메뉴 건너뛰기




Volumn 1784, Issue 10, 2008, Pages 1415-1420

Peroxidase activity of hemoglobin towards ascorbate and urate: A synergistic protective strategy against toxicity of Hemoglobin-Based Oxygen Carriers (HBOC)

Author keywords

Ascorbate; Blood substitute; Ferryl; Hemoglobin; Peroxidase; Urate

Indexed keywords

ASCORBIC ACID; BLOOD SUBSTITUTE; HEMOGLOBIN; HEMOGLOBIN BASED OXYGEN CARRIER; HYDROGEN PEROXIDE; IRON DERIVATIVE; PEROXIDASE; POLYMERIZED HEMOGLOBIN; UNCLASSIFIED DRUG; URATE;

EID: 52049095278     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.03.019     Document Type: Article
Times cited : (71)

References (34)
  • 1
    • 7244243910 scopus 로고    scopus 로고
    • The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology
    • Reeder B.J., Svistunenko D.A., Cooper C.E., and Wilson M.T. The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology. Antioxid. Redox Signal. 6 (2004) 954-966
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 954-966
    • Reeder, B.J.1    Svistunenko, D.A.2    Cooper, C.E.3    Wilson, M.T.4
  • 2
    • 34249778388 scopus 로고    scopus 로고
    • Total antioxidant capacity: appraisal of a concept
    • Sies H. Total antioxidant capacity: appraisal of a concept. J. Nutr. 137 (2007) 1493-1495
    • (2007) J. Nutr. , vol.137 , pp. 1493-1495
    • Sies, H.1
  • 4
    • 1242353138 scopus 로고    scopus 로고
    • Oxygen therapeutics: can we tame haemoglobin?
    • Alayash A.I. Oxygen therapeutics: can we tame haemoglobin?. Nat. Rev. Drug. Disc. 3 (2004) 152-159
    • (2004) Nat. Rev. Drug. Disc. , vol.3 , pp. 152-159
    • Alayash, A.I.1
  • 5
    • 0015722945 scopus 로고
    • Evolution and the biosynthesis of ascorbic acid
    • Chatterjee I.B. Evolution and the biosynthesis of ascorbic acid. Science (New York, N.Y 182 (1973) 1271-1272
    • (1973) Science (New York, N.Y 182 , pp. 1271-1272
    • Chatterjee, I.B.1
  • 7
    • 33845979527 scopus 로고    scopus 로고
    • Human erythrocyte membranes contain a cytochrome b561 that may be involved in extracellular ascorbate recycling
    • Su D., May J.M., Koury M.J., and Asard H. Human erythrocyte membranes contain a cytochrome b561 that may be involved in extracellular ascorbate recycling. J. Biol. Chem. 281 (2006) 39852-39859
    • (2006) J. Biol. Chem. , vol.281 , pp. 39852-39859
    • Su, D.1    May, J.M.2    Koury, M.J.3    Asard, H.4
  • 8
    • 27744494382 scopus 로고    scopus 로고
    • On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide
    • Cooper C.E., Jurd M., Nicholls P., Wankasi M.M., Svistunenko D.A., Reeder B.J., and Wilson M.T. On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide. Dalton Trans. (2005) 3483-3488
    • (2005) Dalton Trans. , pp. 3483-3488
    • Cooper, C.E.1    Jurd, M.2    Nicholls, P.3    Wankasi, M.M.4    Svistunenko, D.A.5    Reeder, B.J.6    Wilson, M.T.7
  • 10
    • 0031028512 scopus 로고    scopus 로고
    • On the molecular mechanism of metmyoglobin-catalyzed reduction of hydrogen peroxide by ascorbate
    • Galaris D., and Korantzopoulos P. On the molecular mechanism of metmyoglobin-catalyzed reduction of hydrogen peroxide by ascorbate. Free Radic. Biol. Med. 22 (1997) 657-667
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 657-667
    • Galaris, D.1    Korantzopoulos, P.2
  • 12
    • 0015352861 scopus 로고
    • Human erythrocyte catalase: an improved method of isolation and a reevaluation of reported properties
