메뉴 건너뛰기




Volumn 259, Issue 1-2, 2009, Pages 77-83

Inhibition of erythrocyte phosphoribosyltransferases (APRT and HPRT) by Pb2+: A potential mechanism of lead toxicity

Author keywords

APRT; Erythrocyte; Hemolysis; HPRT; Lead (Pb2+); Phosphoribosyltransferases

Indexed keywords

ACETIC ACID; ADENINE PHOSPHORIBOSYLTRANSFERASE; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; LEAD;

EID: 63149128565     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tox.2009.02.005     Document Type: Article
Times cited : (23)

References (53)
  • 3
    • 0032173237 scopus 로고    scopus 로고
    • The effect of zinc supplementation on the effects of lead on the rat testis
    • Batra N., Nehru B., and Bansal M.P. The effect of zinc supplementation on the effects of lead on the rat testis. Reprod. Toxicol. 12 (1998) 535-540
    • (1998) Reprod. Toxicol. , vol.12 , pp. 535-540
    • Batra, N.1    Nehru, B.2    Bansal, M.P.3
  • 4
    • 0030009647 scopus 로고    scopus 로고
    • Phosphorylation of membrane proteins in erythrocytes treated with lead
    • Belloni-Olivi L., Annadata M., Goldstein G.W., and Bressler J.P. Phosphorylation of membrane proteins in erythrocytes treated with lead. Biochem. J. 315 (1996) 401-406
    • (1996) Biochem. J. , vol.315 , pp. 401-406
    • Belloni-Olivi, L.1    Annadata, M.2    Goldstein, G.W.3    Bressler, J.P.4
  • 5
    • 45749113752 scopus 로고    scopus 로고
    • Peas, beans, and the Pythagorean theorem-the relevance of glucose-6-phosphate dehydrogenase deficiency in dermatology
    • Brandt O., Rieger A., Geusau A., and Stingl G. Peas, beans, and the Pythagorean theorem-the relevance of glucose-6-phosphate dehydrogenase deficiency in dermatology. J. Dtsch Dermatol. Ges. 6 (2008) 534-539
    • (2008) J. Dtsch Dermatol. Ges. , vol.6 , pp. 534-539
    • Brandt, O.1    Rieger, A.2    Geusau, A.3    Stingl, G.4
  • 6
    • 34047095199 scopus 로고    scopus 로고
    • Free radical-mediated pre-hemolytic injury in human red blood cells subjected to lead acetate as evaluated by chemiluminescence
    • Casado M.F., Cecchini A.L., Simao A.N.C., Oliveira R.D., and Cecchini R. Free radical-mediated pre-hemolytic injury in human red blood cells subjected to lead acetate as evaluated by chemiluminescence. Food Chem. Toxicol. 45 (2007) 945-952
    • (2007) Food Chem. Toxicol. , vol.45 , pp. 945-952
    • Casado, M.F.1    Cecchini, A.L.2    Simao, A.N.C.3    Oliveira, R.D.4    Cecchini, R.5
  • 8
    • 0027461520 scopus 로고
    • Molecular and ionic mimicry of toxic metals
    • Clarkson T. Molecular and ionic mimicry of toxic metals. Annu. Rev. Pharmacol. Toxicol. 33 (1993) 545-571
    • (1993) Annu. Rev. Pharmacol. Toxicol. , vol.33 , pp. 545-571
    • Clarkson, T.1
  • 9
    • 0030624685 scopus 로고    scopus 로고
    • Erythrocyte pyruvate kinase-an enzyme that may have an influence on oxygen transport to tissues
    • Dabrowska A. Erythrocyte pyruvate kinase-an enzyme that may have an influence on oxygen transport to tissues. Postepy Hig. Med. Dosw. 51 (1997) 305-318
    • (1997) Postepy Hig. Med. Dosw. , vol.51 , pp. 305-318
    • Dabrowska, A.1
  • 10
    • 0020424165 scopus 로고
    • Regulation of cellular energy metabolism
    • Erecińska M., and Wilson D.F. Regulation of cellular energy metabolism. J. Membr. Biol. 70 (1982) 1-14
    • (1982) J. Membr. Biol. , vol.70 , pp. 1-14
    • Erecińska, M.1    Wilson, D.F.2
  • 11
    • 6444239186 scopus 로고
    • Biological roles of high affinity metal-binding proteins in mediating cell injury
    • Fowler B.A. Biological roles of high affinity metal-binding proteins in mediating cell injury. Comments Toxicol. 3 (1989) 27-46
    • (1989) Comments Toxicol. , vol.3 , pp. 27-46
    • Fowler, B.A.1
  • 12
    • 0025869511 scopus 로고
    • Effects of lead on the kidneys. Roles of high affinity metal-binding proteins
    • Fowler B.A., and Du Vall G.E. Effects of lead on the kidneys. Roles of high affinity metal-binding proteins. Environ. Health Perspect. 91 (1991) 77-80
    • (1991) Environ. Health Perspect. , vol.91 , pp. 77-80
    • Fowler, B.A.1    Du Vall, G.E.2
  • 13
    • 0025096451 scopus 로고
    • Expression of active human hypoxanthine-guanine phosphoribosyltransferase in Escherichia coli and characterization of the recombinant enzyme
