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Volumn 28, Issue 15, 2003, Pages 1643-1652

Effects of prostaglandin E1, melatonin, and oxytetracycline on lipid peroxidation, antioxidant defense system, paraoxonase (PON1) activities, and homocysteine levels in an animal model of spinal cord injury

Author keywords

Antioxidant drugs; Homocysteine; Lipid peroxidation; Paraoxonase; Spinal cord injury

Indexed keywords

ANTIOXIDANT; ARYLDIALKYLPHOSPHATASE; GLUTATHIONE PEROXIDASE; HOMOCYSTEINE; MALONALDEHYDE; MELATONIN; OXYTETRACYCLINE; PRIMAMYCIN; PROSTAGLANDIN E1; PROSTAVASIN; SUPEROXIDE DISMUTASE;

EID: 0042074511     PISSN: 03622436     EISSN: None     Source Type: Journal    
DOI: 10.1097/01.BRS.0000083163.03910.B1     Document Type: Article
Times cited : (38)

References (109)
  • 1
    • 0020963407 scopus 로고
    • The role of oxygen free radicals in human disease processes
    • Bulkley GB. The role of oxygen free radicals in human disease processes. Surgery 1983;94:407-11.
    • (1983) Surgery , vol.94 , pp. 407-411
    • Bulkley, G.B.1
  • 2
    • 0022529172 scopus 로고
    • Oxygen free radicals and iron in relation to biology and medicine: Some problems and concepts
    • Halliwell B, Gutteridge JM. Oxygen free radicals and iron in relation to biology and medicine: some problems and concepts. Arch Biochem Biophys 1986;246:501-14.
    • (1986) Arch Biochem Biophys , vol.246 , pp. 501-514
    • Halliwell, B.1    Gutteridge, J.M.2
  • 3
    • 0032167533 scopus 로고    scopus 로고
    • Alterations in superoxide dismutase activities, lipid peroxidation and glutathione levels in thinner-inhaled rat lung: Relationship between histopathological properties
    • Ulakoglu EZ, Saygi A, Gumustas MK, et al. Alterations in superoxide dismutase activities, lipid peroxidation and glutathione levels in thinner-inhaled rat lung: relationship between histopathological properties. Pharmacol Res 1998;38:209-14.
    • (1998) Pharmacol Res , vol.38 , pp. 209-214
    • Ulakoglu, E.Z.1    Saygi, A.2    Gumustas, M.K.3
  • 4
    • 0034093311 scopus 로고    scopus 로고
    • Superoxide dismutase activity and the effects of NBQX and CPP on lipid peroxidation in experimental spinal cord injury
    • Gorgulu A, Kiris T, Unal F, et al. Superoxide dismutase activity and the effects of NBQX and CPP on lipid peroxidation in experimental spinal cord injury. Res Exp Med 2000;199:285-93.
    • (2000) Res Exp Med , vol.199 , pp. 285-293
    • Gorgulu, A.1    Kiris, T.2    Unal, F.3
  • 5
    • 0021722482 scopus 로고
    • Reevaluation of assay methods and establishment of kit for superoxide dismutase activity
    • Oyanagui Y. Reevaluation of assay methods and establishment of kit for superoxide dismutase activity. Anal Biochem 1984;142:290-6.
    • (1984) Anal Biochem , vol.142 , pp. 290-296
    • Oyanagui, Y.1
  • 6
    • 0024496830 scopus 로고
    • Antihuman plasma glutathione peroxidase antibodies: Immunologic investigations to determine plasma glutathione peroxidase protein and selenium content in plasma
    • Avissar N, Whitin JC, Allen PZ, et al. Antihuman plasma glutathione peroxidase antibodies: immunologic investigations to determine plasma glutathione peroxidase protein and selenium content in plasma. Blood 1989;73:318-23.
    • (1989) Blood , vol.73 , pp. 318-323
    • Avissar, N.1    Whitin, J.C.2    Allen, P.Z.3
  • 7
    • 0026047054 scopus 로고
    • Oxygen free radicals and myocardial damage: Protective role of thiol-containing agents
    • Ferrari R, Ceconi C, Curello S, et al. Oxygen free radicals and myocardial damage: protective role of thiol-containing agents. Am J Med 1991;91(suppl 3C):95S-105S.
    • (1991) Am J Med , vol.91 , Issue.SUPPL. 3C
    • Ferrari, R.1    Ceconi, C.2    Curello, S.3
  • 8
    • 0001359504 scopus 로고
    • Glutathione peroxidase
    • Jakoby WB, Bend JR, Caldwell J, eds. New York, NY: Academic Press
    • Wendel A. Glutathione peroxidase. In: Jakoby WB, Bend JR, Caldwell J, eds. Enzymatic Basis of Detoxication. New York, NY: Academic Press; 1980:333-48.
    • (1980) Enzymatic Basis of Detoxication , pp. 333-348
    • Wendel, A.1
  • 9
    • 0033822421 scopus 로고    scopus 로고
    • Homocysteine, coagulation, platelet function, and thrombosis
    • Coppola A, Davi G, De Stefano V, et al. Homocysteine, coagulation, platelet function, and thrombosis. Semin Thromb Hemost 2000;26:243-54.
    • (2000) Semin Thromb Hemost , vol.26 , pp. 243-254
    • Coppola, A.1    Davi, G.2    De Stefano, V.3
  • 10
    • 0030728675 scopus 로고    scopus 로고
    • Acute methionine load-induced hyperhomocystinemia enhances platelet aggregation, thromboxane biosynthesis, and macrophage-derived tissue factor activity in rats
    • Durand P, Lussier-Cacan S, Blache D. Acute methionine load-induced hyperhomocystinemia enhances platelet aggregation, thromboxane biosynthesis, and macrophage-derived tissue factor activity in rats. FASEB J 1997;11:1157-68.
    • (1997) FASEB J , vol.11 , pp. 1157-1168
    • Durand, P.1    Lussier-Cacan, S.2    Blache, D.3
  • 11
    • 0031816430 scopus 로고    scopus 로고
    • Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymatic activity
    • Kuo CL, La Du BN. Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymatic activity. Drug Metab Dispos 1998;26:653-60.
    • (1998) Drug Metab Dispos , vol.26 , pp. 653-660
    • Kuo, C.L.1    La Du, B.N.2
  • 12
    • 0002198623 scopus 로고    scopus 로고
    • Paraoxonase polymorphism Met-Leu54 is associated with modified concentrations of the enzyme
    • Blatter Garin M-C, James RW, Dussoix P, et al. Paraoxonase polymorphism Met-Leu54 is associated with modified concentrations of the enzyme. J Clin Invest 1997;99:62-6.