    • Bonaventura J., Schroeder W.A., and Fang S. Human erythrocyte catalase: an improved method of isolation and a reevaluation of reported properties. Arch. Biochem. Biophys. 150 (1972) 606-617
    • (1972) Arch. Biochem. Biophys. , vol.150 , pp. 606-617
    • Bonaventura, J.1    Schroeder, W.A.2    Fang, S.3
  • 13
    • 0002154654 scopus 로고
    • Everse J., Everse K.E., and Grisham M.B. (Eds), CRC Press, Boca Raton
    • Dunford H.B. In: Everse J., Everse K.E., and Grisham M.B. (Eds). Peroxidases in Chemistry and Biology, vol. 2 (1991), CRC Press, Boca Raton 1-137
    • (1991) Peroxidases in Chemistry and Biology, vol. 2 , pp. 1-137
    • Dunford, H.B.1
  • 16
    • 1342283038 scopus 로고    scopus 로고
    • Differential effects of sodium selenite in reducing tissue damage caused by three hemoglobin-based oxygen carriers
    • Baldwin A.L., Wiley E.B., and Alayash A.I. Differential effects of sodium selenite in reducing tissue damage caused by three hemoglobin-based oxygen carriers. J. Appl. Physiol. 96 (2004) 893-903
    • (2004) J. Appl. Physiol. , vol.96 , pp. 893-903
    • Baldwin, A.L.1    Wiley, E.B.2    Alayash, A.I.3
  • 17
    • 0029131674 scopus 로고
    • Limitations of the efficacy of hemoglobin-based oxygen-carrying solutions
    • Lee R., Neya K., Svizzero T.A., and Vlahakes G.J. Limitations of the efficacy of hemoglobin-based oxygen-carrying solutions. J. Appl. Physiol. 79 (1995) 236-242
    • (1995) J. Appl. Physiol. , vol.79 , pp. 236-242
    • Lee, R.1    Neya, K.2    Svizzero, T.A.3    Vlahakes, G.J.4
  • 20
    • 0027482489 scopus 로고
    • The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects
    • Giulivi C., and Cadenas E. The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects. FEBS Lett. 332 (1993) 287-290
    • (1993) FEBS Lett. , vol.332 , pp. 287-290
    • Giulivi, C.1    Cadenas, E.2
  • 21
    • 0042474177 scopus 로고    scopus 로고
    • Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase?
    • Raven E.L. Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase?. Nat. Prod. Rep. 20 (2003) 367-381
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 367-381
    • Raven, E.L.1
  • 22
    • 0037137219 scopus 로고    scopus 로고
    • Substrate binding and catalytic mechanism in ascorbate peroxidase: evidence for two ascorbate binding sites
    • Lad L., Mewies M., and Raven E.L. Substrate binding and catalytic mechanism in ascorbate peroxidase: evidence for two ascorbate binding sites. Biochemistry 41 (2002) 13774-13781
    • (2002) Biochemistry , vol.41 , pp. 13774-13781
    • Lad, L.1    Mewies, M.2    Raven, E.L.3
  • 24
    • 0029887294 scopus 로고    scopus 로고
    • Hemoglobin affects lipid peroxidation and prostaglandin E2 formation in rat corticocerebral tissues in vitro
    • Ciuffi M., Tarlini L., Mugnai S., Franchi-Micheli S., and Zilletti L. Hemoglobin affects lipid peroxidation and prostaglandin E2 formation in rat corticocerebral tissues in vitro. Biochem. Pharmacol. 52 (1996) 97-103
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 97-103
    • Ciuffi, M.1    Tarlini, L.2    Mugnai, S.3    Franchi-Micheli, S.4    Zilletti, L.5
  • 25
    • 0025201423 scopus 로고
    • A novel antioxidant role for hemoglobin. The comproportionation of ferrylhemoglobin with oxyhemoglobin
    • Giulivi C., and Davies K.J. A novel antioxidant role for hemoglobin. The comproportionation of ferrylhemoglobin with oxyhemoglobin. J. Biol. Chem. 265 (1990) 19453-19460
    • (1990) J. Biol. Chem. , vol.265 , pp. 19453-19460
    • Giulivi, C.1    Davies, K.J.2
  • 26
    • 33750546863 scopus 로고    scopus 로고
