메뉴 건너뛰기




Volumn 280, Issue 15, 2013, Pages 3621-3631

Differences in oxygen-dependent nitric oxide metabolism by cytoglobin and myoglobin account for their differing functional roles

Author keywords

cytoglobin; metabolism kinetics; myoglobin; nitric oxide; oxygen

Indexed keywords

ASCORBIC ACID; CYTOGLOBIN; MOLYBDENUM; MYOGLOBIN; NITRIC OXIDE; SUPEROXIDE DISMUTASE;

EID: 84880332674     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12352     Document Type: Article
Times cited : (51)

References (40)
  • 1
    • 67649763457 scopus 로고    scopus 로고
    • Cytoglobin is expressed in the vasculature and regulates cell respiration and proliferation via nitric oxide dioxygenation
    • Halligan KE, Jourd'heuil FL, &, Jourd'heuil D, (2009) Cytoglobin is expressed in the vasculature and regulates cell respiration and proliferation via nitric oxide dioxygenation. J Biol Chem 284, 8539-8547.
    • (2009) J Biol Chem , vol.284 , pp. 8539-8547
    • Halligan, K.E.1    Jourd'Heuil, F.L.2    Jourd'Heuil, D.3
  • 3
    • 0025277646 scopus 로고
    • Control of coronary vascular tone by nitric oxide
    • Kelm M, &, Schrader J, (1990) Control of coronary vascular tone by nitric oxide. Circ Res 66, 1561-1575.
    • (1990) Circ Res , vol.66 , pp. 1561-1575
    • Kelm, M.1    Schrader, J.2
  • 4
    • 0023928184 scopus 로고
    • Endothelium-derived relaxing factor. Identification as nitric oxide and role in the control of vascular tone and platelet function
    • Moncada S, Radomski MW, &, Palmer RM, (1988) Endothelium-derived relaxing factor. Identification as nitric oxide and role in the control of vascular tone and platelet function. Biochem Pharmacol 37, 2495-2501.
    • (1988) Biochem Pharmacol , vol.37 , pp. 2495-2501
    • Moncada, S.1    Radomski, M.W.2    Palmer, R.M.3
  • 7
    • 44349180793 scopus 로고    scopus 로고
    • NO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivo
    • Smagghe BJ, Trent JT 3rd, &, Hargrove MS, (2008) NO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivo. PLoS ONE 3, e2039.
    • (2008) PLoS ONE , vol.3
    • Smagghe, B.J.1    Trent III, J.T.2    Hargrove, M.S.3
  • 8
    • 77954894512 scopus 로고    scopus 로고
    • Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes
    • Gardner AM, Cook MR, &, Gardner PR, (2010) Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes. J Biol Chem 285, 23850-23857.
    • (2010) J Biol Chem , vol.285 , pp. 23850-23857
    • Gardner, A.M.1    Cook, M.R.2    Gardner, P.R.3
  • 9
    • 84862845350 scopus 로고    scopus 로고
    • Characterization of the function of cytoglobin as an oxygen-dependent regulator of nitric oxide concentration
    • Liu X, Follmer D, Zweier JR, Huang X, Hemann C, Liu K, Druhan LJ, &, Zweier JL, (2012) Characterization of the function of cytoglobin as an oxygen-dependent regulator of nitric oxide concentration. Biochemistry 51, 5072-5082.
    • (2012) Biochemistry , vol.51 , pp. 5072-5082
    • Liu, X.1    Follmer, D.2    Zweier, J.R.3    Huang, X.4    Hemann, C.5    Liu, K.6    Druhan, L.J.7    Zweier, J.L.8
  • 11
    • 0035916922 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies of the NO-mediated oxidation of oxymyoglobin and oxyhemoglobin
    • Herold S, Exner M, &, Nauser T, (2001) Kinetic and mechanistic studies of the NO-mediated oxidation of oxymyoglobin and oxyhemoglobin. Biochemistry 40, 3385-3395.
    • (2001) Biochemistry , vol.40 , pp. 3385-3395