    • (1997) J Clin Invest , vol.99 , pp. 62-66
    • Blatter Garin, M.-C.1    James, R.W.2    Dussoix, P.3
  • 14
    • 0032971881 scopus 로고    scopus 로고
    • Paraoxanase genes and disease
    • Hegele RA. Paraoxanase genes and disease. Ann Med 1999;31:217-24.
    • (1999) Ann Med , vol.31 , pp. 217-224
    • Hegele, R.A.1
  • 15
    • 0015954510 scopus 로고
    • Generation of superoxide free radical during the autoxidation of thiols
    • Misra HP. Generation of superoxide free radical during the autoxidation of thiols. J Biol Chem 1974;249:2151-5.
    • (1974) J Biol Chem , vol.249 , pp. 2151-2155
    • Misra, H.P.1
  • 16
    • 0020477158 scopus 로고
    • Superoxide dependent formation of hydroxyl radicals in the presence of thiol compounds
    • Rowley DA, Halliwell B. Superoxide dependent formation of hydroxyl radicals in the presence of thiol compounds. FEBS Lett 1982;138:33-6.
    • (1982) FEBS Lett , vol.138 , pp. 33-36
    • Rowley, D.A.1    Halliwell, B.2
  • 17
    • 0011895769 scopus 로고
    • Membrane lipid changes in laminectomized and traumatized cat spinal cord
    • Demediuk P, Saunders RD, Anderson DK, et al. Membrane lipid changes in laminectomized and traumatized cat spinal cord. Proc Natl Acad Sci USA 1985;82:7071-5.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7071-7075
    • Demediuk, P.1    Saunders, R.D.2    Anderson, D.K.3
  • 18
    • 0025165274 scopus 로고
    • Effects of competitive and non-competitive NMDA receptor antagonists in spinal cord injury
    • Faden AI, Ellison JA, Noble LJ. Effects of competitive and non-competitive NMDA receptor antagonists in spinal cord injury. Eur J Pharmacol 1990;175:165-74.
    • (1990) Eur J Pharmacol , vol.175 , pp. 165-174
    • Faden, A.I.1    Ellison, J.A.2    Noble, L.J.3
  • 19
    • 0034221598 scopus 로고    scopus 로고
    • Comparison of the effects of melatonin and methylprednisolone in experimental spinal cord injury
    • Kaptanoglu E, Tuncel M, Palaoglu S, et al. Comparison of the effects of melatonin and methylprednisolone in experimental spinal cord injury. J Neurosurg 2000;93(suppl 1):77-84.
    • (2000) J Neurosurg , vol.93 , Issue.SUPPL. 1 , pp. 77-84
    • Kaptanoglu, E.1    Tuncel, M.2    Palaoglu, S.3
  • 20
    • 0034109501 scopus 로고    scopus 로고
    • Lazaroid reduces production of IL-8 and IL-1 receptor antagonist in ischemic spinal cord injury
    • Kunihara T, Sasaki S, Shiiya N, et al. Lazaroid reduces production of IL-8 and IL-1 receptor antagonist in ischemic spinal cord injury. Ann Thorac Surg 2000;69:792-8.
    • (2000) Ann Thorac Surg , vol.69 , pp. 792-798
    • Kunihara, T.1    Sasaki, S.2    Shiiya, N.3
  • 21
    • 0023195163 scopus 로고
    • Effects of methylprednisolone and the combination of α-tocopherol and selenium on arachidonic acid metabolism and lipid peroxidation in traumatized spinal cord tissue
    • Saunders RD, Dugan LL, Demediuk P, et al. Effects of methylprednisolone and the combination of α-tocopherol and selenium on arachidonic acid metabolism and lipid peroxidation in traumatized spinal cord tissue. J Neurochem 1987;49:24-31.
    • (1987) J Neurochem , vol.49 , pp. 24-31
    • Saunders, R.D.1    Dugan, L.L.2    Demediuk, P.3
  • 22
    • 0025292485 scopus 로고
    • Experimental neoplastic spinal cord compression: Effect of anti-inflammatory agents and glutamate receptor antagonists on vascular permeability
    • Siegal T, Siegal T, Lossos F. Experimental neoplastic spinal cord compression: effect of anti-inflammatory agents and glutamate receptor antagonists on vascular permeability. Neurosurgery 1990;26:967-70.
    • (1990) Neurosurgery , vol.26 , pp. 967-970
    • Siegal, T.1    Siegal, T.2    Lossos, F.3
  • 23
    • 0036941831 scopus 로고    scopus 로고
    • Effects of methylprednisolone and dextromethorphan on lipid peroxidation in an experimental model of spinal cord injury
    • Topsakal C, Erol FS, Ozveren MF, et al. Effects of methylprednisolone and dextromethorphan on lipid peroxidation in an experimental model of spinal cord injury. Neurosurg Rev 2002;25:258-66.
    • (2002) Neurosurg Rev , vol.25 , pp. 258-266
    • Topsakal, C.1    Erol, F.S.2    Ozveren, M.F.3
  • 24
    • 0036035522 scopus 로고    scopus 로고
    • Medroxyprogesterone acetate, enoxaparin, and pentoxifylline cause alterations in lipid peroxidation, paraoxonase (PON1) activities, and homocysteine levels in the acute oxidative stress in an experimental model of spinal cord injury
    • Topsakal C, Kilic N, Erol FS, et al. Medroxyprogesterone acetate, enoxaparin, and pentoxifylline cause alterations in lipid peroxidation, paraoxonase (PON1) activities, and homocysteine levels in the acute oxidative stress in an experimental model of spinal cord injury. Acta Neurochirurgica (Wien) 2002;144:1021-31.
    • (2002) Acta Neurochirurgica (Wien) , vol.144 , pp. 1021-1031
    • Topsakal, C.1    Kilic, N.2    Erol, F.S.3
  • 25
    • 0024477265 scopus 로고
    • Prostaglandin E1: The endogenous physiological regulator of platelet mediated blood coagulation
    • Dutta-Roy AK, Kahn NN, Sinha AK. Prostaglandin E1: the endogenous physiological regulator of platelet mediated blood coagulation. Prostaglandins Leukot Essent Fatty Acids 1989;35:189-95.
    • (1989) Prostaglandins Leukot Essent Fatty Acids , vol.35 , pp. 189-195
    • Dutta-Roy, A.K.1    Kahn, N.N.2    Sinha, A.K.3
  • 26
    • 0030942790 scopus 로고    scopus 로고
    • Monocyte tissue factor expression, cell activation, and thrombin formation during cardiopulmonary bypass: A clinical study
    • Ernoffson M, Thelin S, Siegbahn A. Monocyte tissue factor expression, cell activation, and thrombin formation during cardiopulmonary bypass: a clinical study. J Thorac Cardiovasc 1997;113:576-84.
