메뉴 건너뛰기




Volumn 20, Issue 2, 2009, Pages 88-94

The reaction of cell-free oxyhemoglobin with nitrite under physiologically relevant conditions: Implications for nitrite-based therapies

Author keywords

Ascorbic acid; Cell free hemoglobin; Ferrylhemoglobin; Haptoglobin; Nitric oxide; Nitrite; Oxyhemoglobin; Reactive nitrogen species; Uric acid

Indexed keywords

ANTIOXIDANT; ASCORBIC ACID; CATALASE; NITRITE; OXYHEMOGLOBIN; URATE;

EID: 59049096495     PISSN: 10898603     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.niox.2008.10.005     Document Type: Article
Times cited : (16)

References (50)
  • 5
    • 0344443777 scopus 로고    scopus 로고
    • Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction
    • Nagababu E., Ramasamy S., Abernethy D.R., and Rifkind J.M. Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin-mediated nitrite reduction. J. Biol. Chem. 278 (2003) 46349-46356
    • (2003) J. Biol. Chem. , vol.278 , pp. 46349-46356
    • Nagababu, E.1    Ramasamy, S.2    Abernethy, D.R.3    Rifkind, J.M.4
  • 7
    • 23644459872 scopus 로고    scopus 로고
    • The reaction between nitrite and deoxyhemoglobin. Reassessment of reaction kinetics and stoichiometry
    • Huang K.T., Keszler A., Patel N., Patel R.P., Gladwin M.T., Kim-Shapiro D.B., and Hogg N. The reaction between nitrite and deoxyhemoglobin. Reassessment of reaction kinetics and stoichiometry. J. Biol. Chem. 280 (2005) 31126-31131
    • (2005) J. Biol. Chem. , vol.280 , pp. 31126-31131
    • Huang, K.T.1    Keszler, A.2    Patel, N.3    Patel, R.P.4    Gladwin, M.T.5    Kim-Shapiro, D.B.6    Hogg, N.7
  • 9
    • 4544378255 scopus 로고    scopus 로고
    • Reduction of nitrite to nitric oxide during ischemia protects against myocardial ischemia-reperfusion damage
    • Webb A., Bond R., McLean P., Uppal R., Benjamin N., and Ahluwalla A. Reduction of nitrite to nitric oxide during ischemia protects against myocardial ischemia-reperfusion damage. PNAS 101 (2004) 13683-13688
    • (2004) PNAS , vol.101 , pp. 13683-13688
    • Webb, A.1    Bond, R.2    McLean, P.3    Uppal, R.4    Benjamin, N.5    Ahluwalla, A.6
  • 10
    • 4544378255 scopus 로고    scopus 로고
    • Reduction of nitrite to nitric oxide during ischemia protects against myocardial ischemia-reperfusion damage
    • Webb A., Bond R., McLean P., Uppal R., Benjamin N., and Ahluwalia A. Reduction of nitrite to nitric oxide during ischemia protects against myocardial ischemia-reperfusion damage. PNAS 101 (2004) 13683-13688
    • (2004) PNAS , vol.101 , pp. 13683-13688
    • Webb, A.1    Bond, R.2    McLean, P.3    Uppal, R.4    Benjamin, N.5    Ahluwalia, A.6
  • 13
    • 33750869692 scopus 로고    scopus 로고
    • Acellular hemoglobin-mediated oxidative stress toward endothelium: a role for ferryl ion
    • Goldman D.W., Breyer R.J., Yeh D., Brockner-Ryan B.A., and Alayash A.I. Acellular hemoglobin-mediated oxidative stress toward endothelium: a role for ferryl ion. Am. J. Physiol. 275 (1998) H1046-H1053
    • (1998) Am. J. Physiol. , vol.275
    • Goldman, D.W.1    Breyer, R.J.2    Yeh, D.3    Brockner-Ryan, B.A.4    Alayash, A.I.5
  • 14
    • 0032818275 scopus 로고    scopus 로고
    • Detection of a ferrylhemoglobin intermediate in an endothelial cell model after hypoxia-reoxygenation
    • McLeod L.L., and Alayash A.I. Detection of a ferrylhemoglobin intermediate in an endothelial cell model after hypoxia-reoxygenation. Am. J. Physiol. 277 (1999) H92-H99
    • (1999) Am. J. Physiol. , vol.277
    • McLeod, L.L.1    Alayash, A.I.2
  • 15
    • 0033969034 scopus 로고    scopus 로고
    • Effects of hypoxia and glutathione depletion on hemoglobin- and myoglobin-mediated oxidative stress toward endothelium
    • D'Agnillo F., Wood F., Porras C., Macdonald V.W., and Alayash A.I. Effects of hypoxia and glutathione depletion on hemoglobin- and myoglobin-mediated oxidative stress toward endothelium. Biochim. Biophys. Acta 1495 (2000) 150-159