    • Oxidation and haem loss kinetics of poly(ethylene glycol)-conjugated haemoglobin (MP4): dissociation between in vitro and in vivo oxidation rates
    • Vandegriff K.D., Malavalli A., Minn C., Jiang E., Lohman J., Young M.A., Samaja M., and Winslow R.M. Oxidation and haem loss kinetics of poly(ethylene glycol)-conjugated haemoglobin (MP4): dissociation between in vitro and in vivo oxidation rates. Biochem. J. 399 (2006) 463-471
    • (2006) Biochem. J. , vol.399 , pp. 463-471
    • Vandegriff, K.D.1    Malavalli, A.2    Minn, C.3    Jiang, E.4    Lohman, J.5    Young, M.A.6    Samaja, M.7    Winslow, R.M.8
  • 27
    • 0037054809 scopus 로고    scopus 로고
    • Myoglobin as a model system for designing heme protein based blood substitutes
    • Dou Y., Maillett D.H., Eich R.F., and Olson J.S. Myoglobin as a model system for designing heme protein based blood substitutes. Biophys. Chemist. 98 (2002) 127-148
    • (2002) Biophys. Chemist. , vol.98 , pp. 127-148
    • Dou, Y.1    Maillett, D.H.2    Eich, R.F.3    Olson, J.S.4
  • 29
    • 0033593463 scopus 로고    scopus 로고
    • Reactions of sperm whale myoglobin with hydrogen peroxide. Effects of distal pocket mutations on the formation and stability of the ferryl intermediate
    • Alayash A.I., Ryan B.A., Eich R.F., Olson J.S., and Cashon R.E. Reactions of sperm whale myoglobin with hydrogen peroxide. Effects of distal pocket mutations on the formation and stability of the ferryl intermediate. J. Biol. Chem. 274 (1999) 2029-2037
    • (1999) J. Biol. Chem. , vol.274 , pp. 2029-2037
    • Alayash, A.I.1    Ryan, B.A.2    Eich, R.F.3    Olson, J.S.4    Cashon, R.E.5
  • 30
    • 84882504096 scopus 로고    scopus 로고
    • Designing recombinant hemoglobin for use as a blood substitute
    • Winslow R.M. (Ed), Academic Press, London
    • Olson J.S., and Maillett D.H. Designing recombinant hemoglobin for use as a blood substitute. In: Winslow R.M. (Ed). Blood Substitutes (2006), Academic Press, London 354-374
    • (2006) Blood Substitutes , pp. 354-374
    • Olson, J.S.1    Maillett, D.H.2
  • 32
    • 38149109843 scopus 로고    scopus 로고
    • Iron chelators can protect against oxidative stress through ferryl heme reduction
    • Reeder B.J., Hider R.C., and Wilson M.T. Iron chelators can protect against oxidative stress through ferryl heme reduction. Free Radic. Biol. Med. 44 (2008) 264-273
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 264-273
    • Reeder, B.J.1    Hider, R.C.2    Wilson, M.T.3
  • 33
    • 34548674201 scopus 로고    scopus 로고
    • The heme pocket geometry of Lucina pectinata hemoglobin II restricts nitric oxide and peroxide entry: model of ligand control for the design of a stable oxygen carrier
    • De Jesus-Bonilla W., Jia Y., Alayash A.I., and Lopez-Garriga J. The heme pocket geometry of Lucina pectinata hemoglobin II restricts nitric oxide and peroxide entry: model of ligand control for the design of a stable oxygen carrier. Biochemistry 46 (2007) 10451-10460
    • (2007) Biochemistry , vol.46 , pp. 10451-10460
    • De Jesus-Bonilla, W.1    Jia, Y.2    Alayash, A.I.3    Lopez-Garriga, J.4
  • 34
    • 0020742068 scopus 로고
    • Serum catalase activity for detection of hemolytic diseases
    • Goth L., Nemeth H., and Meszaros I. Serum catalase activity for detection of hemolytic diseases. Clin. Chem. 29 (1983) 741-743
    • (1983) Clin. Chem. , vol.29 , pp. 741-743
    • Goth, L.1    Nemeth, H.2    Meszaros, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.