    • (1997) J Thorac Cardiovasc , vol.113 , pp. 576-584
    • Ernoffson, M.1    Thelin, S.2    Siegbahn, A.3
  • 27
    • 0025196074 scopus 로고
    • Does prostaglandin E1 and superoxide dismutase prevent ischaemic spinal cord injury after thoracic aortic cross-clamping?
    • Grabitz K, Freye E, Prior R, et al. Does prostaglandin E1 and superoxide dismutase prevent ischaemic spinal cord injury after thoracic aortic cross-clamping? Eur J Vasc Surg 1990;4:19-24.
    • (1990) Eur J Vasc Surg , vol.4 , pp. 19-24
    • Grabitz, K.1    Freye, E.2    Prior, R.3
  • 28
    • 0031754365 scopus 로고    scopus 로고
    • Increased anticoagulation during cardiopulmonary bypass by prostaglandin E1
    • Kozek-Langenecker SA, Wanzel O, Berger R, et al. Increased anticoagulation during cardiopulmonary bypass by prostaglandin E1. Anesth Analg 1998;87:985-8.
    • (1998) Anesth Analg , vol.87 , pp. 985-988
    • Kozek-Langenecker, S.A.1    Wanzel, O.2    Berger, R.3
  • 29
    • 18244426161 scopus 로고    scopus 로고
    • Cell-derived microparticles generated in patients during cardiopulmonary bypass are highly procoagulant
    • Nieuwland R, Berckmans RJ, Rotteveel-Eijkmann RC, et al. Cell-derived microparticles generated in patients during cardiopulmonary bypass are highly procoagulant. Circulation 1997;96:3534-41.
    • (1997) Circulation , vol.96 , pp. 3534-3541
    • Nieuwland, R.1    Berckmans, R.J.2    Rotteveel-Eijkmann, R.C.3
  • 31
    • 0035125953 scopus 로고    scopus 로고
    • Evaluation of spinal cord blood flow during prostaglandin E1-induced hypotension with power doppler ultrasonography
    • Tsuji T, Matsuyama Y, Sato K, et al. Evaluation of spinal cord blood flow during prostaglandin E1-induced hypotension with power doppler ultrasonography. Spinal Cord 2001;39:31-6.
    • (2001) Spinal Cord , vol.39 , pp. 31-36
    • Tsuji, T.1    Matsuyama, Y.2    Sato, K.3
  • 32
    • 0028511448 scopus 로고
    • Inhibitory effect of melatonin on cataract formation in newborn rats: Evidence for an antioxidant role for melatonin
    • Abe M, Reiter RJ, Orhii PB, et al. Inhibitory effect of melatonin on cataract formation in newborn rats: evidence for an antioxidant role for melatonin. J Pinela Res 1994;17:94-100.
    • (1994) J Pinela Res , vol.17 , pp. 94-100
    • Abe, M.1    Reiter, R.J.2    Orhii, P.B.3
  • 33
    • 0029934729 scopus 로고    scopus 로고
    • Neurohormone melatonin prevents cell damage: Effect on gene expression for antioxidant enzymes
    • Antolin I, Rodrigues C, Sainz RM, et al. Neurohormone melatonin prevents cell damage: effect on gene expression for antioxidant enzymes. FASEB J 1996;10:882-90.
    • (1996) FASEB J , vol.10 , pp. 882-890
    • Antolin, I.1    Rodrigues, C.2    Sainz, R.M.3
  • 34
    • 0029032902 scopus 로고
    • Melatonin stimulates brain glutathione peroxidase activity
    • Barlow-Walden L, Reiter RJ, Abe M, et al. Melatonin stimulates brain glutathione peroxidase activity. Neurochem Int 1995;26:497-502.
    • (1995) Neurochem Int , vol.26 , pp. 497-502
    • Barlow-Walden, L.1    Reiter, R.J.2    Abe, M.3
  • 35
    • 0034000083 scopus 로고    scopus 로고
    • Potent protective effects of melatonin on experimental spinal cord injury
    • Fujimoto T, Nakamura T, Ikeda T, et al. Potent protective effects of melatonin on experimental spinal cord injury. Spine 2000;25:769-75.
    • (2000) Spine , vol.25 , pp. 769-775
    • Fujimoto, T.1    Nakamura, T.2    Ikeda, T.3
  • 36
    • 0030733042 scopus 로고    scopus 로고
    • In vitro and in vivo protective effects of melatonin against glutamate oxidative stress and neurotoxicity
    • Giusti P, Lipartiti M, Gusella M, et al. In vitro and in vivo protective effects of melatonin against glutamate oxidative stress and neurotoxicity. Ann NY Acad Sci 1997;825:79-84.
    • (1997) Ann NY Acad Sci , vol.825 , pp. 79-84
    • Giusti, P.1    Lipartiti, M.2    Gusella, M.3
  • 37
    • 0031967974 scopus 로고    scopus 로고
    • Melatonin increases gene expression for antioxidant enzymes in rat brain cortex
    • Kotler M, Rodriguez C, Sainz RM, et al. Melatonin increases gene expression for antioxidant enzymes in rat brain cortex. J Pineal Res 1998;24:83-9.
    • (1998) J Pineal Res , vol.24 , pp. 83-89
    • Kotler, M.1    Rodriguez, C.2    Sainz, R.M.3
  • 38
    • 0035047130 scopus 로고    scopus 로고
    • In vitro melatonin treatment enhances cell-mediated immune function in male prairic voles (Microtus ochrogaster)
    • Kriegsfield LJ, Drazen DL, Nelson RJ. In vitro melatonin treatment enhances cell-mediated immune function in male prairic voles (Microtus ochrogaster). J Pineal Res 2001;30:193-8.
    • (2001) J Pineal Res , vol.30 , pp. 193-198
    • Kriegsfield, L.J.1    Drazen, D.L.2    Nelson, R.J.3
  • 39
    • 0029082155 scopus 로고
    • Melatonin reduces kainate-induced lipid peroxidation in homogenates of different brain regions
    • Melchiori D, Reiter RJ, Sewerynek E, et al. Melatonin reduces kainate-induced lipid peroxidation in homogenates of different brain regions. FASEB J 1995;9:1205-10.