    • (2000) Biochim. Biophys. Acta , vol.1495 , pp. 150-159
    • D'Agnillo, F.1    Wood, F.2    Porras, C.3    Macdonald, V.W.4    Alayash, A.I.5
  • 16
    • 33745141905 scopus 로고    scopus 로고
    • Regular transfusion lower plasma free hemoglobin in children with sickle-cell disease at risk for stroke
    • Lezcano N.E., Odo N., Kutlar A., Brambilla D., and Adams R.J. Regular transfusion lower plasma free hemoglobin in children with sickle-cell disease at risk for stroke. Stroke 37 (2006) 1424-1426
    • (2006) Stroke , vol.37 , pp. 1424-1426
    • Lezcano, N.E.1    Odo, N.2    Kutlar, A.3    Brambilla, D.4    Adams, R.J.5
  • 18
    • 44349096391 scopus 로고    scopus 로고
    • The reaction between nitrite and oxyhemoglobin: a mechanistic study
    • Keszler A., Piknova B., Schechter A.N., and Hogg N. The reaction between nitrite and oxyhemoglobin: a mechanistic study. J. Biol. Chem. 283 (2008) 9615-9622
    • (2008) J. Biol. Chem. , vol.283 , pp. 9615-9622
    • Keszler, A.1    Piknova, B.2    Schechter, A.N.3    Hogg, N.4
  • 19
    • 0020473987 scopus 로고
    • Mechanism of autocatalytic oxidation of oxyhemoglobin by nitrite. An intermediate detected by electron spin resonance
    • Kosaka H., Imaizumi K., and Tyuma I. Mechanism of autocatalytic oxidation of oxyhemoglobin by nitrite. An intermediate detected by electron spin resonance. Biochim. Biophys. Acta 702 (1982) 237-241
    • (1982) Biochim. Biophys. Acta , vol.702 , pp. 237-241
    • Kosaka, H.1    Imaizumi, K.2    Tyuma, I.3
  • 21
    • 0037371492 scopus 로고    scopus 로고
    • Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin
    • Herold S., and Relunann F.G. Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin. Free Rad. Biol. Med. 34 (2003) 531-545
    • (2003) Free Rad. Biol. Med. , vol.34 , pp. 531-545
    • Herold, S.1    Relunann, F.G.2
  • 23
    • 31344462066 scopus 로고    scopus 로고
    • Immuno-spin trapping of hemoglobin and myoglobin radicals derived from nitrite-mediated oxidation
    • Keszler A., Mason R.P., and Hogg N. Immuno-spin trapping of hemoglobin and myoglobin radicals derived from nitrite-mediated oxidation. Free Rad. Biol. Med. 40 (2006) 507-515
    • (2006) Free Rad. Biol. Med. , vol.40 , pp. 507-515
    • Keszler, A.1    Mason, R.P.2    Hogg, N.3
  • 24
    • 0014360531 scopus 로고
    • Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases
    • Muller-Eberhard U., Javid J., Liem H.H., Hanstein A., and Hanna M. Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases. Blood 32 (1968) 811-815
    • (1968) Blood , vol.32 , pp. 811-815
    • Muller-Eberhard, U.1    Javid, J.2    Liem, H.H.3    Hanstein, A.4    Hanna, M.5
  • 26
    • 0029854812 scopus 로고    scopus 로고
    • Biological and clinical significance of haptoglobin polymorphism in humans
    • Langlois M.R., and Delanghe J.R. Biological and clinical significance of haptoglobin polymorphism in humans. Clin. Chem. 42 (1996) 1589-1600
    • (1996) Clin. Chem. , vol.42 , pp. 1589-1600
    • Langlois, M.R.1    Delanghe, J.R.2
  • 28
    • 85047676633 scopus 로고
    • Haptoglobin-haemoglobin complex in human plasma inhibits endothelium dependent relaxation: evidence that endothelium derived relaxing factor acts as a local autocoid
    • Edwards D.H., Griffith T.M., Ryley H.C., and Henderson A.H. Haptoglobin-haemoglobin complex in human plasma inhibits endothelium dependent relaxation: evidence that endothelium derived relaxing factor acts as a local autocoid. Cardiovasc. Res. 8 (1986) 549-556
    • (1986) Cardiovasc. Res. , vol.8 , pp. 549-556
    • Edwards, D.H.1    Griffith, T.M.2    Ryley, H.C.3    Henderson, A.H.4
  • 30
    • 0011085260 scopus 로고
    • Comparative study of peroxidase activity of hemoglobin, methemoglobin and the hemoglobin-haptoglobin complex
    • Waks M., Yon J., Moretti J., and Jayle M.F. Comparative study of peroxidase activity of hemoglobin, methemoglobin and the hemoglobin-haptoglobin complex. Biochim. Biophys. Acta 67 (1963) 417-424
