.M.4
  • 33
    • 77949471906 scopus 로고    scopus 로고
    • L-carnitine attenuates cardiac remodelling rather than vascular remodelling in deoxycorticosterone acetate-salt hypertensive rats
    • O'Brien D, Chunduri P, Iyer A, and Brown L. L-carnitine attenuates cardiac remodelling rather than vascular remodelling in deoxycorticosterone acetate-salt hypertensive rats. Basic Clin Pharmacol Toxicol 106: 296-301, 2010.
    • (2010) Basic Clin Pharmacol Toxicol , vol.106 , pp. 296-301
    • O'Brien, D.1    Chunduri, P.2    Iyer, A.3    Brown, L.4
  • 38
    • 0029160781 scopus 로고
    • In utero placement of aorto-pulmonary shunts: A model of postnatal pulmonary hypertension with increased pulmonary blood flow in lambs
    • Reddy VM, Meyrick B, Wong J, Khoor A, Liddicoat JR, Hanley FL, and Fineman Jr. In utero placement of aorto-pulmonary shunts: a model of postnatal pulmonary hypertension with increased pulmonary blood flow in lambs. Circulation 92: 1-8, 1995.
    • (1995) Circulation , vol.92 , pp. 1-8
    • Reddy, V.M.1    Meyrick, B.2    Wong, J.3    Khoor, A.4    Liddicoat, J.R.5    Hanley, F.L.6    Fineman, J.R.7
  • 39
    • 77951220191 scopus 로고    scopus 로고
    • A proposed mitochondrial-metabolic mechanism for initiation and maintenance of pulmonary arterial hypertension in fawn-hooded rats: The Warburg model of pulmonary arterial hypertension
    • Rehman J and Archer SL. A proposed mitochondrial-metabolic mechanism for initiation and maintenance of pulmonary arterial hypertension in fawn-hooded rats: the Warburg model of pulmonary arterial hypertension. Adv Exp Med Biol 661: 171-185.
    • Adv Exp Med Biol , vol.661 , pp. 171-185
    • Rehman, J.1    Archer, S.L.2
  • 40
    • 77956649059 scopus 로고    scopus 로고
    • Carnitine homeostasis, mitochon-drial function, and cardiovascular disease
    • Sharma S and Black SM. Carnitine homeostasis, mitochon-drial function, and cardiovascular disease. Drug Discov Today Dis Mech 6: e31-e39, 2009.
    • (2009) Drug Discov Today Dis Mech , vol.6
    • Sharma, S.1    Black, S.M.2
  • 42
    • 0032483099 scopus 로고    scopus 로고
    • Deletion of the conserved first 18 N-terminal amino acid residues in rat liver carnitine palmitoyltransferase i abolishes malonyl-CoA sensitivity and binding
    • Shi J, Zhu H, Arvidson DN, Cregg JM, and Woldegiorgis G. Deletion of the conserved first 18 N-terminal amino acid residues in rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA sensitivity and binding. Biochemistry (Mosc) 37: 11033-11038, 1998.
    • (1998) Biochemistry (Mosc) , vol.37 , pp. 11033-11038
    • Shi, J.1    Zhu, H.2    Arvidson, D.N.3    Cregg, J.M.4    Woldegiorgis, G.5
  • 43
    • 0033515467 scopus 로고    scopus 로고
    • A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitoyl-transferase i abolishes malonyl-CoA inhibition and high affinity binding
    • Shi J, Zhu H, Arvidson DN, and Woldegiorgis G. A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitoyl-transferase I abolishes malonyl-CoA inhibition and high affinity binding. J Biol Chem 274: 9421-9426, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 9421-9426
    • Shi, J.1    Zhu, H.2    Arvidson, D.N.3    Woldegiorgis, G.4
  • 45
    • 47249137061 scopus 로고    scopus 로고
    • Asymmetric dimethylarginine inhibits HSP90 activity in pulmonary arterial endothelial cells: Role of mi-tochondrial dysfunction
    • Sud N, Wells SM, Sharma S, Wiseman DA, Wilham J, and Black SM. Asymmetric dimethylarginine inhibits HSP90 activity in pulmonary arterial endothelial cells: role of mi-tochondrial dysfunction. Am J Physiol Cell Physiol 294: C1407-C1418, 2008.
    • (2008) Am J Physiol Cell Physiol , vol.294
    • Sud, N.1    Wells, S.M.2    Sharma, S.3    Wiseman, D.A.4    Wilham, J.5    Black, S.M.6
  • 48
    • 84856766992 scopus 로고    scopus 로고
    • Targeting energetic metabolism: A new frontier in the pathogenesis and treatment of pulmonary hypertension
    • Tuder RM, Davis LA, and Graham BB. Targeting energetic metabolism: a new frontier in the pathogenesis and treatment of pulmonary hypertension. Am J Respir Crit Care Med 185: 260-266.
    • Am J Respir Crit Care Med , vol.185 , pp. 260-266
    • Tuder, R.M.1    Davis, L.A.2    Graham, B.B.3
  • 49
    • 0036471216 scopus 로고    scopus 로고
    • Carnitine biosynthesis in mammals
    • Vaz FM and Wanders RJ. Carnitine biosynthesis in mammals. Biochem J 361: 417-429, 2002.
