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Volumn 24, Issue 12, 1999, Pages 1507-1514

Potential role of cerebral glutathione in the maintenance of blood-brain barrier integrity in rat

Author keywords

Antioxidants; Blood brain barrier permeability; Brain; Glutathione depletion; Microvessels; Rat; Sulfhydryls

Indexed keywords

ALPHA TOCOPHEROL; ASCORBIC ACID; GLUTATHIONE;

EID: 0032752658     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1021191729865     Document Type: Article
Times cited : (79)

References (41)
  • 1
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister, A. 1988. Glutathione metabolism and its selective modification. J. Biol. Chem. 263:17205-17208.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 3
    • 0025719132 scopus 로고
    • Role of lipid peroxidation on renal dysfunction associated with glutathione depletion: Effects of vitamin E
    • Torres, M. A., Ochoa, E., and Elias, M. M. 1991. Role of lipid peroxidation on renal dysfunction associated with glutathione depletion: effects of vitamin E. Toxicology 70:163-172.
    • (1991) Toxicology , vol.70 , pp. 163-172
    • Torres, M.A.1    Ochoa, E.2    Elias, M.M.3
  • 4
    • 0002149754 scopus 로고
    • The anatomic basis of the blood-brain barrier
    • Neuwelt, E. A. (ed.) Pelnum Medical Book, New York, NY
    • Brightman, M. W. 1989. The anatomic basis of the blood-brain barrier. Pages 53-83, in Neuwelt, E. A. (ed.) Implications of the blood-brain barrier and its manipulation, vol. I, Pelnum Medical Book, New York, NY.
    • (1989) Implications of the Blood-brain Barrier and Its Manipulation , vol.1 , pp. 53-83
    • Brightman, M.W.1
  • 5
    • 0029890931 scopus 로고    scopus 로고
    • Pathophysiology of the blood-brain barrier
    • Selmaj, K. 1996. Pathophysiology of the blood-brain barrier. Springer Seminars in Immunopathol. 18:57-73.
    • (1996) Springer Seminars in Immunopathol. , vol.18 , pp. 57-73
    • Selmaj, K.1
  • 6
    • 0024496048 scopus 로고
    • Methods for depleting brain glutathione
    • Masukawa, T., Sai, H., and Tochino, Y. 1989. Methods for depleting brain glutathione. Life Sci. 44:417-424.
    • (1989) Life Sci. , vol.44 , pp. 417-424
    • Masukawa, T.1    Sai, H.2    Tochino, Y.3
  • 7
    • 0021252274 scopus 로고
    • Morphine metabolism revisited. II Isolation and chemical characterization of a glutathionyl morphine adduct from rat liver microsome preparation
    • Correira, M. A., Krowech, G., Caldera, M. P., Yei, S. L., Straub, K., and Castagnoli, J. R. N. 1984. Morphine metabolism revisited. II Isolation and chemical characterization of a glutathionyl morphine adduct from rat liver microsome preparation. Chem. Biol. Interact. 51:13-24.
    • (1984) Chem. Biol. Interact. , vol.51 , pp. 13-24
    • Correira, M.A.1    Krowech, G.2    Caldera, M.P.3    Yei, S.L.4    Straub, K.5    Castagnoli, J.R.N.6
  • 8
    • 0023837593 scopus 로고
    • Phenytoin metabolic activation role of cytochrome P-450 glutathione on age and sex in rats and mice
    • Roy, D., and Snodgrass, W. R. 1988. Phenytoin metabolic activation role of cytochrome P-450 glutathione on age and sex in rats and mice. Res. Commun. Chem. Pathol. Pharmacol. 59:173-190.
    • (1988) Res. Commun. Chem. Pathol. Pharmacol. , vol.59 , pp. 173-190
    • Roy, D.1    Snodgrass, W.R.2
  • 10
    • 0026004832 scopus 로고
    • Inhibition of glutathione in the new born rat: A model for endogenously produced oxidative stress
    • Martensson, J., Jain, A., Stole, E., Frayer, W., Auld, P., and Meister, A. 1991. Inhibition of glutathione in the new born rat: a model for endogenously produced oxidative stress. Proc. Natn. Acad. Sci. USA 88:9360-9364.
    • (1991) Proc. Natn. Acad. Sci. USA , vol.88 , pp. 9360-9364
    • Martensson, J.1    Jain, A.2    Stole, E.3    Frayer, W.4    Auld, P.5    Meister, A.6
  • 11
    • 0027160230 scopus 로고
    • Alterations in free radical scanvenging mechanisms following blood-brain barrier disruption
