Hemoglobin and iron-evoked oxidative stress in the brain: Protection by bile pigments, managanese and S-nitrosoglutathione

References

• Sadrzadeh S.M.H., Graf E., Panter S.S., Hallaway P.E., Eaton J.W. Hemoglobin. A biological Fenton reagent. Journal of Biological Chemistry 1984; 259: 14354–14356
   PubMed Web of Science ®Google Scholar
• Regan R.F., Panter S.S. Neurotoxicity of hemoglobin in cortical cell culture. Neuroscience Letters 1993; 153: 219–222
   PubMed Web of Science ®Google Scholar
• Everse J., Hsia N. The toxicities of native and modified hemoglobins. Free Radical Biology and Medicine 1997; 22: 1075–1099
   PubMed Web of Science ®Google Scholar
• Gutteridge J.M.C. Iron promotors of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides. FEBS Letters 1986; 201: 291–295
   PubMed Web of Science ®Google Scholar
• Mohanakumar K.P., De Bartolomeis A., Wu R.-M., Yeh K.J., Sternberger L.M., Peng S.-Y., Murphy D.L., Chiueh C.C. Ferrous-citrate complex and nigral degeneration: evidence for free-radical formation and lipid peroxidation. Annals of the New York Academy of Sciences 1994; 738: 392–399
   PubMed Web of Science ®Google Scholar
• Rauhala P., Lin A.M.-Y., Chiueh C.C. Neuroprotection by S-nitrosoglutathione of brain dopamine neurons from oxidative stress. FASEB Journal 1998; 12: 165–173
   PubMed Web of Science ®Google Scholar
• Gutteridge J.M., Bannister J.V. Copper + zinc and manganese superoxide dismutases inhibit deoxyribose degradation by the superoxide-driven Fenton reaction at two different stages. Implications for the redox states of copper and manganese. Biochemical Journal 1986; 234: 225–228
   PubMed Web of Science ®Google Scholar
• Coassin M., Ursini F., Bindoli A. Antioxidant effect of manganese. Archives of Biochemistry and Biophysics 1992; 299: 330–333
   PubMed Web of Science ®Google Scholar
• Sziráki I., Mohanakumar K.P., Rauhala P., Kim H.G., Yeh K.J., Chiueh C.C. Manganese: A transition metal protects nigrostriatal neurons from oxidative stress in the iron-induced animal model of parkinsonism. Neuroscience 1998; 85: 1101–1111
   PubMed Web of Science ®Google Scholar
• Maines M.D. Heme Oxygenase: Clinical Applications and Functions. CRC Press, Inc., Boca Raton 1992
   Google Scholar
• Ewing J.F., Weber C.M., Maines M.D. Bibliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain. Journal of Neurochemistry 1993; 61: 1015–1023
   PubMed Web of Science ®Google Scholar
• Robertson P.J., Fridovich I. A reaction of the superoxide radical with tetrapyrroles. Archives of Biochemistry and Biophysics 1982; 213: 353–357
   PubMed Web of Science ®Google Scholar
• Stocker R., Peterhans E. Antioxidant properties of conjugated bilirubin and biliverdin: biologically relevant scavenging of hypochlorous acid. Free Radical Research Communications 1989; 6: 57–66
   PubMed Web of Science ®Google Scholar
• Stocker R., Yamamoto Y., McDonagh A.F., Glazer A.N., Ames B.N. Bilirubin is an antioxidant of possible physiological importance. Science 1987; 235: 1043–1046
   PubMed Web of Science ®Google Scholar
• Dillard C.J., Tappel A.L. Fluorescent products from reaction of peroxidizing polyunsaturated fatty acids with phosphatidyl ethanolamine and phenylalanine. Lipids 1973; 8: 183–189
   PubMed Web of Science ®Google Scholar
• Paxinos G., Watson C. The Rat Brain in Stereotaxic Coordinates. Academic Press, Inc., San DiegoCalifornia 1986
   Google Scholar
• Chiueh C.C., Zukowska-Grojec Z., Kirk K.L., Kopin I.J. 6-Fluorocatecholamines as false adrenergic neurotransmitters. Journal of Pharmacology and Experimental Therapeutics 1983; 225: 529–533
   PubMedGoogle Scholar
• Singh R.J., Hogg N., Joseph J., Kalyanaraman B. Mechanism of nitric oxide release from S-nitrosothiols. Journal of Biological Chemistry 1996; 271: 18596–18603
   PubMed Web of Science ®Google Scholar
• Panter S.S., Sadrzadeh S.M.H., Hallaway P.E., Haines J.L., Anderson V.E., Eaton J.W. Hypohaptoglobinea associated with familial epilepsy. Journal of Experimental Medicine 1985; 161: 748–754
   PubMedGoogle Scholar
• Sadrzadeh S.M.H., Anderson D.K., Panter S.S., Hallaway P.E., Eaton J.W. Hemoglobin potentiates central nervous system damage. Journal of Clinical Investigation 1987; 79: 662–664
   PubMed Web of Science ®Google Scholar
• Prat A.G., Turrens J.F. Ascorbate- and hemoglobin-dependent brain chemiluminescence. Free Radical Biology and Medicine 1990; 8: 319–325
   PubMed Web of Science ®Google Scholar
• Puppo A., Halliwell B. Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron: Is haemoglobin a biological Fenton reagent?. Biochemical Journal 1988; 249: 185–190
   PubMed Web of Science ®Google Scholar
• Rauhala P., Mohanakumar P., Sziraki I., Lin A.M.-Y., Chiueh C.C. S-Nitrosothiols and nitric oxide, but not sodium nitroprusside, protect nigrostriatal dopamine neurons against iron-induced oxidative stress in vivo. Synapse 1996; 23: 58–60
   PubMed Web of Science ®Google Scholar
• Kanner J., German J.B., Kinsella J.E. Initiation of lipid peroxidation in biological systems. Critical Reviews in Food Science and Nutrition 1987; 25: 317–364
   PubMed Web of Science ®Google Scholar
• Mohanakumar K.P., Hanbauer I., Chiueh C.C. Neuroprotection by nitric oxide against hydroxyl radical-induced nigral neurotoxicity. Journal of Chemical Neuroanatomy 1998; 14: 195–205
   PubMed Web of Science ®Google Scholar
• Sziráki I., Rauhala P., Koh K.K., Van Bergen P., Chiueh C.C. Implications for atypical antioxidative properties of manganese in iron-induced brain lipid peroxidation and copper-dependent low density lipoprotein conjugation. Neurotoxicology 1999; 20: 455–466
   PubMed Web of Science ®Google Scholar
• Hogg N. Pro-oxidant and antioxidant effects of nitric oxide. Analysis of Free Radical in Biological Systems, N. Hogg. Birkhäuser Verlag, Boston 1995; 37–49, In
   Google Scholar
• Kanner J., Harel S., Granit R. Nitric oxide, an inhibitor of lipid peroxidation by lipoxygenase, cycloxy-genase and hemoglobin. Lipids 1992; 27: 46–49
   PubMed Web of Science ®Google Scholar
• Chiueh C.C. Neurobiology of NO· and ·OH: Basic research and clinical relevance. Annals of the New York Academy of Sciences 1994; 738: 279–281
   PubMedGoogle Scholar
• Balla G., Jacob H.S., Balla J. Ferritin: A cytoprotective antioxidant stratagem of endothelium. Journal of Biological Chemistry 1992; 267: 18148–18153
   PubMed Web of Science ®Google Scholar
• Kondo Y., Ogawa N., Asanuma M., Ota Z. Regional differences in late-onset iron deposition, ferritin, transferrin, astrocyte proliferation, and microglial activation after transient forebrain ischemia in rat brain. Journal of Cerebral Blood Flow and Metabolism 1995; 15: 216–226
   PubMed Web of Science ®Google Scholar
• Llesuy S.F., Tomaro M.L. Heme oxygenase and oxidative stress. Evidence of involvement of bilirubin as physiological protector against oxidative damage. Biochimica et Biophysica Acta 1994; 1223: 9–14
   PubMed Web of Science ®Google Scholar
• Velapoldi R.A., Menis O. Formation and stabilities of free bilirubin and bilirubin complexes with transition and rare-earth elements. Clinical Chemistry 1971; 17: 1165–1170
   PubMed Web of Science ®Google Scholar
• Tichy M., Cikrt M., Havrdova J. Manganese binding in rat bile. Archives of Toxicology 1973; 30: 227–236
   Google Scholar
• Matz P., Turner C., Weinstein P.R., Massa S.M., Panter S.S., Sharp F.R. Heme-oxygenase-1 induction in glia throughout rat brain following experimental subarachnoid hemorrhage. Brain Research 1996; 713: 211–222
   PubMed Web of Science ®Google Scholar
• Hall E.D., Braughler J.M. Central nervous system trauma and stroke. Physiological and pharmacological evidence for involvement of oxygen radicals and lipid-peroxidation. Free Radical Biology and Medicine 1989; 6: 303–313
   PubMed Web of Science ®Google Scholar