    • Free M.L., Gordon R.B., Keough D.T., Beachman I.R., Emmerson B.T., and Jersey J. Expression of active human hypoxanthine-guanine phosphoribosyltransferase in Escherichia coli and characterization of the recombinant enzyme. Biochim. Biophys. Acta 1087 (1990) 205-211
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 205-211
    • Free, M.L.1    Gordon, R.B.2    Keough, D.T.3    Beachman, I.R.4    Emmerson, B.T.5    Jersey, J.6
  • 14
    • 51349117161 scopus 로고    scopus 로고
    • Oxidative stress in the regulation of normal and neoplastic hemopoiesis
    • Ghaffari S. Oxidative stress in the regulation of normal and neoplastic hemopoiesis. Antioxid. Redox Signal. 10 (2008) 1923-1940
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1923-1940
    • Ghaffari, S.1
  • 15
    • 0029827776 scopus 로고    scopus 로고
    • The effect of lead on lactate formation, ATP level and membrane ATPase activities in human erythrocytes in vitro
    • Grabowska M., and Gumińska M. The effect of lead on lactate formation, ATP level and membrane ATPase activities in human erythrocytes in vitro. Int. J. Occup. Med. Environ. Health 9 (1996) 265-274
    • (1996) Int. J. Occup. Med. Environ. Health , vol.9 , pp. 265-274
    • Grabowska, M.1    Gumińska, M.2
  • 16
    • 0021874741 scopus 로고
    • Mathematical modelling of metabolic pathways affected by enzyme deficiency. A mathematical model of glycolysis in normal and pyruvate kinase-deficient red blood cells
    • Holzhutter H., Jacobasch G., and Bisdorff A. Mathematical modelling of metabolic pathways affected by enzyme deficiency. A mathematical model of glycolysis in normal and pyruvate kinase-deficient red blood cells. Eur. J. Biochem. 149 (1985) 101-111
    • (1985) Eur. J. Biochem. , vol.149 , pp. 101-111
    • Holzhutter, H.1    Jacobasch, G.2    Bisdorff, A.3
  • 17
    • 0028805697 scopus 로고
    • Identification of the active sites of human and schistosomal hypoxanthine-guanine phosphoribosyltransferases by GMP-2′,3′-dialdehyde affinity labeling
    • Kanaani J., Maltby D., Focia P., and Wang C.C. Identification of the active sites of human and schistosomal hypoxanthine-guanine phosphoribosyltransferases by GMP-2′,3′-dialdehyde affinity labeling. Biochemistry 34 (1995) 14987-14996
    • (1995) Biochemistry , vol.34 , pp. 14987-14996
    • Kanaani, J.1    Maltby, D.2    Focia, P.3    Wang, C.C.4
  • 18
    • 0029949033 scopus 로고    scopus 로고
    • Probing the active site of Tritrichomonas foetus hypoxanthine-guanine-xanthine phosphoribosyltransferase using covalent modification of cysteine residues
    • Kanaani J., Somoza J.R., Maltby D., and Wang C.C. Probing the active site of Tritrichomonas foetus hypoxanthine-guanine-xanthine phosphoribosyltransferase using covalent modification of cysteine residues. Eur. J. Biochem. 239 (1996) 764-772
    • (1996) Eur. J. Biochem. , vol.239 , pp. 764-772
    • Kanaani, J.1    Somoza, J.R.2    Maltby, D.3    Wang, C.C.4
  • 19
    • 0025518872 scopus 로고
    • Effect of lead acetate on erythrocyte morphology in rats
    • Karmarkar N., Saxena N., and Anand S. Effect of lead acetate on erythrocyte morphology in rats. Indian J. Exp. Biol. 28 (1990) 1084-1085
    • (1990) Indian J. Exp. Biol. , vol.28 , pp. 1084-1085
    • Karmarkar, N.1    Saxena, N.2    Anand, S.3
  • 20
    • 0021340352 scopus 로고
    • Inhibition of pentose phosphate shunt by lead: a potential mechanism for hemolysis in lead poisoning
    • Lachant N.E., Tomoda A., and Tanaka K.R. Inhibition of pentose phosphate shunt by lead: a potential mechanism for hemolysis in lead poisoning. Blood 63 (1984) 518-524
    • (1984) Blood , vol.63 , pp. 518-524
    • Lachant, N.E.1    Tomoda, A.2    Tanaka, K.R.3
  • 21
    • 0012441495 scopus 로고    scopus 로고
    • Characteristic changes in erythrocyte nucleotides in haemolytic anemia with basophilic stippling of differing aetiology
    • Laurence A., Duley J.A., Simmonds H.A., and Layton M. Characteristic changes in erythrocyte nucleotides in haemolytic anemia with basophilic stippling of differing aetiology. Cell. Mol. Biol. Lett. 4 (1999) 406
    • (1999) Cell. Mol. Biol. Lett. , vol.4 , pp. 406