    • (2002) Biochem J , vol.361 , pp. 417-429
    • Vaz, F.M.1    Wanders, R.J.2
  • 50
    • 0032555637 scopus 로고    scopus 로고
    • Malonyl-CoA-independent acute control of hepatic carnitine palmitoyltransferase i activity. Role of Ca2 +/calmodulin-dependent protein kinase II and cytoskeletal components
    • Velasco G, Geelen MJ, Gomez del Pulgar T, and Guzman M. Malonyl-CoA-independent acute control of hepatic carnitine palmitoyltransferase I activity. Role of Ca2 +/calmodulin-dependent protein kinase II and cytoskeletal components. J Biol Chem 273: 21497-21504, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 21497-21504
    • Velasco, G.1    Geelen, M.J.2    Gomez Del Pulgar, T.3    Guzman, M.4
  • 51
    • 0345131692 scopus 로고    scopus 로고
    • Evidence that the AMP-activated protein kinase stimulates rat liver carnitine palmitoyltransferase i by phosphor-ylating cytoskeletal components
    • Velasco G, Gomez del Pulgar T, Carling D, and Guzman M. Evidence that the AMP-activated protein kinase stimulates rat liver carnitine palmitoyltransferase I by phosphor-ylating cytoskeletal components. FEBS Lett 439: 317-320, 1998.
    • (1998) FEBS Lett , vol.439 , pp. 317-320
    • Velasco, G.1    Gomez Del Pulgar, T.2    Carling, D.3    Guzman, M.4
  • 52
    • 0031033160 scopus 로고    scopus 로고
    • Involvement of Ca2+/calmodulin-dependent protein kinase II in the activation of carnitine palmitoyltransferase i by oka-daic acid in rat hepatocytes
    • Velasco G, Guzman M, Zammit VA, and Geelen MJ. Involvement of Ca2+/calmodulin-dependent protein kinase II in the activation of carnitine palmitoyltransferase I by oka-daic acid in rat hepatocytes. Biochem J 321 (Pt 1): 211-216, 1997.
    • (1997) Biochem J , vol.321 , Issue.PART 1 , pp. 211-216
    • Velasco, G.1    Guzman, M.2    Zammit, V.A.3    Geelen, M.J.4
  • 53
    • 70349235991 scopus 로고    scopus 로고
    • Mi-tochondrial targets for stroke: Focusing basic science research toward development of clinically translatable therapeutics
    • Vosler PS, Graham SH, Wechsler LR, and Chen J. Mi-tochondrial targets for stroke: focusing basic science research toward development of clinically translatable therapeutics. Stroke 40: 3149-3155, 2009.
    • (2009) Stroke , vol.40 , pp. 3149-3155
    • Vosler, P.S.1    Graham, S.H.2    Wechsler, L.R.3    Chen, J.4
  • 54
    • 24044492236 scopus 로고    scopus 로고
    • Roles of 3-phosphoinositide-dependent kinase 1 in the regulation of endothelial nitric-oxide synthase phosphorylation and function by heat shock protein 90
    • Wei Q and Xia Y. Roles of 3-phosphoinositide-dependent kinase 1 in the regulation of endothelial nitric-oxide synthase phosphorylation and function by heat shock protein 90. J Biol Chem 280: 18081-18086, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 18081-18086
    • Wei, Q.1    Xia, Y.2
  • 55
    • 0029978799 scopus 로고    scopus 로고
    • Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise
    • Winder WW and Hardie DG. Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise. Am J Physiol 270: E299-E304, 1996.
    • (1996) Am J Physiol , vol.270
    • Winder, W.W.1    Hardie, D.G.2
  • 56
    • 33846243367 scopus 로고    scopus 로고
    • Alterations in zinc homeostasis underlie endothelial cell death induced by oxidative stress from acute exposure to hydrogen peroxide
    • Wiseman DA, Wells SM, Hubbard M, Welker JE, and Black SM. Alterations in zinc homeostasis underlie endothelial cell death induced by oxidative stress from acute exposure to hydrogen peroxide. Am J Physiol Lung Cell Mol Physiol 292: L165-L177, 2007.
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.292
    • Wiseman, D.A.1    Wells, S.M.2    Hubbard, M.3    Welker, J.E.4    Black, S.M.5
  • 59
    • 33646451361 scopus 로고    scopus 로고
    • Functional relevance of Golgi-and plasma membrane-localized endothelial NO synthase in reconstituted endothelial cells
    • Zhang Q, Church JE, Jagnandan D, Catravas JD, Sessa WC, and Fulton D. Functional relevance of Golgi-and plasma membrane-localized endothelial NO synthase in reconstituted endothelial cells. Arterioscler Thromb Vasc Biol 26: 1015-1021, 2006.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 1015-1021
    • Zhang, Q.1    Church, J.E.2    Jagnandan, D.3    Catravas, J.D.4    Sessa, W.C.5    Fulton, D.6


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