    • (1995) FASEB J , vol.9 , pp. 1205-1210
    • Melchiori, D.1    Reiter, R.J.2    Sewerynek, E.3
  • 40
    • 0031827904 scopus 로고    scopus 로고
    • Protective effect of melatonin in a model of traumatic brain injury in mice
    • Mesenge C, Margaill I, Verrecchia C, et al. Protective effect of melatonin in a model of traumatic brain injury in mice. J Pineal Res 1998;25:41-6.
    • (1998) J Pineal Res , vol.25 , pp. 41-46
    • Mesenge, C.1    Margaill, I.2    Verrecchia, C.3
  • 41
    • 0034997153 scopus 로고    scopus 로고
    • The neuroprotective and antiapoptotic effects of melatonin in cerebellar neurons involve glucocorticoid receptor and p130 signal pathways
    • Persengiev SP. The neuroprotective and antiapoptotic effects of melatonin in cerebellar neurons involve glucocorticoid receptor and p130 signal pathways. J Steroid Biochem Mol Biol 2001;77:151-8.
    • (2001) J Steroid Biochem Mol Biol , vol.77 , pp. 151-158
    • Persengiev, S.P.1
  • 42
    • 0028137186 scopus 로고
    • Melatonin: A peroxyl radical scavenger more effective than vitamin E
    • Pieri C, Marra M, Moroni F, et al. Melatonin: a peroxyl radical scavenger more effective than vitamin E. Life Sci 1994;55:PL271-6.
    • (1994) Life Sci , vol.55
    • Pieri, C.1    Marra, M.2    Moroni, F.3
  • 43
    • 33750889329 scopus 로고    scopus 로고
    • Melatonin improves cerebral circulation security margin in rats
    • Regrigny O, Delagrange P, Scalbert E, et al. Melatonin improves cerebral circulation security margin in rats. Am J Physiol 1998;275:H139-44.
    • (1998) Am J Physiol , vol.275
    • Regrigny, O.1    Delagrange, P.2    Scalbert, E.3
  • 44
    • 0002979059 scopus 로고
    • Melatonin: A potent, endogenous hydroxyl radical scavenger
    • Tan DX, Chen LD, Poeggeler B, et al. Melatonin: a potent, endogenous hydroxyl radical scavenger. Endocr J 1993;1:57-60.
    • (1993) Endocr J , vol.1 , pp. 57-60
    • Tan, D.X.1    Chen, L.D.2    Poeggeler, B.3
  • 45
    • 0033825692 scopus 로고    scopus 로고
    • The effects of melatonin on the antioxidant systems in experimental spinal injury
    • Taskiran D, Tanyalcin T, Sozmen EY, et al. The effects of melatonin on the antioxidant systems in experimental spinal injury. Int J Neurosci 2000;104:63-73.
    • (2000) Int J Neurosci , vol.104 , pp. 63-73
    • Taskiran, D.1    Tanyalcin, T.2    Sozmen, E.Y.3
  • 46
    • 0028278413 scopus 로고
    • Reduction of central nervous system reperfusion injury in rabbits using doxycycline treatment
    • Clark WM, Calcagno FA, Gabler WL, et al. Reduction of central nervous system reperfusion injury in rabbits using doxycycline treatment. Stroke 1994;25:1411-6.
    • (1994) Stroke , vol.25 , pp. 1411-1416
    • Clark, W.M.1    Calcagno, F.A.2    Gabler, W.L.3
  • 47
    • 0026018690 scopus 로고
    • Suppression of human neutrophil functions by tetracyclines
    • Gabler WL, Creamer HR. Suppression of human neutrophil functions by tetracyclines. J Periodontal Res 1991;26:52-8.
    • (1991) J Periodontal Res , vol.26 , pp. 52-58
    • Gabler, W.L.1    Creamer, H.R.2
  • 48
    • 0027942457 scopus 로고
    • In vivo inhibition of human neutrophil collagenase (MMP-8) activity during long-term combination therapy of doxycycline and non-steroidal anti-inflammatory drugs (NSAID) in acute reactive arthritis
    • Lauhio A, Salo T, Ding Y, et al. In vivo inhibition of human neutrophil collagenase (MMP-8) activity during long-term combination therapy of doxycycline and non-steroidal anti-inflammatory drugs (NSAID) in acute reactive arthritis. Clin Exp Immunol 1994;98:21-8.
    • (1994) Clin Exp Immunol , vol.98 , pp. 21-28
    • Lauhio, A.1    Salo, T.2    Ding, Y.3
  • 49
    • 0027968777 scopus 로고
    • Role of cell adhesion molecules in brain injury after transient middle cerebral artery occlusion in the rat
    • Matsuo Y, Onodera H, Shiga Y, et al. Role of cell adhesion molecules in brain injury after transient middle cerebral artery occlusion in the rat. Brain Res 1994;656:344-52.
    • (1994) Brain Res , vol.656 , pp. 344-352
    • Matsuo, Y.1    Onodera, H.2    Shiga, Y.3
  • 50
    • 0030863566 scopus 로고    scopus 로고
    • Doxycycline reduces early neurologic impairment after cerebral arterial air embolism in the rabbit
    • Reasoner DK, Hindman BJ, Dexter F, et al. Doxycycline reduces early neurologic impairment after cerebral arterial air embolism in the rabbit. Anesthesiology 1997;87:569-76.
    • (1997) Anesthesiology , vol.87 , pp. 569-576
    • Reasoner, D.K.1    Hindman, B.J.2    Dexter, F.3
  • 51
    • 0020348156 scopus 로고
    • Effect of tetracycline antibiotics on lipid peroxidation
    • Skakun NP, Vysotskii II. Effect of tetracycline antibiotics on lipid peroxidation. Antibiotiki 1982;27:684-7.
    • (1982) Antibiotiki , vol.27 , pp. 684-687
    • Skakun, N.P.1    Vysotskii, I.I.2
  • 52
    • 0041724984 scopus 로고    scopus 로고
    • Axis Biochemicals ASA. Enzymatic Assay for Homocysteine and a Kit Therefor. EP 623174/US5631127
    • Sundrehagen E. Axis Biochemicals ASA. Enzymatic Assay for Homocysteine and a Kit Therefor. EP 623174/US5631127.
    • Sundrehagen, E.1
  • 53
    • 0035876916 scopus 로고    scopus 로고
    • Minocycline provides neuroprotection against n-methyl-d-aspartate neurotoxicity by inhibiting microglia
    • Tikka TM, Koistinaho JE. Minocycline provides neuroprotection against n-methyl-d-aspartate neurotoxicity by inhibiting microglia. J Immunol 2001;16:7527-33.
    • (2001) J Immunol , vol.16 , pp. 7527-7533
    • Tikka, T.M.1    Koistinaho, J.E.2
  • 55
    • 0017992470 scopus 로고
    • Effect of duration of acute spinal cord compression in a new acute cord injury model in the rat
    • Rivlin AS, Tator CH. Effect of duration of acute spinal cord compression in a new acute cord injury model in the rat. Surg Neurol 1978;10:39-43.
    • (1978) Surg Neurol , vol.10 , pp. 39-43
    • Rivlin, A.S.1    Tator, C.H.2
  • 56
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H, Ohishi N, Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 1979;95:351-8.
    • (1979) Anal Biochem , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 57
    • 0018079943 scopus 로고
    • Serum lipoperoxides in cerebrovascular disorders determined by colorimetric method
    • Satoh K. Serum lipoperoxides in cerebrovascular disorders determined by colorimetric method. Clin Chim Acta 1978;90:37-43.
    • (1978) Clin Chim Acta , vol.90 , pp. 37-43
    • Satoh, K.1
  • 58
    • 0000888890 scopus 로고
    • Assay for plasma lipid peroxides
    • Yagi K. Assay for plasma lipid peroxides. Methods Enzymol 1984;109:328-31.
    • (1984) Methods Enzymol , vol.109 , pp. 328-331
    • Yagi, K.1
  • 59
    • 0002804061 scopus 로고    scopus 로고
    • Biochemical aspect of hematology
    • Burtis CA, Ashwood ER, eds. Philadelphia, PA: Saunders
    • Fairbanks VF, Klee GG. Biochemical aspect of hematology. In: Burtis CA, Ashwood ER, eds. Tietz Textbook of Clinical Chemistry. 3rd ed. Philadelphia, PA: Saunders; 1999:1642-710.
    • (1999) Tietz Textbook of Clinical Chemistry. 3rd Ed. , pp. 1642-1710
    • Fairbanks, V.F.1    Klee, G.G.2
  • 60
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • Paglia DE, Valentine WN. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 1967;70:158-68.
    • (1967) J Lab Clin Med , vol.70 , pp. 158-168
    • Paglia, D.E.1    Valentine, W.N.2
  • 61
    • 0020534463 scopus 로고
    • The human serum paraoxonase polymorphism: Identification of phenotypes by their response to salts
    • Eckerson HW, Romson J, Wyte C, et al. The human serum paraoxonase polymorphism: identification of phenotypes by their response to salts. Am J Hum Genet 1983;35:214-27.
    • (1983) Am J Hum Genet , vol.35 , pp. 214-227
    • Eckerson, H.W.1    Romson, J.2    Wyte, C.3
  • 62
    • 0031886747 scopus 로고    scopus 로고
    • An enzyme conversion immunoassay for determining total homocysteine in plasma of serum
    • Frantzen F, Faaren AL, Alfheim I, et al. An enzyme conversion immunoassay for determining total homocysteine in plasma of serum. Clin Chem 1998;44:311-6.
    • (1998) Clin Chem , vol.44 , pp. 311-316
    • Frantzen, F.1    Faaren, A.L.2    Alfheim, I.3
  • 63
    • 0033139846 scopus 로고    scopus 로고
    • Homocysteine, platelet function and thrombosis
    • Di Monno G, Coppola A, Mancini FP, et al. Homocysteine, platelet function and thrombosis. Haematologica 1999;84:61-3.
    • (1999) Haematologica , vol.84 , pp. 61-63
    • Di Monno, G.1    Coppola, A.2    Mancini, F.P.3
  • 64
    • 0029891753 scopus 로고    scopus 로고
    • Effect of homocysteine on copper ion-catalyzed, azo compound-initiated, and mononuclear cell-mediated oxidative modification of low density lipoprotein
    • Halvorsen B, Brude I, Drevon CA, et al. Effect of homocysteine on copper ion-catalyzed, azo compound-initiated, and mononuclear cell-mediated oxidative modification of low density lipoprotein. J Lipid Res 1996;37:1591-600.
    • (1996) J Lipid Res , vol.37 , pp. 1591-1600
    • Halvorsen, B.1    Brude, I.2    Drevon, C.A.3
  • 65
    • 0031757519 scopus 로고    scopus 로고
    • LDL oxidation by arterial wall macrophages depends on the oxidative status in the lipoprotein and in the cells: Role of pro-oxidants vs. antioxidants
    • Aviram M, Fuhrman B. LDL oxidation by arterial wall macrophages depends on the oxidative status in the lipoprotein and in the cells: role of pro-oxidants vs. antioxidants. Mol Cell Biochem 1998;188:149-59.
    • (1998) Mol Cell Biochem , vol.188 , pp. 149-159
    • Aviram, M.1    Fuhrman, B.2
  • 66
    • 0035009789 scopus 로고    scopus 로고
    • Lipid peroxidation is increased in paraoxonase 155 homozygotes compared with m-allele carriers
    • Malin R, Laine S, Rantalaiho V, et al. Lipid peroxidation is increased in paraoxonase 155 homozygotes compared with m-allele carriers. Free Radic Res 2001;34:477-84.
    • (2001) Free Radic Res , vol.34 , pp. 477-484
    • Malin, R.1    Laine, S.2    Rantalaiho, V.3
  • 67
    • 0035936847 scopus 로고    scopus 로고
    • Genetic determinants of homocysteine thiolactonase activity in humans: Implications for atherosclerosis
    • Jakubowski H, Ambrosius WT, Pratt JH. Genetic determinants of homocysteine thiolactonase activity in humans: implications for atherosclerosis. FEBS Lett 2001;492:35-9.
    • (2001) FEBS Lett , vol.492 , pp. 35-39
    • Jakubowski, H.1    Ambrosius, W.T.2    Pratt, J.H.3
  • 68
    • 0034635449 scopus 로고    scopus 로고
    • Calcium-dependent human serum homocysteine thiolactone hydrolase
    • Jakubowski H. Calcium-dependent human serum homocysteine thiolactone hydrolase. J Biol Chem 2000;11:3957-62.
    • (2000) J Biol Chem , vol.11 , pp. 3957-3962
    • Jakubowski, H.1
  • 69
    • 0344613971 scopus 로고    scopus 로고
    • Catalase and paraoxonase in hypertensive type 2 diabetes mellitus: Correlation with glycemic control
    • Sozmen B, Delen Y, Girgin FK, et al. Catalase and paraoxonase in hypertensive type 2 diabetes mellitus: correlation with glycemic control. Clin Biochem 1999;32:423-7.
