메뉴 건너뛰기




Volumn 302, Issue 6, 2012, Pages 693-701

Functional differentiation of myoglobin isoforms in hypoxia-tolerant carp indicates tissue-specific protective roles

Author keywords

Fish; Hydrogen peroxide; Nitric oxide; Nitrite reductase; Oxygen binding

Indexed keywords

CARBON MONOXIDE; HYDROGEN PEROXIDE; MYOGLOBIN; NITRIC OXIDE; NITRITE REDUCTASE; PEROXIDASE; PROTEIN MYOGLOBIN 1; PROTEIN MYOGLOBIN 2; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84863230557     PISSN: 03636119     EISSN: 15221490     Source Type: Journal    
DOI: 10.1152/ajpregu.00501.2011     Document Type: Article
Times cited : (55)

References (51)
  • 1
    • 0001459583 scopus 로고
    • Hemoglobin and myoglobin in their reactionswith ligands
    • edited by Neuberger, A and Tatum,EL. Amsterdam, Holland: North-Holland Publishing
    • Antonini E, Brunori M. Hemoglobin and myoglobin in their reactionswith ligands. In: Frontiers in Biology, edited by Neuberger, A and Tatum,EL. Amsterdam, Holland: North-Holland Publishing, 1971.
    • (1971) Frontiers in Biology
    • Antonini, E.1    Brunori, M.2
  • 2
    • 33947418921 scopus 로고    scopus 로고
    • Hypoxia tolerance in reptiles, amphibians, and fishes: Life with variable oxygen availability
    • Bickler PE, Buck LT. Hypoxia tolerance in reptiles, amphibians, and fishes: life with variable oxygen availability. Annu Rev Physiol 69: 145-170, 2007.
    • (2007) Annu Rev Physiol , vol.69 , pp. 145-170
    • Bickler, P.E.1    Buck, L.T.2
  • 4
    • 0030819158 scopus 로고    scopus 로고
    • Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures
    • Cashon RE, Vayda ME, Sidell BD. Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures. Comp Biochem Physiol B Biochem Mol Biol 117: 613-620, 1997.
    • (1997) Comp Biochem Physiol B Biochem Mol Biol , vol.117 , pp. 613-620
    • Cashon, R.E.1    Vayda, M.E.2    Sidell, B.D.3
  • 5
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 59: 527-605, 1979.
    • (1979) Physiol Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 6
    • 62849105365 scopus 로고    scopus 로고
    • Diverse cell-specific expression of myoglobin isoforms in brain, kidney, gill and liver of the hypoxia-tolerant carp and zebrafish
    • Cossins AR, Williams DR, Foulkes NS, Berenbrink M, Kipar A. Diverse cell-specific expression of myoglobin isoforms in brain, kidney, gill and liver of the hypoxia-tolerant carp and zebrafish. J Exp Biol 212: 627-638, 2009.
    • (2009) J Exp Biol , vol.212 , pp. 627-638
    • Cossins, A.R.1    Williams, D.R.2    Foulkes, N.S.3    Berenbrink, M.4    Kipar, A.5
  • 7
    • 0042836783 scopus 로고    scopus 로고
    • Recent duplication of the common carp (Cyprinus carpio L.) genome as revealed by analyses of microsatellite loci
    • David L, Blum S, Feldman MW, Lavi U, Hillel J. Recent duplication of the common carp (Cyprinus carpio L.) genome as revealed by analyses of microsatellite loci. Mol Biol Evol 20: 1425-1434, 2003.
    • (2003) Mol Biol Evol , vol.20 , pp. 1425-1434
    • David, L.1    Blum, S.2    Feldman, M.W.3    Lavi, U.4    Hillel, J.5
  • 9
  • 11
    • 48849107315 scopus 로고    scopus 로고
    • A role for neuroglobin: Resetting the trigger level for apoptosis in neuronal and retinal cells
    • Fago A, Mathews AJ, Brittain T. A role for neuroglobin: Resetting the trigger level for apoptosis in neuronal and retinal cells. IUBMB Life 60: 398-401, 2008.
    • (2008) IUBMB Life , vol.60 , pp. 398-401
    • Fago, A.1    Mathews, A.J.2    Brittain, T.3
  • 12