    • Laurence, A.1    Duley, J.A.2    Simmonds, H.A.3    Layton, M.4
  • 22
    • 0037227997 scopus 로고    scopus 로고
    • Lead neurotoxicity in children: basic mechanisms and clinical correlates
    • Lidsky T.I., and Schneider J.S. Lead neurotoxicity in children: basic mechanisms and clinical correlates. Brain 126 (2003) 5-19
    • (2003) Brain , vol.126 , pp. 5-19
    • Lidsky, T.I.1    Schneider, J.S.2
  • 24
    • 0034145645 scopus 로고    scopus 로고
    • Lead poisoning: a disease for the next millennium
    • Markowitz M. Lead poisoning: a disease for the next millennium. Curr. Probl. Pediatr. 30 (2000) 62-70
    • (2000) Curr. Probl. Pediatr. , vol.30 , pp. 62-70
    • Markowitz, M.1
  • 25
    • 0017694520 scopus 로고
    • Factors in the pathogenesis of brain damage and anaemia in the Lesch-Nyhan syndrome
    • McKeran R.O. Factors in the pathogenesis of brain damage and anaemia in the Lesch-Nyhan syndrome. Ciba Found. Symp. 48 (1977) 83-96
    • (1977) Ciba Found. Symp. , vol.48 , pp. 83-96
    • McKeran, R.O.1
  • 26
    • 0003329149 scopus 로고
    • Disorders of erythrocyte metabolism
    • Mentzer W.C., and Wagner G.M. (Eds), Churchill Livingstone, New York
    • Mentzer W.C., and Glader B.E. Disorders of erythrocyte metabolism. In: Mentzer W.C., and Wagner G.M. (Eds). The Hereditary Hemolytic Anemias (1989), Churchill Livingstone, New York 267
    • (1989) The Hereditary Hemolytic Anemias , pp. 267
    • Mentzer, W.C.1    Glader, B.E.2
  • 27
    • 0015245542 scopus 로고
    • Adenosine metabolism in human erythrocytes
    • Meyskens F.L., and Williams H.E. Adenosine metabolism in human erythrocytes. Biochim. Biophys. Acta 240 (1971) 170-179
    • (1971) Biochim. Biophys. Acta , vol.240 , pp. 170-179
    • Meyskens, F.L.1    Williams, H.E.2
  • 31
    • 0033926261 scopus 로고    scopus 로고
    • Dopamine function in Lesch-Nyhan disease
    • Nyhan W.L. Dopamine function in Lesch-Nyhan disease. Environ. Health Perspect. 108 (2000) 409-411
    • (2000) Environ. Health Perspect. , vol.108 , pp. 409-411
    • Nyhan, W.L.1
  • 32
    • 0028457898 scopus 로고
    • The importance of vitamins in the relation to presence of heavy metals in food
    • Pace V., and Iannucci E. The importance of vitamins in the relation to presence of heavy metals in food. Panminerva Med. 36 (1994) 80-82
    • (1994) Panminerva Med. , vol.36 , pp. 80-82
    • Pace, V.1    Iannucci, E.2
  • 33
    • 0016802326 scopus 로고
    • Effects of low-level lead exposure on pyrimidine 5′-nucleotidase and other erythrocyte enzymes. Possible role of pyrimidine 5′-nucleotidase in the pathogenesis of lead-induced anemia
    • Paglia D.E., Valentine W.N., and Dahlgren J.G. Effects of low-level lead exposure on pyrimidine 5′-nucleotidase and other erythrocyte enzymes. Possible role of pyrimidine 5′-nucleotidase in the pathogenesis of lead-induced anemia. J. Clin. Invest. 56 (1975) 1164-1169
    • (1975) J. Clin. Invest. , vol.56 , pp. 1164-1169
    • Paglia, D.E.1    Valentine, W.N.2    Dahlgren, J.G.3
  • 35
    • 9244231524 scopus 로고
    • The role of phosphoribosyltransferases in purine metabolism
    • Horecker B.L., and Stadtman E.R. (Eds), Academic Press, Inc., New York
    • Raivio K.O., and Seegmiller J.E. The role of phosphoribosyltransferases in purine metabolism. In: Horecker B.L., and Stadtman E.R. (Eds). Current Topics in Cellular Regulation vol. 2 (1970), Academic Press, Inc., New York 201-225
    • (1970) Current Topics in Cellular Regulation , vol.2 , pp. 201-225
    • Raivio, K.O.1    Seegmiller, J.E.2
  • 36
    • 0020079059 scopus 로고
    • Hypoxanthine-guanine phosphoribosyl transferase: assay using high performance liquid chromatography
    • Rylance H.J., Wallace R.C., and Nuki G. Hypoxanthine-guanine phosphoribosyl transferase: assay using high performance liquid chromatography. Clin. Chim. Acta 121 (1982) 159-165
    • (1982) Clin. Chim. Acta , vol.121 , pp. 159-165
    • Rylance, H.J.1    Wallace, R.C.2    Nuki, G.3
  • 37
    • 0023579935 scopus 로고
    • Screening for adenine and hypoxanthine phosphoribosyltransferase deficiencies in human erythrocytes by high-performance liquid chromatography
    • Sakuma R., Nishina T., Kitamura M., