메뉴 건너뛰기




Volumn 49, Issue 1, 2011, Pages 305-308

Inhibition of hepatic δ-aminolevulinate dehydratase activity induced by mercuric chloride is potentiated by N-acetylcysteine in vitro

Author keywords

Aminolevulinate dehydratase; Lipid peroxidation; Mercury; N acetylcysteine

Indexed keywords

ACETYLCYSTEINE; MERCURIC CHLORIDE; PORPHOBILINOGEN SYNTHASE; THIOBARBITURIC ACID REACTIVE SUBSTANCE; THIOL GROUP;

EID: 78650278965     PISSN: 02786915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fct.2010.10.033     Document Type: Article
Times cited : (5)

References (33)
  • 1
    • 0024394697 scopus 로고
    • The antioxidant action of N-acetylcysteine: its reaction with hydrogen peroxide, hydroxyl radical, superoxide and hypochlorous acid
    • Aruoma O.I., Halliwell B., Hoey B.M., Butler J. The antioxidant action of N-acetylcysteine: its reaction with hydrogen peroxide, hydroxyl radical, superoxide and hypochlorous acid. Free Radic. Biol. Med. 1989, 6:593-597.
    • (1989) Free Radic. Biol. Med. , vol.6 , pp. 593-597
    • Aruoma, O.I.1    Halliwell, B.2    Hoey, B.M.3    Butler, J.4
  • 2
    • 0022577007 scopus 로고
    • Experimental chelation therapy in chromium, lead and boron intoxication with N-acetylcysteine and other compounds
    • Banner W.J.R., Koch M., Capin D.M., Hopf S.B., Chang S., Tong T.G. Experimental chelation therapy in chromium, lead and boron intoxication with N-acetylcysteine and other compounds. Toxicol. Appl. Pharmacol. 1986, 83:142-147.
    • (1986) Toxicol. Appl. Pharmacol. , vol.83 , pp. 142-147
    • Banner, W.J.R.1    Koch, M.2    Capin, D.M.3    Hopf, S.B.4    Chang, S.5    Tong, T.G.6
  • 3
    • 84984558818 scopus 로고    scopus 로고
    • Effect of organic forms of selenium on δ-aminolevulinate dehydratase from liver, kidney and brain of adults rats
    • Barbosa N.B.V., Rocha J.B.T., Zeni G., Emanuelli T., Beque M.C., Braga A.L. Effect of organic forms of selenium on δ-aminolevulinate dehydratase from liver, kidney and brain of adults rats. Toxicol. Appl. Pharmacol. 1998, 149:243-253.
    • (1998) Toxicol. Appl. Pharmacol. , vol.149 , pp. 243-253
    • Barbosa, N.B.V.1    Rocha, J.B.T.2    Zeni, G.3    Emanuelli, T.4    Beque, M.C.5    Braga, A.L.6
  • 4
    • 0030016990 scopus 로고    scopus 로고
    • Oxidative stress in acute intermittent porphiria and lead poisoning may be triggered by 5- aminolevulinic acid
    • Bechara E.J. Oxidative stress in acute intermittent porphiria and lead poisoning may be triggered by 5- aminolevulinic acid. Braz. J. Med. Biol. Res. 1996, 29:841-851.
    • (1996) Braz. J. Med. Biol. Res. , vol.29 , pp. 841-851
    • Bechara, E.J.1
  • 5
    • 0025016146 scopus 로고
    • Thiol antidotes effect on lipid peroxidation in mercury-poisoned rats
    • Benov L.C., Benchev I.C., Monovich O.H. Thiol antidotes effect on lipid peroxidation in mercury-poisoned rats. Chem. Biol. Interact. 1990, 76:321.
    • (1990) Chem. Biol. Interact. , vol.76 , pp. 321
    • Benov, L.C.1    Benchev, I.C.2    Monovich, O.H.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 84984588507 scopus 로고    scopus 로고
    • DMPS and N-acetylcysteine induced renal toxicity in mice exposed to mercury
    • Brandão R., Santos F.W., Zeni G., Rocha J.B.T., Nogueira C.W. DMPS and N-acetylcysteine induced renal toxicity in mice exposed to mercury. Biometals 2006, 19:389-398.
    • (2006) Biometals , vol.19 , pp. 389-398
    • Brandão, R.1    Santos, F.W.2    Zeni, G.3    Rocha, J.B.T.4    Nogueira, C.W.5
  • 9
    • 0029885005 scopus 로고    scopus 로고
    • Inhibition of ATPase activity in rat synaptic plasma membranes by simultaneous exposure to metals
    • Carfagna M.A., Ponsler G.D., Muhoberac B.B. Inhibition of ATPase activity in rat synaptic plasma membranes by simultaneous exposure to metals. Chem. Biol. Interact. 1996, 100:53-65.
    • (1996) Chem. Biol. Interact. , vol.100 , pp. 53-65
    • Carfagna, M.A.1    Ponsler, G.D.2    Muhoberac, B.B.3
  • 11
    • 0028178456 scopus 로고
    • Activity of erythrocyte δ-aminolevulinic acid dehydratase in the female cynomolgus monkey (Macaca fascicularis): kinetic analysis in control and lead-exposed animals
    • Dorward A., Yagminas A.P. Activity of erythrocyte δ-aminolevulinic acid dehydratase in the female cynomolgus monkey (Macaca fascicularis): kinetic analysis in control and lead-exposed animals. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 1994, 108:241-252.
    • (1994) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.108 , pp. 241-252
    • Dorward, A.1    Yagminas, A.P.2
  • 12
    • 84984578359 scopus 로고    scopus 로고
    • Effect of mercury chloride intoxication and dimercaprol treatment on delta-aminolevulinate dehydratase from brain, liver and kidney of adult mice
    • Emanuelli T., Rocha J.B.T., Pereira M.E., Porciúncula L.O., Morsch V.M., Martins A.F., Souza D.O.G. Effect of mercury chloride intoxication and dimercaprol treatment on delta-aminolevulinate dehydratase from brain, liver and kidney of adult mice. Pharmacol. Toxicol. 1996, 79:136-143.
    • (1996) Pharmacol. Toxicol. , vol.79 , pp. 136-143
    • Emanuelli, T.1    Rocha, J.B.T.2    Pereira, M.E.3    Porciúncula, L.O.4    Morsch, V.M.5    Martins, A.F.6    Souza, D.O.G.7
  • 13
    • 84984536095 scopus 로고    scopus 로고
    • Profile of nonprotein thiols, lipid peroxidation and delta-aminolevulinate dehydratase activity in mouse kidney and liver in response to acute exposure to mercuric chloride and sodium selenite
    • Farina M., Brandão R., Lara F.S., Soares F.A.A., Souza D.O., Rocha J.B.T. Profile of nonprotein thiols, lipid peroxidation and delta-aminolevulinate dehydratase activity in mouse kidney and liver in response to acute exposure to mercuric chloride and sodium selenite. Toxicology 2003, 184:179-187.
    • (2003) Toxicology , vol.184 , pp. 179-187
    • Farina, M.1    Brandão, R.2    Lara, F.S.3    Soares, F.A.A.4    Souza, D.O.5    Rocha, J.B.T.6
  • 14
    • 84984537253 scopus 로고    scopus 로고
    • High sucrose consumption potentiates the sub-acute cadmium effect on Na+-K+-ATPase but not on and δ-aminolevulinate dehydratase in mice
    • Folmer V., Santos F.W., Savegnago L., Brito V.B., Nogueira C.W., Rocha J.B.T. High sucrose consumption potentiates the sub-acute cadmium effect on Na+-K+-ATPase but not on and δ-aminolevulinate dehydratase in mice. Toxicol Lett. 2004, 153:333-341.
    • (2004) Toxicol Lett. , vol.153 , pp. 333-341
    • Folmer, V.1    Santos, F.W.2    Savegnago, L.3    Brito, V.B.4    Nogueira, C.W.5    Rocha, J.B.T.6
  • 15
    • 0025760160 scopus 로고
    • Effectiveness of N-acetylcysteine in protecting against mercuric chloride-induced nephrotoxicity
    • Girardi G., Elias M.M. Effectiveness of N-acetylcysteine in protecting against mercuric chloride-induced nephrotoxicity. Toxicology 1991, 67:155-164.
    • (1991) Toxicology , vol.67 , pp. 155-164
    • Girardi, G.1    Elias, M.M.2
  • 16
    • 0027930460 scopus 로고
    • Mechanisms for the oxygen radical mediated toxicity of various thiol-containing compounds in cultured mammalian cells
    • Held K.D., Biaglow J.E. Mechanisms for the oxygen radical mediated toxicity of various thiol-containing compounds in cultured mammalian cells. Radiat. Res. 1994, 139:15-23.
    • (1994) Radiat. Res. , vol.139 , pp. 15-23
    • Held, K.D.1    Biaglow, J.E.2
  • 17
    • 0033000105 scopus 로고    scopus 로고
    • Accumulation of mercury and its effect on antioxidant enzymes in brain, liver and kidneys of mice
    • Hussain S., Atkinson A., Thompson S.J., Khan A.T. Accumulation of mercury and its effect on antioxidant enzymes in brain, liver and kidneys of mice. J. Environ. Sci. Health B 1999, 34:645-660.
    • (1999) J. Environ. Sci. Health B , vol.34 , pp. 645-660
    • Hussain, S.1    Atkinson, A.2    Thompson, S.J.3    Khan, A.T.4
  • 18
    • 0027164227 scopus 로고
    • Studies on Hg(II)-induced H2O2 formation and oxidative stress in vivo and in vitro in rat kidney mitochondria
    • Lund B.O., Miller M.D., Woods J.S. Studies on Hg(II)-induced H2O2 formation and oxidative stress in vivo and in vitro in rat kidney mitochondria. Biochem. Pharmacol. 1993, 45:2017-2024.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 2017-2024
    • Lund, B.O.1    Miller, M.D.2    Woods, J.S.3
  • 19
    • 0027397253 scopus 로고
    • Spatial proximity and sequence localization of the reactive sulfhydryls of porphobilinogen synthase
    • Markham G.D., Myers C.M., Harris K.A., Volin J.R.M., Jaffe E.K. Spatial proximity and sequence localization of the reactive sulfhydryls of porphobilinogen synthase. Prot. Sci. 1993, 2:71-79.
    • (1993) Prot. Sci. , vol.2 , pp. 71-79
    • Markham, G.D.1    Myers, C.M.2    Harris, K.A.3    Volin, J.R.M.4    Jaffe, E.K.5
  • 20
    • 0023029952 scopus 로고
    • Lung protection by a thiol-containing antioxidant: N-acetylcysteine
    • Moldeus P., Cotgreave I.A., Berggren M. Lung protection by a thiol-containing antioxidant: N-acetylcysteine. Respiration 1986, 50:31-42.
    • (1986) Respiration , vol.50 , pp. 31-42
    • Moldeus, P.1    Cotgreave, I.A.2    Berggren, M.3
  • 21
    • 84984563933 scopus 로고    scopus 로고
    • 2, 3-Dimercaptopropane-1-sulfonic acid and meso-2, 3-dimercaptosuccinic acid inhibit δ-aminolevulinate dehydratase from human erythrocytes in vitro
    • Nogueira C.W., Santos F.W., Soares F.A., Rocha J.B.T. 2, 3-Dimercaptopropane-1-sulfonic acid and meso-2, 3-dimercaptosuccinic acid inhibit δ-aminolevulinate dehydratase from human erythrocytes in vitro. Environ. Res. 2004, 94:254-261.
    • (2004) Environ. Res. , vol.94 , pp. 254-261
    • Nogueira, C.W.1    Santos, F.W.2    Soares, F.A.3    Rocha, J.B.T.4
  • 22
    • 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, 95:351-358.
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 23
    • 0032841575 scopus 로고    scopus 로고
    • N-acetylcysteine, a cancer chemopreventive agent, causes oxidative damage to cellular and isolated DNA
    • Okiawa S., Yamada K., Yamashita N., Tada-Oikawa S., Kawanishi S. N-acetylcysteine, a cancer chemopreventive agent, causes oxidative damage to cellular and isolated DNA. Carcinogenesis 1999, 20:1485-1490.
    • (1999) Carcinogenesis , vol.20 , pp. 1485-1490
    • Okiawa, S.1    Yamada, K.2    Yamashita, N.3    Tada-Oikawa, S.4    Kawanishi, S.5
  • 24
    • 0023228762 scopus 로고
    • Differential effect of N-acetylcysteine on excretion of the metals Hg, Cd, Pb and Au
    • Ottenwalder H., Simon P. Differential effect of N-acetylcysteine on excretion of the metals Hg, Cd, Pb and Au. Arch. Toxicol. 1987, 60:401-402.
    • (1987) Arch. Toxicol. , vol.60 , pp. 401-402
    • Ottenwalder, H.1    Simon, P.2
  • 25
    • 0026547563 scopus 로고
    • 5-Aminolevulinic acid-induced alterations of oxidative metabolism in sedentary and exercise-trained rats
    • Pereira B., Curi R., Kokubun E., Bechara E.J. 5-Aminolevulinic acid-induced alterations of oxidative metabolism in sedentary and exercise-trained rats. J. Appl. Physiol. 1992, 72:226-230.
    • (1992) J. Appl. Physiol. , vol.72 , pp. 226-230
    • Pereira, B.1    Curi, R.2    Kokubun, E.3    Bechara, E.J.4
  • 26
  • 28
    • 0029080228 scopus 로고
    • Effects of mercury chloride and lead acetate treatment during the second stage of rapid postnatal brain growth on ALA-D activity in brain, liver, kidney and blood of suckling rats
    • Rocha J.B.T., Pereira M.E., Emanuelli T., Christofari R.S., Souza D.O. Effects of mercury chloride and lead acetate treatment during the second stage of rapid postnatal brain growth on ALA-D activity in brain, liver, kidney and blood of suckling rats. Toxicology 1995, 100:27-37.
    • (1995) Toxicology , vol.100 , pp. 27-37
    • Rocha, J.B.T.1    Pereira, M.E.2    Emanuelli, T.3    Christofari, R.S.4    Souza, D.O.5
  • 29
    • 0020426709 scopus 로고
    • Delta- aminolevulinic acid dehidratase assay
    • Sassa S. Delta- aminolevulinic acid dehidratase assay. Enzyme 1982, 28:133-145.
    • (1982) Enzyme , vol.28 , pp. 133-145
    • Sassa, S.1
  • 30
    • 0001539277 scopus 로고
    • Genetic and chemical influences on heme biosynthesis
    • VSP, Utrecht, A. Kotyk, J. Skoda, V. Paces, V. Kostka (Eds.)
    • Sassa S., Fujita H., Kappas A. Genetic and chemical influences on heme biosynthesis. Highlights of Modern Biochemistry 1989, 329-338. VSP, Utrecht. A. Kotyk, J. Skoda, V. Paces, V. Kostka (Eds.).
    • (1989) Highlights of Modern Biochemistry , pp. 329-338
    • Sassa, S.1    Fujita, H.2    Kappas, A.3
  • 32
    • 0031923777 scopus 로고    scopus 로고
    • Participation of mercuric conjugates of cysteine, homocysteine and N-acetylcysteine in mechanisms involved in the renal tubular uptake of inorganic mercury
    • Zalups R.K., Barfuss D.W. Participation of mercuric conjugates of cysteine, homocysteine and N-acetylcysteine in mechanisms involved in the renal tubular uptake of inorganic mercury. J. Am. Soc. Nephrol. 1998, 9:551-561.
    • (1998) J. Am. Soc. Nephrol. , vol.9 , pp. 551-561
    • Zalups, R.K.1    Barfuss, D.W.2
  • 33
    • 0023007080 scopus 로고
    • N-acetylcysteine: a drug with an interesting past and a fascinating future
    • Ziment I. N-acetylcysteine: a drug with an interesting past and a fascinating future. Respiration 1986, 50:26-30.
    • (1986) Respiration , vol.50 , pp. 26-30
    • Ziment, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.