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 417-424
    • Waks, M.1    Yon, J.2    Moretti, J.3    Jayle, M.F.4
  • 31
    • 0015863914 scopus 로고
    • Comparative study of peroxidase activity of met- and oxyhemoglobin complexes with haptoglobin
    • Andreeva A.P., Belostotskii V.M., and Rozenberg G.Ya. Comparative study of peroxidase activity of met- and oxyhemoglobin complexes with haptoglobin. Vopr. Med. Khim. 4 (1973) 378-381
    • (1973) Vopr. Med. Khim. , vol.4 , pp. 378-381
    • Andreeva, A.P.1    Belostotskii, V.M.2    Rozenberg, G.Ya.3
  • 33
    • 1842539298 scopus 로고    scopus 로고
    • Haptoglobin phenotypes differ in their ability to inhibit heme transfer from hemoglobin to LDL
    • Bamm V.V., Tsemakhovich V.A., Shaklai M., and Shaklai N. Haptoglobin phenotypes differ in their ability to inhibit heme transfer from hemoglobin to LDL. Biochemistry 43 (2004) 3899-3906
    • (2004) Biochemistry , vol.43 , pp. 3899-3906
    • Bamm, V.V.1    Tsemakhovich, V.A.2    Shaklai, M.3    Shaklai, N.4
  • 34
    • 72949148692 scopus 로고
    • Studies on the relation between molecular and functional properties of hemoglobin. I. The effect of salts on the molecular weight of human hemoglobin
    • Rossi-Fanelli A., Antonini E., and Caputo A. Studies on the relation between molecular and functional properties of hemoglobin. I. The effect of salts on the molecular weight of human hemoglobin. J. Biol. Chem. 236 (1961) 391-396
    • (1961) J. Biol. Chem. , vol.236 , pp. 391-396
    • Rossi-Fanelli, A.1    Antonini, E.2    Caputo, A.3
  • 35
    • 10444220188 scopus 로고    scopus 로고
    • The reaction between nitrite and hemoglobin: the role of nitrite in hemoglobin-mediated hypoxic vasodilation
    • Kim-Shapiro D.B., Gladwin M.T., Patel R.P., and Hogg N. The reaction between nitrite and hemoglobin: the role of nitrite in hemoglobin-mediated hypoxic vasodilation. J. Inorg. Biochem. 99 (2005) 237-246
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 237-246
    • Kim-Shapiro, D.B.1    Gladwin, M.T.2    Patel, R.P.3    Hogg, N.4
  • 36
    • 0019787519 scopus 로고
    • Uric acid provides antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis
    • Ames B.N., Cathcart R., Schwiers E., and Hochstein P. Uric acid provides antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis. PNAS 78 (1981) 6858-6862
    • (1981) PNAS , vol.78 , pp. 6858-6862
    • Ames, B.N.1    Cathcart, R.2    Schwiers, E.3    Hochstein, P.4
  • 37
    • 0344701041 scopus 로고    scopus 로고
    • How different constituents of human plasma and low density lipoprotein determine plasma oxidizability by copper
    • Spranger T., Finckh B., Fingerhut R., Kohlshutter A., Beisiegel U., and Kontush A. How different constituents of human plasma and low density lipoprotein determine plasma oxidizability by copper. Chem. Phys. Lipids 91 (1998) 39-52
    • (1998) Chem. Phys. Lipids , vol.91 , pp. 39-52
    • Spranger, T.1    Finckh, B.2    Fingerhut, R.3    Kohlshutter, A.4    Beisiegel, U.5    Kontush, A.6
  • 38
    • 0033067174 scopus 로고    scopus 로고
    • Ascorbate prevents prooxidant effects of urate in oxidation of human low density lipoprotein
    • Abuja P.M. Ascorbate prevents prooxidant effects of urate in oxidation of human low density lipoprotein. FEBS Lett. 446 (1999) 305-308
    • (1999) FEBS Lett. , vol.446 , pp. 305-308
    • Abuja, P.M.1
  • 40
    • 0014545815 scopus 로고
    • Formation of ferrihaemoglobin with aminophenols in the human for the treatment of cyanide poisoning
    • Kiese M., and Weger N. Formation of ferrihaemoglobin with aminophenols in the human for the treatment of cyanide poisoning. Eur. J. Pharmacol. 7 (1969) 97-105
    • (1969) Eur. J. Pharmacol. , vol.7 , pp. 97-105
    • Kiese, M.1    Weger, N.2
  • 41
    • 0015219592 scopus 로고
    • Some spectral properties of the human hemoglobin-haptoglobin complex
    • Hamaguchi H., Isomoto A., Miyake Y., and Nakajima H. Some spectral properties of the human hemoglobin-haptoglobin complex. Biochemistry 10 (1971) 1741-1745
    • (1971) Biochemistry , vol.10 , pp. 1741-1745
    • Hamaguchi, H.1    Isomoto, A.2    Miyake, Y.3    Nakajima, H.4
  • 42
    • 0015209659 scopus 로고
    • Studies on structure of haptoglobin 1-1 and hemoglobin in the haptoglobin-hemoglobin complex
    • Waks M., Kahn P.C., and Beychok S. Studies on structure of haptoglobin 1-1 and hemoglobin in the haptoglobin-hemoglobin complex. Biochem. Biophys. Res. Commun. 45 (1971) 1232-1239
    • (1971) Biochem. Biophys. Res. Commun. , vol.45 , pp. 1232-1239
    • Waks, M.1    Kahn, P.C.2    Beychok, S.3
  • 43
    • 0030766447 scopus 로고    scopus 로고
    • Oxidation of low-density lipoprotein by hemoglobin stems from heme-initiated globin radical: antioxidant role of haptoglobin
    • Miller Y.I., Altamentova S.M., and Shaklai N. Oxidation of low-density lipoprotein by hemoglobin stems from heme-initiated globin radical: antioxidant role of haptoglobin. Biochemistry 36 (1997) 12189-12198
    • (1997) Biochemistry , vol.36 , pp. 12189-12198
    • Miller, Y.I.1    Altamentova, S.M.2    Shaklai, N.3
  • 44
    • 0017085842 scopus 로고
    • A mechanism for the conversion of oxyhemoglobin to methemoglobin by nitrite
    • Rodkey F. A mechanism for the conversion of oxyhemoglobin to methemoglobin by nitrite. Clin. Chem. 22 (1976) 1986-1990
    • (1976) Clin. Chem. , vol.22 , pp. 1986-1990
    • Rodkey, F.1
  • 45
    • 0022313068 scopus 로고
    • Autocatalytic oxidation of hemoglobin induced by nitrite: activation and chemical inhibition
    • Doyle M., Herman J., and Dykstra L. Autocatalytic oxidation of hemoglobin induced by nitrite: activation and chemical inhibition. J. Free Rad. Biol. Med. 1 (1985) 145-153
    • (1985) J. Free Rad. Biol. Med. , vol.1 , pp. 145-153
    • Doyle, M.1    Herman, J.2    Dykstra, L.3
  • 46
    • 0031865532 scopus 로고
    • Autocatalytic oxidation of hemoglobin by nitrite: a possible mechanism
    • Lissi E. Autocatalytic oxidation of hemoglobin by nitrite: a possible mechanism. J. Free Rad. Biol. Med. 24 (1988) 1535-1536
    • (1988) J. Free Rad. Biol. Med. , vol.24 , pp. 1535-1536
    • Lissi, E.1
  • 47
    • 0023553145 scopus 로고
    • Mechanism of autocatalytic oxidation of oxyhemoglobin by nitrite
    • Kosaka H., and Tyuma I. Mechanism of autocatalytic oxidation of oxyhemoglobin by nitrite. Environ. Health Perspect. 73 (1987) 147-151
    • (1987) Environ. Health Perspect. , vol.73 , pp. 147-151
    • Kosaka, H.1    Tyuma, I.2
  • 48
    • 4644255218 scopus 로고    scopus 로고
    • Scavenging of reactive nitrogen species by oxygenated hemoglobin: globin radicals and nitrotyrosines distinguish nitrite from nitric oxide reaction
    • Pietraforte D., Salzano A.M., Scorza G., and Minetti M. Scavenging of reactive nitrogen species by oxygenated hemoglobin: globin radicals and nitrotyrosines distinguish nitrite from nitric oxide reaction. Free Rad. Biol. Med. 37 (2004) 1244-1255
    • (2004) Free Rad. Biol. Med. , vol.37 , pp. 1244-1255
    • Pietraforte, D.1    Salzano, A.M.2    Scorza, G.3    Minetti, M.4
  • 50
    • 34249284160 scopus 로고    scopus 로고
    • Repetition of ischemic preconditioning augments endothelium-dependent vasodilation in humans. Role of endothelium-derived nitric oxide and endothelial progenitor cells
    • Kimura M., Ueda K., Goto C., Jitsuiki D., Nishioka K., Umemura T., Noma K., Yoshizumi M., Chayama K., and Higashi Y. Repetition of ischemic preconditioning augments endothelium-dependent vasodilation in humans. Role of endothelium-derived nitric oxide and endothelial progenitor cells. Arterioscler. Thromb. Vasc. Biol. 27 (2007) 1403-1410
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 1403-1410
    • Kimura, M.1    Ueda, K.2    Goto, C.3    Jitsuiki, D.4    Nishioka, K.5    Umemura, T.6    Noma, K.7    Yoshizumi, M.8    Chayama, K.9    Higashi, Y.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.