메뉴 건너뛰기




Volumn 18, Issue 2, 2005, Pages 277-282

Monochloroacetic acid inhibits liver gluconeogenesis by inactivating glyceraldehyde-3-phosphate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; ACONITATE HYDRATASE; CHLOROACETIC ACID; CITRIC ACID; ENOLASE; GLUCOSE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCEROL; ISOCITRIC ACID; LACTIC ACID; PHOSPHOGLYCERATE KINASE; PHOSPHOGLYCERATE MUTASE;

EID: 13844252094     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx0497705     Document Type: Article
Times cited : (19)

References (31)
  • 3
    • 0029049471 scopus 로고
    • Accidental fatal monochloroacetic acid poisoning
    • Rogers, D. R. (1995) Accidental fatal monochloroacetic acid poisoning. Am. J. Forensic Med. Pathol. 16, 115-116.
    • (1995) Am. J. Forensic Med. Pathol. , vol.16 , pp. 115-116
    • Rogers, D.R.1
  • 5
    • 0015172924 scopus 로고
    • Some metabolic aspects of fluoroacetate especially related to fluorocitrate
    • Peters, R. A. (1971) Some metabolic aspects of fluoroacetate especially related to fluorocitrate. Ciba Found. Symp. 2, 55-76.
    • (1971) Ciba Found. Symp. , vol.2 , pp. 55-76
    • Peters, R.A.1
  • 6
    • 0025936333 scopus 로고
    • Fluoroacetate and fluorocitrate: Mechanism of action
    • Clarke, D. D. (1991) Fluoroacetate and fluorocitrate: Mechanism of action. Neurochem. Res. 16, 1055-1058.
    • (1991) Neurochem. Res. , vol.16 , pp. 1055-1058
    • Clarke, D.D.1
  • 8
    • 0026510835 scopus 로고
    • Toxicity of monochloroacetic acid administered by gavage to F344 rats and B6C3F1 mice for up to 13 weeks
    • Bryant, B. J., Jokinen, M. P., Eustis, S. L., Thompson, M. B., and Abdo, K. M. (1992) Toxicity of monochloroacetic acid administered by gavage to F344 rats and B6C3F1 mice for up to 13 weeks. Toxicology 72, 77-87.
    • (1992) Toxicology , vol.72 , pp. 77-87
    • Bryant, B.J.1    Jokinen, M.P.2    Eustis, S.L.3    Thompson, M.B.4    Abdo, K.M.5
  • 9
    • 0017802994 scopus 로고
    • Biochemical and ultrastructural evaluation of isolated rat liver systems perfused with a hemoglobin-free medium
    • Sugano, T., Suda, K., Shimada, M., and Oshino, N. (1978) Biochemical and ultrastructural evaluation of isolated rat liver systems perfused with a hemoglobin-free medium. J. Biochem. 83, 995-1007.
    • (1978) J. Biochem. , vol.83 , pp. 995-1007
    • Sugano, T.1    Suda, K.2    Shimada, M.3    Oshino, N.4
  • 10
    • 0022921896 scopus 로고
    • Anomer specificity of glucose-6-phosphatase and glucokinase
    • Furuya, E., Hotta, K., and Tagawa, K. (1986) Anomer specificity of glucose-6-phosphatase and glucokinase. Biochem. Biophys. Res. Commun. 141, 931-936.
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 931-936
    • Furuya, E.1    Hotta, K.2    Tagawa, K.3
  • 12
    • 0021999777 scopus 로고
    • Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its nonmetabolizable analogues
    • Watanabe, F., Hashimoto, T., and Tagawa, K. (1985) Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its nonmetabolizable analogues. J. Biochem. 97, 1229-1234.
    • (1985) J. Biochem. , vol.97 , pp. 1229-1234
    • Watanabe, F.1    Hashimoto, T.2    Tagawa, K.3
  • 13
    • 0036122112 scopus 로고    scopus 로고
    • Protein kinase and NO-stimulated ADP-ribosyltransferase activities associated with glyceraldehyde-3-phosphate dehydrogenase isolated from human liver
    • Duclos-Vallee, J. C., Capel, F., Mabit, H., and Petit, M. A. (2002) Protein kinase and NO-stimulated ADP-ribosyltransferase activities associated with glyceraldehyde-3-phosphate dehydrogenase isolated from human liver. Hepatol. Res. 22, 65-73.
    • (2002) Hepatol. Res. , vol.22 , pp. 65-73
    • Duclos-Vallee, J.C.1    Capel, F.2    Mabit, H.3    Petit, M.A.4
  • 14
    • 0021815748 scopus 로고
    • Determinants of triad junction reformation: Identification and isolation of an endogenous promotor for junction reformation in skeletal muscle
    • Corbett, A. M., Caswell, A. H., Brandt, N. R., and Brunschwig, J. P. (1985) Determinants of triad junction reformation: Identification and isolation of an endogenous promotor for junction reformation in skeletal muscle. J. Membr. Biol. 86, 267-276.
    • (1985) J. Membr. Biol. , vol.86 , pp. 267-276
    • Corbett, A.M.1    Caswell, A.H.2    Brandt, N.R.3    Brunschwig, J.P.4
  • 15
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 17
    • 0017278671 scopus 로고
    • Studies on phosphoglyceromutase from chicken breast muscle: Number and reactivity of sulfhydryl groups
    • Carne, T. J., McKay, D. J., and Flynn, T. G. (1976) Studies on phosphoglyceromutase from chicken breast muscle: Number and reactivity of sulfhydryl groups. Can. J. Biochem. 54, 307-320.
    • (1976) Can. J. Biochem. , vol.54 , pp. 307-320
    • Carne, T.J.1    McKay, D.J.2    Flynn, T.G.3
  • 18
    • 0017260959 scopus 로고
    • Alkylation of cysteinyl residues of pig heart NAD-specific isocitrate dehydrogenase by iodoacetate
    • Mauck, L., and Colman, R. F. (1976) Alkylation of cysteinyl residues of pig heart NAD-specific isocitrate dehydrogenase by iodoacetate. Biochim. Biophys. Acta 429, 301-315.
    • (1976) Biochim. Biophys. Acta , vol.429 , pp. 301-315
    • Mauck, L.1    Colman, R.F.2
  • 20
    • 0016737733 scopus 로고
    • Nonidentical alkylation sites in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
    • Bode, J., Blumenstein, M., and Raftery, M. A. (1975) Nonidentical alkylation sites in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 14, 1146-1152.
    • (1975) Biochemistry , vol.14 , pp. 1146-1152
    • Bode, J.1    Blumenstein, M.2    Raftery, M.A.3
  • 21
    • 0017200660 scopus 로고
    • Effect of modification of SH-groups in D-glyceraldehyde-3-phosphate dehydrogenase on the properties of enzyme-coenzyme complex
    • Vas, M., and Bartha, F. (1976) Effect of modification of SH-groups in D-glyceraldehyde-3-phosphate dehydrogenase on the properties of enzyme-coenzyme complex. Acta Biochim. Biophys. Acad. Sci. Hung. 11, 95-104.
    • (1976) Acta Biochim. Biophys. Acad. Sci. Hung. , vol.11 , pp. 95-104
    • Vas, M.1    Bartha, F.2
  • 22
    • 0015900920 scopus 로고
    • Differential toxicity of monochloroacetate, monofluoroacetate and monoiodoacetate in rats
    • Hayes, F. D., Short, R. D., and Gibson, J. E. (1973) Differential toxicity of monochloroacetate, monofluoroacetate and monoiodoacetate in rats. Toxicol. Appl. Pharmacol. 26, 93-102.
    • (1973) Toxicol. Appl. Pharmacol. , vol.26 , pp. 93-102
    • Hayes, F.D.1    Short, R.D.2    Gibson, J.E.3
  • 23
    • 0025357939 scopus 로고
    • Toxicokinetics of monochloroacetic acid: A whole-body autoradiography study
    • Bhat, H. K., Ahmed, A. E., and Ansari, G. A. (1990) Toxicokinetics of monochloroacetic acid: A whole-body autoradiography study. Toxicology 63, 35-43.
    • (1990) Toxicology , vol.63 , pp. 35-43
    • Bhat, H.K.1    Ahmed, A.E.2    Ansari, G.A.3
  • 24
    • 0035146490 scopus 로고    scopus 로고
    • Kinetics of monochloroacetic acid in adult male rats after intravenous injection of a subtoxic and a toxic dose
    • Saghir, S. A., Fried, K., and Rozman, K. K. (2001) Kinetics of monochloroacetic acid in adult male rats after intravenous injection of a subtoxic and a toxic dose. J. Pharmacol. Exp. Ther. 296, 612-622.
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 612-622
    • Saghir, S.A.1    Fried, K.2    Rozman, K.K.3
  • 25
    • 0030044996 scopus 로고    scopus 로고
    • The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver cells determined using the fluorescent intracellular pH indicator, 2′,7′-bis(carboxyethyl)-5(6)- carboxyfluorescein
    • Jackson, V. N., and Halestrap, A. P. (1996) The kinetics, substrate, and inhibitor specificity of the monocarboxylate (lactate) transporter of rat liver cells determined using the fluorescent intracellular pH indicator, 2′,7′-bis(carboxyethyl)-5(6)-carboxyfluorescein. J. Biol. Chem. 271, 861-868.
    • (1996) J. Biol. Chem. , vol.271 , pp. 861-868
    • Jackson, V.N.1    Halestrap, A.P.2
  • 26
    • 0033569442 scopus 로고    scopus 로고
    • The proton-linked monocarboxylate transporter (MCT) family. Structure, function and regulation
    • Halestrap, A. P., and Price, N. T. (1999) The proton-linked monocarboxylate transporter (MCT) family. Structure, function and regulation. Biochem. J. 343, 281-299.
    • (1999) Biochem. J. , vol.343 , pp. 281-299
    • Halestrap, A.P.1    Price, N.T.2
  • 27
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover, M. A. (1999) New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta 1432, 159-184.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 28
    • 0035017658 scopus 로고    scopus 로고
    • Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress
    • Dastoor, Z., and Dreyer, J. L. (2001) Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress. J. Cell Sci. 114, 1643-1653.
    • (2001) J. Cell Sci. , vol.114 , pp. 1643-1653
    • Dastoor, Z.1    Dreyer, J.L.2
  • 29
    • 0038771936 scopus 로고    scopus 로고
    • Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function
    • Mazzola, J. L., and Sirover, M. A. (2003) Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function. Biochim. Biophys. Acta 1622, 50-56.
    • (2003) Biochim. Biophys. Acta , vol.1622 , pp. 50-56
    • Mazzola, J.L.1    Sirover, M.A.2
  • 30
    • 0030930536 scopus 로고    scopus 로고
    • Koningic acid (a potent glyceraldehyde-3-phosphate dehydrogenase inhibitor)-induced fragmentation and condensation of DNA in NG108-15 cells
    • Nakazawa, M., Uehara, T., and Nomura, Y. (1997) Koningic acid (a potent glyceraldehyde-3-phosphate dehydrogenase inhibitor)-induced fragmentation and condensation of DNA in NG108-15 cells. J. Neurochem. 68, 2493-2499.
    • (1997) J. Neurochem. , vol.68 , pp. 2493-2499
    • Nakazawa, M.1    Uehara, T.2    Nomura, Y.3
  • 31
    • 0034656409 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase and apoptosis
    • Berry, M. D., and Boulton, A. A. (2000) Glyceraldehyde-3-phosphate dehydrogenase and apoptosis. J. Neurosci. Res. 60, 150-154.
    • (2000) J. Neurosci. Res. , vol.60 , pp. 150-154
    • Berry, M.D.1    Boulton, A.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.