    • Shukla, A., Shukla, R., Dikshit, M., and Srimal, R. C. 1993. Alterations in free radical scanvenging mechanisms following blood-brain barrier disruption. Free Radical Biol. Med. 15: 97-100.
    • (1993) Free Radical Biol. Med. , vol.15 , pp. 97-100
    • Shukla, A.1    Shukla, R.2    Dikshit, M.3    Srimal, R.C.4
  • 12
    • 0025319983 scopus 로고
    • Brain edema and cerebrovascular permeability during cerebral ischemia in rats
    • Hatashita, S., and Hoff, J. T. 1990. Brain edema and cerebrovascular permeability during cerebral ischemia in rats. Stroke 21:582-588.
    • (1990) Stroke , vol.21 , pp. 582-588
    • Hatashita, S.1    Hoff, J.T.2
  • 13
    • 0031831764 scopus 로고    scopus 로고
    • Gelatinase B modulates selective opening of blood-brain barrier during inflammation
    • Mun-Bryce, S., and Rosenberg, G. A. 1998. Gelatinase B modulates selective opening of blood-brain barrier during inflammation. Am. J. Physiol. 274:R1203-1211.
    • (1998) Am. J. Physiol. , vol.274
    • Mun-Bryce, S.1    Rosenberg, G.A.2
  • 14
    • 0015406680 scopus 로고
    • The interaction of sol uble horseradish peroxidase with mouse peritoneal macrophage in vitro
    • Steinman, R. M., and Cohn, Z. A. 1972. The interaction of sol uble horseradish peroxidase with mouse peritoneal macrophage in vitro. J. Cell Biol. 55:186-207.
    • (1972) J. Cell Biol. , vol.55 , pp. 186-207
    • Steinman, R.M.1    Cohn, Z.A.2
  • 15
    • 0019015965 scopus 로고
    • Quantitative aspects of reversible osmotic opening of blood-brain barrier
    • Rapoport, S. I., Fredericks, W. R., Ohono, K., and Pettigrew, K. D. 1980. Quantitative aspects of reversible osmotic opening of blood-brain barrier. Am. J. Physiol. 238:R421-R431.
    • (1980) Am. J. Physiol. , vol.238
    • Rapoport, S.I.1    Fredericks, W.R.2    Ohono, K.3    Pettigrew, K.D.4
  • 16
    • 0023220937 scopus 로고
    • Enzymatic protection against peroxidative damage in isolated capillaries
    • Tayarani, I., Chaudiere, J., Leufauconnier, J. M., and Bouree, J. M. 1987. Enzymatic protection against peroxidative damage in isolated capillaries. J. Neurochem. 48:1399-1402.
    • (1987) J. Neurochem. , vol.48 , pp. 1399-1402
    • Tayarani, I.1    Chaudiere, J.2    Leufauconnier, J.M.3    Bouree, J.M.4
  • 17
    • 0016151122 scopus 로고
    • Bromobenzene induced liver necrosis: Protective role of glutathione and evidence for 34-bromobenzene oxide as the hepatotoxic intermediate
    • Jollow, D. J., Mitchell, J. R., Zampaglione, N., and Gillete, J. R. 1974. Bromobenzene induced liver necrosis: Protective role of glutathione and evidence for 34-bromobenzene oxide as the hepatotoxic intermediate. Pharmacol. 11:151-169.
    • (1974) Pharmacol. , vol.11 , pp. 151-169
    • Jollow, D.J.1    Mitchell, J.R.2    Zampaglione, N.3    Gillete, J.R.4
  • 18
    • 0017064979 scopus 로고
    • A fluorometric method for determination of oxidized and reduced glutathione in tissues
    • Hissin, P. J., and Hilf, R. 1976. A fluorometric method for determination of oxidized and reduced glutathione in tissues. Analyt. Chem. 74:214-226.
    • (1976) Analyt. Chem. , vol.74 , pp. 214-226
    • Hissin, P.J.1    Hilf, R.2
  • 19
    • 0018384650 scopus 로고
    • Assay of lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa, H., Ohishi, N., and Yagi, K. 1979. Assay of lipid peroxides in animal tissues by thiobarbituric acid reaction. Analyt. Biochem. 95:351-358.
    • (1979) Analyt. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 20
    • 0031418498 scopus 로고    scopus 로고
    • Neurodegenerative disorders in humans: The role of glutathione in oxidative stress-mediated neuronal death
    • Bains, J. S., and Shaw, C. A. 1997. Neurodegenerative disorders in humans: The role of glutathione in oxidative stress-mediated neuronal death. Brain Res. Rev. 25:335-358.
    • (1997) Brain Res. Rev. , vol.25 , pp. 335-358
    • Bains, J.S.1    Shaw, C.A.2
  • 22
    • 0022451496 scopus 로고
    • Effect of diethylmaleate and other glutathione depletors on protein synthesis
    • Costa, L. G., and Murphy, S. D. 1986. Effect of diethylmaleate and other glutathione depletors on protein synthesis. Biochem. Pharmacol. 19:3383-3388.
    • (1986) Biochem. Pharmacol. , vol.19 , pp. 3383-3388
    • Costa, L.G.1    Murphy, S.D.2
  • 23
    • 0022335174 scopus 로고
    • Influences of pyrazolones of hepatic glutathione in rats
    • Bien, E., and Witt, M. 1985. Influences of pyrazolones of hepatic glutathione in rats. Archs Toxicol. 8 Suppl.:366-369.
    • (1985) Archs Toxicol. , vol.8 , Issue.SUPPL. , pp. 366-369
    • Bien, E.1    Witt, M.2
  • 24
    • 0025218499 scopus 로고
    • Development of the blood-brain barrier
    • Risau, W., and Wolburg, H. 1990. Development of the blood-brain barrier. Trends Neurosci. 13:174-178.
    • (1990) Trends Neurosci. , vol.13 , pp. 174-178
    • Risau, W.1    Wolburg, H.2
  • 25
    • 0024407187 scopus 로고
    • Biochemistry of oxygen toxicity
    • Cadenas, E. 1989. Biochemistry of oxygen toxicity. Ann. Rev. Biochem. 58:79-110.
    • (1989) Ann. Rev. Biochem. , vol.58 , pp. 79-110
    • Cadenas, E.1
  • 26
    • 0026468245 scopus 로고
    • Commentary on antioxidant effects of ascorbic acid and glutathione
    • Meister, A. 1992. Commentary on antioxidant effects of ascorbic acid and glutathione. Biochem. Pharmacol. 44:1905-1915.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 1905-1915
    • Meister, A.1
  • 27
    • 0022559216 scopus 로고
    • Oxy-radicals and related species. Their formation lifetime and reaction
    • Pryor, W. A. 1986. Oxy-radicals and related species. Their formation lifetime and reaction. Ann. Rev. Physiol. 48:657-667.
    • (1986) Ann. Rev. Physiol. , vol.48 , pp. 657-667
    • Pryor, W.A.1
  • 29
    • 0031037710 scopus 로고    scopus 로고
    • Effect of 2-cyclohexene-1-one induced glutathione diminution on ischemia/ reperfusion induced alterations in the physical state of brain synaptosomal membrane proteins and lipids
    • Hall, N. C., Carney, J. M., Plante, O. J., Chang, M., and Butterfield, D. A. 1997. Effect of 2-cyclohexene-1-one induced glutathione diminution on ischemia/ reperfusion induced alterations in the physical state of brain synaptosomal membrane proteins and lipids. Neurosci. 77:283-290.
    • (1997) Neurosci. , vol.77 , pp. 283-290
    • Hall, N.C.1    Carney, J.M.2    Plante, O.J.3    Chang, M.4    Butterfield, D.A.5
  • 30
    • 0021815329 scopus 로고
    • Natural antioxidants. III. Antioxidative compounds isolated from rhizome of Curcuma longa L
    • Toda, S., Miyase, T., Tanizawa, H., and Takino, Y. 1985. Natural antioxidants. III. Antioxidative compounds isolated from rhizome of Curcuma longa L. Chem. Pharmaceutical Bull.Tokyo 33:1725-1728.
    • (1985) Chem. Pharmaceutical Bull.Tokyo , vol.33 , pp. 1725-1728
    • Toda, S.1    Miyase, T.2    Tanizawa, H.3    Takino, Y.4
  • 31
    • 0026556889 scopus 로고
    • Turmerin: A water soluble antioxidant peptide from turmeric Curcuma longa
    • Srinivas, L., Shalini, V. K., and Shylaja, M. 1992. Turmerin: A water soluble antioxidant peptide from turmeric Curcuma longa. Arch. Biochem. Biophys. 292:617-623.
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 617-623
    • Srinivas, L.1    Shalini, V.K.2    Shylaja, M.3
  • 32
    • 0016732297 scopus 로고
    • Long term home use of acetyl cysteine in chronic bronchitis
    • Chodosh, S., Baigelman, W., Medici, T. C., and Enslein, K. 1975. Long term home use of acetyl cysteine in chronic bronchitis. Curr. Ther. Res. 17:319-334.
    • (1975) Curr. Ther. Res. , vol.17 , pp. 319-334
    • Chodosh, S.1    Baigelman, W.2    Medici, T.C.3    Enslein, K.4
  • 33
    • 0017753701 scopus 로고
    • The role of methionine in glutathione biosynthesis
    • Reed, D. J., and Orrenius, S. 1977. The role of methionine in glutathione biosynthesis. Biochem. biophys. Res. Commun. 77: 1257-1264.
    • (1977) Biochem. Biophys. Res. Commun. , vol.77 , pp. 1257-1264
    • Reed, D.J.1    Orrenius, S.2
  • 34
    • 0020479399 scopus 로고
    • Effect of sulfhydryl group modification on the activities of 5-oxo-L-prolinase
    • Williamson, J. M., and Meister, A. 1982. Effect of sulfhydryl group modification on the activities of 5-oxo-L-prolinase. J. Biol. Chem. 257:9167-9169.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9167-9169
    • Williamson, J.M.1    Meister, A.2
  • 35
    • 0024820974 scopus 로고
    • Effect of oral glutathione on hepatic glutathione levels in rats and mice
    • Vina, J., Penez, C., Furukawa, T., Palacin, M., and Vina, J. R. 1989. Effect of oral glutathione on hepatic glutathione levels in rats and mice. Br. J. Nutr. 62:683-691.
    • (1989) Br. J. Nutr. , vol.62 , pp. 683-691
    • Vina, J.1    Penez, C.2    Furukawa, T.3    Palacin, M.4    Vina, J.R.5
  • 36
    • 0026343403 scopus 로고
    • Glutathione deficiency produced by inhibition of its synthesis and its reversal application in research and therapy
    • Meister, A. 1991. Glutathione deficiency produced by inhibition of its synthesis and its reversal application in research and therapy. Pharmacol. Ther. 55:155-194.
    • (1991) Pharmacol. Ther. , vol.55 , pp. 155-194
    • Meister, A.1
  • 37
    • 0025303448 scopus 로고
    • Evidence for carrier-mediated transport of glutathione across the blood-brain barrier in the rat
    • Kannan, R., Kuhlenkamp, J. F., Jeandider, E., Triuh, H., Ookntens, M., and Kaplowitz, N. 1990. Evidence for carrier-mediated transport of glutathione across the blood-brain barrier in the rat. J. Clin. Invest. 85:2009-2013.
    • (1990) J. Clin. Invest. , vol.85 , pp. 2009-2013
    • Kannan, R.1    Kuhlenkamp, J.F.2    Jeandider, E.3    Triuh, H.4    Ookntens, M.5    Kaplowitz, N.6
  • 38
    • 0029942499 scopus 로고    scopus 로고
    • Evidence of the existence of sodium-dependent glutathione GSH transporter. Expression of bovine capillary mRNA and size fractions in Xenopus laevis oocytes and dissociation from γ-glutamyl transpeptidase and facilitative transporters
    • Kannan, R., Yi, J. R., Tang, D., Li, Y., Zlokovic, B. V., and Kaplowitz, N. 1996. Evidence of the existence of sodium-dependent glutathione GSH transporter. Expression of bovine capillary mRNA and size fractions in Xenopus laevis oocytes and dissociation from γ-glutamyl transpeptidase and facilitative transporters. J. Biol. Chem. 271:9754-9758.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9754-9758
    • Kannan, R.1    Yi, J.R.2    Tang, D.3    Li, Y.4    Zlokovic, B.V.5    Kaplowitz, N.6
  • 39
    • 0023571723 scopus 로고
    • Lipid peroxidation protein thiols and calcium homeostasis in bromobenzene-induced liver damage
    • Casini, A. F., Maellaro, E., Pompella, A., Ferrali, M., and Comporti, M. 1987. Lipid peroxidation protein thiols and calcium homeostasis in bromobenzene-induced liver damage. Biochem. Pharmacol. 36:3689-3695.
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 3689-3695
    • Casini, A.F.1    Maellaro, E.2    Pompella, A.3    Ferrali, M.4    Comporti, M.5
  • 40
    • 0029160112 scopus 로고
    • 21-aminosteroid and 2-aminomethyl chromans inhibition of arachnoid acid-induced lipid peroxidation and permeability enhancement in bovine brain microvessel endothelial cell monlayers
    • Shi, F., Cavitt, J., and Audus, K. L. 1995. 21-aminosteroid and 2-aminomethyl chromans inhibition of arachnoid acid-induced lipid peroxidation and permeability enhancement in bovine brain microvessel endothelial cell monlayers. Free Radical Biol. Med. 19:349-357.
    • (1995) Free Radical Biol. Med. , vol.19 , pp. 349-357
    • Shi, F.1    Cavitt, J.2    Audus, K.L.3
  • 41
    • 0030058338 scopus 로고    scopus 로고
    • Protective effects of tirilazad mesylate and metabolite U-89678 against blood-brain barrier damage after subarachnoid hemorrage and lipid peroxidative neuronal injury
    • Smith, S. L., Scherch, H. M., and Hall, E. D. 1996. Protective effects of tirilazad mesylate and metabolite U-89678 against blood-brain barrier damage after subarachnoid hemorrage and lipid peroxidative neuronal injury. J. Neurosurg. 84:229-233.
    • (1996) J. Neurosurg. , vol.84 , pp. 229-233
    • Smith, S.L.1    Scherch, H.M.2    Hall, E.D.3


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