    • Herold, S.1    Exner, M.2    Nauser, T.3
  • 12
    • 0029893918 scopus 로고    scopus 로고
    • A brief history of hemoglobins: Plant, animal, protist, and bacteria
    • Hardison RC, (1996) A brief history of hemoglobins: plant, animal, protist, and bacteria. Proc Natl Acad Sci USA 93, 5675-5679.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5675-5679
    • Hardison, R.C.1
  • 14
  • 20
    • 20444500960 scopus 로고    scopus 로고
    • Oxygen supply and nitric oxide scavenging by myoglobin contribute to exercise endurance and cardiac function
    • Merx MW, Godecke A, Flogel U, &, Schrader J, (2005) Oxygen supply and nitric oxide scavenging by myoglobin contribute to exercise endurance and cardiac function. FASEB J 19, 1015-1017.
    • (2005) FASEB J , vol.19 , pp. 1015-1017
    • Merx, M.W.1    Godecke, A.2    Flogel, U.3    Schrader, J.4
  • 21
    • 34247899197 scopus 로고    scopus 로고
    • Estimation of nitric oxide concentration in blood for different rates of generation. Evidence that intravascular nitric oxide levels are too low to exert physiological effects
    • Liu X, Yan Q, Baskerville KL, &, Zweier JL, (2007) Estimation of nitric oxide concentration in blood for different rates of generation. Evidence that intravascular nitric oxide levels are too low to exert physiological effects. J Biol Chem 282, 8831-8836.
    • (2007) J Biol Chem , vol.282 , pp. 8831-8836
    • Liu, X.1    Yan, Q.2    Baskerville, K.L.3    Zweier, J.L.4
  • 23
    • 17144420129 scopus 로고    scopus 로고
    • Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins
    • Fago A, Hundahl C, Malte H, &, Weber RE, (2004) Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins. IUBMB Life 56, 689-696.
    • (2004) IUBMB Life , vol.56 , pp. 689-696
    • Fago, A.1    Hundahl, C.2    Malte, H.3    Weber, R.E.4
  • 24
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T, Ebner B, Weich B, &, Hankeln T, (2002) Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol Biol Evol 19, 416-421.
    • (2002) Mol Biol Evol , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 25
    • 0003650072 scopus 로고    scopus 로고
    • 6th edn. Woodhead Publishing, Cambridge, UK
    • Lawrie RA, (1998) Lawrie's Meat Science, 6th edn. Woodhead Publishing, Cambridge, UK.
    • (1998) Lawrie's Meat Science
    • Lawrie, R.A.1
  • 26
    • 0001279637 scopus 로고
    • Kinetics of reduction of metmyoglobins by ascorbate. Effect of the modification of the heme distal side, heme propionates, and 2,4-substituents of deuterohemin
    • Tsukahara K, Okazawa T, Takahashi H, &, Yamamoto Y, (1986) Kinetics of reduction of metmyoglobins by ascorbate. Effect of the modification of the heme distal side, heme propionates, and 2,4-substituents of deuterohemin. Inorg Chem 25, 4756-4760.
    • (1986) Inorg Chem , vol.25 , pp. 4756-4760
    • Tsukahara, K.1    Okazawa, T.2    Takahashi, H.3    Yamamoto, Y.4
  • 27
    • 0005837780 scopus 로고
    • Oxidation of oxymyoglobin by nitric oxide through dissociation from cobalt nitrosyls
    • Doyle MP, Pickering RA, &, Cook BR, (1983) Oxidation of oxymyoglobin by nitric oxide through dissociation from cobalt nitrosyls. J Inorg Biochem 19, 329-338.
    • (1983) J Inorg Biochem , vol.19 , pp. 329-338
    • Doyle, M.P.1    Pickering, R.A.2    Cook, B.R.3
  • 28
    • 0019726454 scopus 로고
    • Oxidation of nitrogen oxides by bound dioxygen in hemoproteins
    • Doyle MP, &, Hoekstra JW, (1981) Oxidation of nitrogen oxides by bound dioxygen in hemoproteins. J Inorg Biochem 14, 351-358.
    • (1981) J Inorg Biochem , vol.14 , pp. 351-358
    • Doyle, M.P.1    Hoekstra, J.W.2
  • 30
    • 68149169007 scopus 로고    scopus 로고
    • What is the real physiological NO concentration in vivo?
    • Hall CN, &, Garthwaite J, (2009) What is the real physiological NO concentration in vivo? Nitric Oxide 21, 92-103.
    • (2009) Nitric Oxide , vol.21 , pp. 92-103
    • Hall, C.N.1    Garthwaite, J.2
  • 32
    • 67650077095 scopus 로고    scopus 로고
    • Transfer of ascorbic acid across the vascular endothelium: Mechanism and self-regulation
    • May JM, Qu ZC, &, Qiao H, (2009) Transfer of ascorbic acid across the vascular endothelium: mechanism and self-regulation. Am J Physiol 297, C169-C178.
    • (2009) Am J Physiol , vol.297
    • May, J.M.1    Qu, Z.C.2    Qiao, H.3
  • 33
    • 15444364954 scopus 로고    scopus 로고
    • Effect of acute hypoxia on microcirculatory and tissue oxygen levels in rat cremaster muscle
    • Johnson PC, Vandegriff K, Tsai AG, &, Intaglietta M, (2005) Effect of acute hypoxia on microcirculatory and tissue oxygen levels in rat cremaster muscle. J Appl Physiol 98, 1177-1184.
    • (2005) J Appl Physiol , vol.98 , pp. 1177-1184
    • Johnson, P.C.1    Vandegriff, K.2    Tsai, A.G.3    Intaglietta, M.4
  • 36
    • 4644261106 scopus 로고    scopus 로고
    • Bis-histidyl hexacoordination in hemoglobins facilitates heme reduction kinetics
    • Weiland TR, Kundu S, Trent JT 3rd, Hoy JA, &, Hargrove MS, (2004) Bis-histidyl hexacoordination in hemoglobins facilitates heme reduction kinetics. J Am Chem Soc 126, 11930-11935.
    • (2004) J Am Chem Soc , vol.126 , pp. 11930-11935
    • Weiland, T.R.1    Kundu, S.2    Trent III, J.T.3    Hoy, J.A.4    Hargrove, M.S.5
  • 37
    • 77958153190 scopus 로고    scopus 로고
    • Application of carbon fiber composite minielectrodes for measurement of kinetic constants of nitric oxide decay in solution
    • Liu X, El-Sherbiny GA, Collard E, Huang X, Follmer D, El-Mahdy M, &, Zweier JL, (2010) Application of carbon fiber composite minielectrodes for measurement of kinetic constants of nitric oxide decay in solution. Nitric Oxide 23, 311-318.
    • (2010) Nitric Oxide , vol.23 , pp. 311-318
    • Liu, X.1    El-Sherbiny, G.A.2    Collard, E.3    Huang, X.4    Follmer, D.5    El-Mahdy, M.6    Zweier, J.L.7
  • 39
    • 0030056291 scopus 로고    scopus 로고
    • Aplysia limacina myoglobin cDNA cloning: An alternative mechanism of oxygen stabilization as studied by active-site mutagenesis
    • Cutruzzola F, Travaglini Allocatelli C, Brancaccio A, &, Brunori M, (1996) Aplysia limacina myoglobin cDNA cloning: an alternative mechanism of oxygen stabilization as studied by active-site mutagenesis. Biochem J 314, 83-90.
    • (1996) Biochem J , vol.314 , pp. 83-90
    • Cutruzzola, F.1    Travaglini Allocatelli, C.2    Brancaccio, A.3    Brunori, M.4
  • 40
    • 0023042546 scopus 로고
    • A kinetic description of ligand binding to sperm whale myoglobin
    • Gibson QH, Olson JS, McKinnie RE, &, Rohlfs RJ, (1986) A kinetic description of ligand binding to sperm whale myoglobin. J Biol Chem 261, 10228-10239.
    • (1986) J Biol Chem , vol.261 , pp. 10228-10239
    • Gibson, Q.H.1    Olson, J.S.2    McKinnie, R.E.3    Rohlfs, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.