    • (1999) Clin Biochem , vol.32 , pp. 423-427
    • Sozmen, B.1    Delen, Y.2    Girgin, F.K.3
  • 71
    • 0031670596 scopus 로고    scopus 로고
    • The serum paraoxonase activity in patients with chronic renal failure and hyperlipidemia
    • Paragh G, Seres I, Balogh Z, et al. The serum paraoxonase activity in patients with chronic renal failure and hyperlipidemia. Nephron 1998;80:166-70.
    • (1998) Nephron , vol.80 , pp. 166-170
    • Paragh, G.1    Seres, I.2    Balogh, Z.3
  • 72
    • 0033941426 scopus 로고    scopus 로고
    • MRI cerebral white matter lesions and paraoxonase PON1 polymorphism. Three-year follow-up of the Austrian Stroke prevention study
    • Schmidt R, Scmidt H, Fazekas F, et al. MRI cerebral white matter lesions and paraoxonase PON1 polymorphism. Three-year follow-up of the Austrian Stroke prevention study. Arterioscler Tromb Vasc Biol 2000;20:1811-6.
    • (2000) Arterioscler Tromb Vasc Biol , vol.20 , pp. 1811-1816
    • Schmidt, R.1    Scmidt, H.2    Fazekas, F.3
  • 73
    • 0034051557 scopus 로고    scopus 로고
    • Genetic and temporal determinants of pesticide sensitivity: Role of paraoxonase (PON1)
    • Furlong CE, Li W-F, Shih DM, et al. Genetic and temporal determinants of pesticide sensitivity: role of paraoxonase (PON1). Neurotoxicology 2000;21:91-100.
    • (2000) Neurotoxicology , vol.21 , pp. 91-100
    • Furlong, C.E.1    Li, W.-F.2    Shih, D.M.3
  • 74
    • 0035852877 scopus 로고    scopus 로고
    • Cysteine substitution in apolipoprotein A-1 primary structure modulate paraoxonase activity
    • Oda MN, Bielicki JK, Berger T, et al. Cysteine substitution in apolipoprotein A-1 primary structure modulate paraoxonase activity. Biochemistry 2001;40:1710-8.
    • (2001) Biochemistry , vol.40 , pp. 1710-1718
    • Oda, M.N.1    Bielicki, J.K.2    Berger, T.3
  • 75
    • 0033803134 scopus 로고    scopus 로고
    • Dietary far modulates serum paraoxonase 1 activity in rats
    • Kudchodkar BJ, Lacko AG, Dory L, et al. Dietary far modulates serum paraoxonase 1 activity in rats. J Nutr 2000;130:2427-33.
    • (2000) J Nutr , vol.130 , pp. 2427-2433
    • Kudchodkar, B.J.1    Lacko, A.G.2    Dory, L.3
  • 76
    • 0033011245 scopus 로고    scopus 로고
    • Increased plasma levels of homocysteine and other thiol compounds in rheumatoid arthritis women
    • Hernanz A, Plaza A, Martin-Mola E, et al. Increased plasma levels of homocysteine and other thiol compounds in rheumatoid arthritis women. Clin Biochem 1999;32:65-70.
    • (1999) Clin Biochem , vol.32 , pp. 65-70
    • Hernanz, A.1    Plaza, A.2    Martin-Mola, E.3
  • 77
    • 0026729430 scopus 로고
    • Hyperhomocystinemia as a risk factor for stroke
    • Brattstrom I, Lindgren A. Hyperhomocystinemia as a risk factor for stroke [review]. Neurol Res 1992;14(suppl 2):81-4.
    • (1992) Neurol Res , vol.14 , Issue.SUPPL. 2 , pp. 81-84
    • Brattstrom, I.1    Lindgren, A.2
  • 78
    • 0028229392 scopus 로고    scopus 로고
    • Elevated serum homocysteine as a predictor for vitamin B12 or folate deficiency
    • 194
    • Curtis D, Sparow R, Brennan L, et al. Elevated serum homocysteine as a predictor for vitamin B12 or folate deficiency. Eur J Haematol 194;52:227-32.
    • Eur J Haematol , vol.52 , pp. 227-232
    • Curtis, D.1    Sparow, R.2    Brennan, L.3
  • 79
    • 0035002032 scopus 로고    scopus 로고
    • Total homocysteine, vitamin B(12), and total antioxidant status in vegetarians
    • Hermann W, Schorr H, Purschwitz K, et al. Total homocysteine, vitamin B(12), and total antioxidant status in vegetarians. Clin Chem 2001;47:1094-101.
    • (2001) Clin Chem , vol.47 , pp. 1094-1101
    • Hermann, W.1    Schorr, H.2    Purschwitz, K.3
  • 80
    • 0028284362 scopus 로고
    • Rapid HPLC determination of total homocysteine and other thiols in serum and plasma: Sex differences and correlation with cobalamin and folate concentrations in healthy subjects
    • Jacobsen DW, Gatautis VJ, Green R, et al. Rapid HPLC determination of total homocysteine and other thiols in serum and plasma: sex differences and correlation with cobalamin and folate concentrations in healthy subjects. Clin Chem 1994;40:873-81.
    • (1994) Clin Chem , vol.40 , pp. 873-881
    • Jacobsen, D.W.1    Gatautis, V.J.2    Green, R.3
  • 81
    • 0029827897 scopus 로고    scopus 로고
    • Hyperhomocystinemia - A common finding in a psychogeriatric population
    • Nilsson K, Gustafson L, Faldt R, et al. Hyperhomocystinemia - a common finding in a psychogeriatric population. Eur J Clin Invest 1996;26:853-9.
    • (1996) Eur J Clin Invest , vol.26 , pp. 853-859
    • Nilsson, K.1    Gustafson, L.2    Faldt, R.3
  • 82
    • 0034620573 scopus 로고    scopus 로고
    • Effects of methionine-induced hyperhomocystinemia on endothelium-dependent vasodilatation and oxidative status in healthy adults
    • Chao CL, Kuo TL, Lee YT. Effects of methionine-induced hyperhomocystinemia on endothelium-dependent vasodilatation and oxidative status in healthy adults. Circulation 2000;101:485-90.
    • (2000) Circulation , vol.101 , pp. 485-490
    • Chao, C.L.1    Kuo, T.L.2    Lee, Y.T.3
  • 83
    • 0035122294 scopus 로고    scopus 로고
    • Homocysteine, oxidative stress, and endothelium function in uremic patients
    • Massy ZA, Ceballos I, Chadefaux-Vekemens B, et al. Homocysteine, oxidative stress, and endothelium function in uremic patients. Kidney Int Supp 2001;78:S243-5.
    • (2001) Kidney Int Supp , vol.78
    • Massy, Z.A.1    Ceballos, I.2    Chadefaux-Vekemens, B.3
  • 84
    • 0027092328 scopus 로고
    • Endothelium-derived relaxing factor modulates the atherothrombogenic effects of homocysteine
    • Stamler JS, Loscalzo J. Endothelium-derived relaxing factor modulates the atherothrombogenic effects of homocysteine. J Cardiovasc Pharm 1992;20: S202-4.
    • (1992) J Cardiovasc Pharm , vol.20
    • Stamler, J.S.1    Loscalzo, J.2
  • 85
    • 0022472013 scopus 로고
    • Activation of endogenous factor V by a homocysteine-induced vascular endothelial cell activator
    • Rodgers GM, Kane WH. Activation of endogenous factor V by a homocysteine-induced vascular endothelial cell activator. J Clin Invest 1986;77:1909-16.
    • (1986) J Clin Invest , vol.77 , pp. 1909-1916
    • Rodgers, G.M.1    Kane, W.H.2
  • 86
    • 0000167774 scopus 로고
    • Disorders of transulphuration
    • Scriver CR, Beaudet AL, Sly WS, et al, eds. New York, NY: McGraw-Hill
    • Mudd SH, Levy HL, Skovby F. Disorders of transulphuration. In: Scriver CR, Beaudet AL, Sly WS, et al, eds. Metabolic Basis of Inherited Disease. 7th ed. New York, NY: McGraw-Hill; 1995:1279-327.
    • (1995) Metabolic Basis of Inherited Disease. 7th Ed. , pp. 1279-1327
    • Mudd, S.H.1    Levy, H.L.2    Skovby, F.3
  • 87
    • 0028292931 scopus 로고
    • Sulfhydryl compounds influence immunoreactivity, structure and functional aspect of lipoprotein (a)
    • Bas Leerink C, van Ham DFJ, Heeres A, et al. Sulfhydryl compounds influence immunoreactivity, structure and functional aspect of lipoprotein (a). Thromb Res 1994;74:219-32.
    • (1994) Thromb Res , vol.74 , pp. 219-232
    • Bas Leerink, C.1    Van Ham, D.F.J.2    Heeres, A.3
  • 88
    • 0026486960 scopus 로고
    • Homocysteine and other sulfhydryl compounds enhance the bonding of lipoprotein (a) to fibrin: A potential biochemical link between thrombosis, atherogenesis, and sulfhydryl compound metabolism
    • Harpel PC, Chang VT, Borth W. Homocysteine and other sulfhydryl compounds enhance the bonding of lipoprotein (a) to fibrin: a potential biochemical link between thrombosis, atherogenesis, and sulfhydryl compound metabolism. Proc Natl Acad Sci USA 1992;89:10193-7.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10193-10197
    • Harpel, P.C.1    Chang, V.T.2    Borth, W.3
  • 89
    • 0028329986 scopus 로고
    • Lipid peroxidation and homocysteine induced toxicity
    • Jones BG, Rose FA, Tudball N. Lipid peroxidation and homocysteine induced toxicity. Atherosclerosis 1994;105:165-70.
    • (1994) Atherosclerosis , vol.105 , pp. 165-170
    • Jones, B.G.1    Rose, F.A.2    Tudball, N.3
  • 90
    • 0031127537 scopus 로고    scopus 로고
    • Physiological thiol compounds exert pro-and antioxidant effects, respectively, on iron-and copper-dependent oxidation of human low-density lipoprotein
    • Lynch SM, Frei B. Physiological thiol compounds exert pro-and antioxidant effects, respectively, on iron-and copper-dependent oxidation of human low-density lipoprotein. Biochem Biophys Acta 1997;1345:215-21.
    • (1997) Biochem Biophys Acta , vol.1345 , pp. 215-221
    • Lynch, S.M.1    Frei, B.2
  • 91
    • 0028113988 scopus 로고
    • Plasma thiols, copper and rheumatoid arthritis
    • Rafter GW. Plasma thiols, copper and rheumatoid arthritis. Med Hypotheses 1994;43:59-61.
    • (1994) Med Hypotheses , vol.43 , pp. 59-61
    • Rafter, G.W.1
  • 92
    • 0034602571 scopus 로고    scopus 로고
    • Oxidative stress and an altered methionine metabolism in alcoholism
    • Bleich S, Spilker K, Kurth C, et al. Oxidative stress and an altered methionine metabolism in alcoholism. Neuroscience Lett 2000;286:171-4.
    • (2000) Neuroscience Lett , vol.286 , pp. 171-174
    • Bleich, S.1    Spilker, K.2    Kurth, C.3
  • 93
    • 0030915272 scopus 로고    scopus 로고
    • Neurotoxicity associated with dual actions of homocysteine at the N-methyl-D-aspartate receptor
    • Lipton SA, Kim W-K, Choi Y-B, et al. Neurotoxicity associated with dual actions of homocysteine at the N-methyl-D-aspartate receptor. Proc Natl Acad Sci USA 1997;94:5923-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5923-5928
    • Lipton, S.A.1    Kim, W.-K.2    Choi, Y.-B.3
  • 94
    • 0035093878 scopus 로고    scopus 로고
    • Homocysteine potentiates copper- and amyloid beta peptide-mediated toxicity in primary neuronal cultures: Possible risk factors in the Alzheimer's type neurodegenerative pathways
    • White AR, Huang X, Jobling MF, et al. Homocysteine potentiates copper- and amyloid beta peptide-mediated toxicity in primary neuronal cultures: possible risk factors in the Alzheimer's type neurodegenerative pathways. J Neurochem 2001;76:1509-20.
    • (2001) J Neurochem , vol.76 , pp. 1509-1520
    • White, A.R.1    Huang, X.2    Jobling, M.F.3
  • 95
    • 0035929641 scopus 로고    scopus 로고
    • Homocysteine induces programmed cell death in human vascular endothelial cells through activation of the unfolded protein response
    • Zhang C, Cai Y, Adachi MT, et al. Homocysteine induces programmed cell death in human vascular endothelial cells through activation of the unfolded protein response. J Biol Chem 2001;276:35867-74.
    • (2001) J Biol Chem , vol.276 , pp. 35867-35874
    • Zhang, C.1    Cai, Y.2    Adachi, M.T.3
  • 96
    • 0033855267 scopus 로고    scopus 로고
    • Oxidative stress in the context of acute cerebrovascular stoke
    • El Kossi M, Zakhary MM. Oxidative stress in the context of acute cerebrovascular stoke. Stroke 2000;31:1889-92.
    • (2000) Stroke , vol.31 , pp. 1889-1892
    • El Kossi, M.1    Zakhary, M.M.2
  • 97
    • 0029918732 scopus 로고    scopus 로고
    • Genetic-dietary regulation of serum paraoxonase expression and its role in atherogenesis in a mouse model
    • Shih DM, Gu L, Hama S, et al. Genetic-dietary regulation of serum paraoxonase expression and its role in atherogenesis in a mouse model. J Clin Invest 1996;97:1630-9.
    • (1996) J Clin Invest , vol.97 , pp. 1630-1639
    • Shih, D.M.1    Gu, L.2    Hama, S.3
  • 98
    • 0030783147 scopus 로고    scopus 로고
    • Homocysteine as a modulator of platelet-derived growth factor action in vascular smooth muscle cells: A possible role for hydrogen peroxide
    • Nishio E, Watanebe Y. Homocysteine as a modulator of platelet-derived growth factor action in vascular smooth muscle cells: a possible role for hydrogen peroxide. Br J Pharmacol 1997;122:269-74.
    • (1997) Br J Pharmacol , vol.122 , pp. 269-274
    • Nishio, E.1    Watanebe, Y.2
  • 99
    • 0032524586 scopus 로고    scopus 로고
    • Characterization of the stress-inducing effects of homocysteine
    • Outinen PA, Sood SK, Liaw PC, et al. Characterization of the stress-inducing effects of homocysteine. Biochem J 1998;332:213-21.
    • (1998) Biochem J , vol.332 , pp. 213-221
    • Outinen, P.A.1    Sood, S.K.2    Liaw, P.C.3
  • 100
    • 0034624251 scopus 로고    scopus 로고
    • Effects of homocysteine on the binding of extracellular-superoxide dismutase to the endothelial cell surface
    • Yamamoto M, Hara H, Adachi T. Effects of homocysteine on the binding of extracellular-superoxide dismutase to the endothelial cell surface. FEBS Lett 2000;486:159-62.
    • (2000) FEBS Lett , vol.486 , pp. 159-162
    • Yamamoto, M.1    Hara, H.2    Adachi, T.3
  • 101
    • 0026322413 scopus 로고
    • Biological variability of superoxide dismutase, glutathione peroxidase, and catalase in blood
    • Guemori L, Arthur Y, Herbeth B, et al. Biological variability of superoxide dismutase, glutathione peroxidase, and catalase in blood. Clin Chem 1991;37:1932-7.
    • (1991) Clin Chem , vol.37 , pp. 1932-1937
    • Guemori, L.1    Arthur, Y.2    Herbeth, B.3
  • 102
    • 0033957291 scopus 로고    scopus 로고
    • Elevated plasma homocysteine elicits an increase in antioxidant enzyme activity
    • Moat SJ, Bonham JR, Cragg RA, et al. Elevated plasma homocysteine elicits an increase in antioxidant enzyme activity. Free Radic Res 2000;32:171-9.
    • (2000) Free Radic Res , vol.32 , pp. 171-179
    • Moat, S.J.1    Bonham, J.R.2    Cragg, R.A.3
  • 103
    • 0343569885 scopus 로고    scopus 로고
    • Relationship between homocysteine and superoxide dismutase in homocystinuria: Possible relevance to cardiovascular risk
    • Wilcken DEL, Wang XL, Adachi T, et al. Relationship between homocysteine and superoxide dismutase in homocystinuria: possible relevance to cardiovascular risk. Arterioscler Thromb Vasc Biol 2000;20:1199-202.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 1199-1202
    • Wilcken, D.E.L.1    Wang, X.L.2    Adachi, T.3
  • 104
    • 0030188563 scopus 로고    scopus 로고
    • The oxidant stress of hyperhomocysteinemia
    • Loscalzo J. The oxidant stress of hyperhomocysteinemia. J Clin Invest 1996;98:5-7.
    • (1996) J Clin Invest , vol.98 , pp. 5-7
    • Loscalzo, J.1
  • 105
    • 0034983585 scopus 로고    scopus 로고
    • Anticarcinogenic actions of melatonin which involve antioxidative processes: Comparison with other antioxidants
    • Karbownik M, Lewinski A, Reiter RJ. Anticarcinogenic actions of melatonin which involve antioxidative processes: comparison with other antioxidants. Int J Biochem Cell Biol 2001;33:735-53.
    • (2001) Int J Biochem Cell Biol , vol.33 , pp. 735-753
    • Karbownik, M.1    Lewinski, A.2    Reiter, R.J.3
  • 106
    • 0033509001 scopus 로고    scopus 로고
    • Pinealectomy aggravates and melatonin administration attenuates brain damage in focal brain ischemia
    • Kilic E, Ozdemir YG, Bolay H, et al. Pinealectomy aggravates and melatonin administration attenuates brain damage in focal brain ischemia. J Cereb Blood Flow Metab 1999;19:511-6.
    • (1999) J Cereb Blood Flow Metab , vol.19 , pp. 511-516
    • Kilic, E.1    Ozdemir, Y.G.2    Bolay, H.3
  • 107
    • 0030730368 scopus 로고    scopus 로고
    • Prophylactic actions of melatonin in oxidative neurotoxicity
    • Reiter RJ, Guerrero JM, Escames G, et al. Prophylactic actions of melatonin in oxidative neurotoxicity. Ann NY Acad Sci 1997;825:70-8.
    • (1997) Ann NY Acad Sci , vol.825 , pp. 70-78
    • Reiter, R.J.1    Guerrero, J.M.2    Escames, G.3
  • 108
    • 0034805552 scopus 로고    scopus 로고
    • Melatonin counteracts potentiation by homocysteine of KCL-induced vasoconstriction in human umbilical artery: Relation to calcium influx
    • Okatani Y, Wakatsuki A, Reiter RJ. Melatonin counteracts potentiation by homocysteine of KCL-induced vasoconstriction in human umbilical artery: relation to calcium influx. Biochem Biophys Res 2001;280:940-4.
    • (2001) Biochem Biophys Res , vol.280 , pp. 940-944
    • Okatani, Y.1    Wakatsuki, A.2    Reiter, R.J.3
  • 109
    • 0030031399 scopus 로고    scopus 로고
    • Loss of high-affinity prostacyclin receptors in platelets and the lack of prostaglandin-induced inhibition of platelet-stimulated thrombin generation in subjects with spinal cord injury
    • Kahn NN, Bauman WA, Sinha AK. Loss of high-affinity prostacyclin receptors in platelets and the lack of prostaglandin-induced inhibition of platelet-stimulated thrombin generation in subjects with spinal cord injury. Proc Natl Acad Sci USA 1996;93:245-9.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 245-249
    • Kahn, N.N.1    Bauman, W.A.2    Sinha, A.K.3


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