    • 8844260650 scopus 로고    scopus 로고
    • Role of myoglobin in the antioxidant defense of the heart
    • Flogel U, Godecke A, Klotz LO, Schrader J. Role of myoglobin in the antioxidant defense of the heart. FASEB J 18: 1156-1158, 2004.
    • (2004) FASEB J , vol.18 , pp. 1156-1158
    • Flogel, U.1    Godecke, A.2    Klotz, L.O.3    Schrader, J.4
  • 15
  • 16
    • 0014060675 scopus 로고
    • Determination of sulfhydryl groups with 2,2′- Or 4,4′-dithiodipyridine
    • Grasset DR, Murray JF. Determination of sulfhydryl groups with 2,2′- Or 4,4′-dithiodipyridine. Arch Biochem Biophys 119: 41-49, 1967.
    • (1967) Arch Biochem Biophys , vol.119 , pp. 41-49
    • Grasset, D.R.1    Murray, J.F.2
  • 17
    • 77955650019 scopus 로고    scopus 로고
    • Myoglobin's old and new clothes: From molecular structure to function in living cells
    • Gros G, Wittenberg BA, Jue T. Myoglobin's old and new clothes: from molecular structure to function in living cells. J Exp Biol 213: 2713-2725, 2010.
    • (2010) J Exp Biol , vol.213 , pp. 2713-2725
    • Gros, G.1    Wittenberg, B.A.2    Jue, T.3
  • 18
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biol 59: 307-321, 2010.
    • (2010) Syst Biol , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 19
    • 84863235509 scopus 로고
    • Metmyoglobin reductase - Identification of reduced nicotinamide adenine-dinucleotide (NADH) dependent enzyme-activity from bovine heart which reduces metmyoglobin
    • Hagler L, Coppes RI, Herman RH. Metmyoglobin reductase - Identification of reduced nicotinamide adenine-dinucleotide (NADH) dependent enzyme-activity from bovine heart which reduces metmyoglobin. Fed Proc 35: 1423, 1976.
    • (1976) Fed Proc , vol.35 , pp. 1423
    • Hagler, L.1    Coppes, R.I.2    Herman, R.H.3
  • 21
    • 78650640417 scopus 로고    scopus 로고
    • 2 affinity myoglobin from rainbow trout
    • Helbo S, Fago A. Allosteric modulation by S-nitrosation in the low-O2 affinity myoglobin from rainbow trout. Am J Physiol Regul Integr Comp Physiol 300: R101-R108, 2011.
    • (2011) Am J Physiol Regul Integr Comp Physiol , vol.300
    • Helbo, S.1    Fago, A.2
  • 22
    • 2542447171 scopus 로고    scopus 로고
    • Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress
    • Herold S, Fago A, Weber RE, Dewilde S, Moens L. Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress. J Biol Chem 279: 22841-22847, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 22841-22847
    • Herold, S.1    Fago, A.2    Weber, R.E.3    Dewilde, S.4    Moens, L.5
  • 23
    • 0037371492 scopus 로고    scopus 로고
    • Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin
    • Herold S, Rehmann FJK. Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin. Free Radic Biol Med 34: 531-545, 2003.
    • (2003) Free Radic Biol Med , vol.34 , pp. 531-545
    • Herold, S.1    Rehmann, F.J.K.2
  • 27
    • 0016642727 scopus 로고
    • Functional properties of hemoglobins in teleost tilapia-grahami
    • Lykkeboe G, Johansen K, Maloiy GMO. Functional properties of hemoglobins in teleost tilapia-grahami. J Comp Physiol A 104: 1-11, 1975.
    • (1975) J Comp Physiol A , vol.104 , pp. 1-11
    • Lykkeboe, G.1    Johansen, K.2    Maloiy, G.M.O.3
  • 28
    • 1842474583 scopus 로고    scopus 로고
    • Structural and kinetic characterization of myoglobins from eurythermal and stenothermal fish species
    • Madden PW, Babcock MJ, Vayda ME, Cashon RE. Structural and kinetic characterization of myoglobins from eurythermal and stenothermal fish species. Comp Biochem Physiol B Biochem Mol Biol 137: 341-350, 2004.
    • (2004) Comp Biochem Physiol B Biochem Mol Biol , vol.137 , pp. 341-350
    • Madden, P.W.1    Babcock, M.J.2    Vayda, M.E.3    Cashon, R.E.4
  • 30
    • 4644324293 scopus 로고    scopus 로고
    • Hypoxic survival strategies in two fishes: Extreme anoxia tolerance in the North European crucian carp and natural hypoxic preconditioning in a coral-reef shark
    • Nilsson GE, Renshaw GMC. Hypoxic survival strategies in two fishes: extreme anoxia tolerance in the North European crucian carp and natural hypoxic preconditioning in a coral-reef shark. J Exp Biol 207: 3131-3139, 2004.
    • (2004) J Exp Biol , vol.207 , pp. 3131-3139
    • Nilsson, G.E.1    Renshaw, G.M.C.2
  • 31
    • 80053629048 scopus 로고    scopus 로고
    • Molecular and structural antioxidant defenses against oxidative stress in animals
    • Pamplona R, Costantini D. Molecular and structural antioxidant defenses against oxidative stress in animals. Am J Physiol Regul Integr Comp Physiol 301: R843-R863, 2011.
    • (2011) Am J Physiol Regul Integr Comp Physiol , vol.301
    • Pamplona, R.1    Costantini, D.2
  • 32
    • 77955597015 scopus 로고    scopus 로고
    • Roles of nitric oxide, nitrite and myoglobin on myocardial efficiency in trout (Oncorhynchus mykiss) and goldfish (Carassius auratus): Implications for hypoxia tolerance
    • Pedersen CL, Faggiano S, Helbo S, Gesser H, Fago A. Roles of nitric oxide, nitrite and myoglobin on myocardial efficiency in trout (Oncorhynchus mykiss) and goldfish (Carassius auratus): implications for hypoxia tolerance. J Exp Biol 213: 2755-2762, 2010.
    • (2010) J Exp Biol , vol.213 , pp. 2755-2762
    • Pedersen, C.L.1    Faggiano, S.2    Helbo, S.3    Gesser, H.4    Fago, A.5
  • 33
    • 15444365918 scopus 로고    scopus 로고
    • Human S-nitroso oxymyoglobin is a store of vasoactive nitric oxide
    • Rayner BS, Wu BJ, Raftery M, Stocker R, Witting PK. Human S-nitroso oxymyoglobin is a store of vasoactive nitric oxide. J Biol Chem 280: 9985-9993, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 9985-9993
    • Rayner, B.S.1    Wu, B.J.2    Raftery, M.3    Stocker, R.4    Witting, P.K.5
  • 34
    • 77955880548 scopus 로고    scopus 로고
    • The redox activity of hemoglobins: From physiologic functions to pathologic mechanisms
    • Reeder BJ. The redox activity of hemoglobins: from physiologic functions to pathologic mechanisms. Antioxid Redox Signal 13: 1087-1123, 2010.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1087-1123
    • Reeder, B.J.1
  • 35
    • 50549094066 scopus 로고    scopus 로고
    • Globins and hypoxia adaptation in the goldfish, Carassius auratus
    • Roesner A, Mitz SA, Hankeln T, Burmester T. Globins and hypoxia adaptation in the goldfish, Carassius auratus. FEBS J 275: 3633-3643, 2008.
    • (2008) FEBS J , vol.275 , pp. 3633-3643
    • Roesner, A.1    Mitz, S.A.2    Hankeln, T.3    Burmester, T.4
  • 36
    • 44449098314 scopus 로고    scopus 로고
    • Kinetics of reaction of nitrite with deoxy hemoglobin after rapid deoxygenation or predeoxygenation by dithionite measured in solution and bound to the cytoplasmic domain of band 3 (SLC4A1)
    • Salhany JM. Kinetics of reaction of nitrite with deoxy hemoglobin after rapid deoxygenation or predeoxygenation by dithionite measured in solution and bound to the cytoplasmic domain of band 3 (SLC4A1). Biochemistry 47: 6059-6072, 2008.
    • (2008) Biochemistry , vol.47 , pp. 6059-6072
    • Salhany, J.M.1
  • 38
    • 37049066149 scopus 로고
    • A scheme for the colorimetric determination of microgram amounts of thiols
    • Saville B. A scheme for the colorimetric determination of microgram amounts of thiols. Analyst 83: 670-672, 1958.
    • (1958) Analyst , vol.83 , pp. 670-672
    • Saville, B.1
  • 41
    • 0014630980 scopus 로고
    • 2-binding curves of hemoproteins by means of a diffusion chamber
    • Sick H, Gersonde K. Method for continuous registration of O2-binding curves of hemoproteins by means of a diffusion chamber. Anal Biochem 32: 362-376, 1969.
    • (1969) Anal Biochem , vol.32 , pp. 362-376
    • Sick, H.1    Gersonde, K.2
  • 42
    • 9644280260 scopus 로고    scopus 로고
    • Measurement of nitric oxide production in biological systems by using Griess reaction assay
    • Sun J, Zhang XJ, Broderick M, Fein H. Measurement of nitric oxide production in biological systems by using Griess reaction assay. Sensors 3: 276-284, 2003.
    • (2003) Sensors , vol.3 , pp. 276-284
    • Sun, J.1    Zhang, X.J.2    Broderick, M.3    Fein, H.4
  • 43
    • 0035909992 scopus 로고    scopus 로고
    • Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury
    • Sun YJ, Jin KL, Mao XO, Zhu YH, Greenberg DA. Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury. Proc Natl Acad Sci USA 98: 15306-15311, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15306-15311
    • Sun, Y.J.1    Jin, K.L.2    Mao, X.O.3    Zhu, Y.H.4    Greenberg, D.A.5
  • 44
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S. MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24: 1596-1599, 2007.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 46
    • 34250282108 scopus 로고
    • 2 on hemoglobin-oxygen affinity
    • Weber RE, Lykkeboe G. Respiratory adaptations in carp blood influences of hypoxia, red-cell organic-phosphates, divalent-cations and CO2 on hemoglobin-oxygen affinity. J Comp Physiol 128: 127-137, 1978.
    • (1978) J Comp Physiol , vol.128 , pp. 127-137
    • Weber, R.E.1    Lykkeboe, G.2
  • 47
    • 0023624230 scopus 로고
    • The interaction of oxymyoglobin with hydrogen-peroxide - The formation of ferrylmyoglobin at moderate excesses of hydrogenperoxide
    • Whitburn KD. The interaction of oxymyoglobin with hydrogen-peroxide - The formation of ferrylmyoglobin at moderate excesses of hydrogenperoxide. Arch Biochem Biophys 253: 419-430, 1987.
    • (1987) Arch Biochem Biophys , vol.253 , pp. 419-430
    • Whitburn, K.D.1
  • 48
    • 0022252821 scopus 로고
    • The synproportionation reaction between the oxy and ferryl derivatives of myoglobin
    • Whitburn KD. The synproportionation reaction between the oxy and ferryl derivatives of myoglobin. J Inorg Biochem 24: 35-46, 1985.
    • (1985) J Inorg Biochem , vol.24 , pp. 35-46
    • Whitburn, K.D.1
  • 49
  • 50
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin - A 2ndlook
    • Wyman J. Linked functions and reciprocal effects in hemoglobin - A 2ndlook. Adv Protein Chem 19: 223-286, 1964.
    • (1964) Adv Protein Chem , vol.19 , pp. 223-286
    • Wyman, J.1
  • 51
    • 0023661090 scopus 로고
    • Oxidation of oxymyoglobin to metmyoglobin with hydrogen-peroxide - Involvement of ferryl intermediate
    • Yusa K, Shikama K. Oxidation of oxymyoglobin to metmyoglobin with hydrogen-peroxide - Involvement of ferryl intermediate. Biochemistry 26: 6684-6688, 1987.
    • (1987) Biochemistry , vol.26 , pp. 6684-6688
    • Yusa, K.1    Shikama, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.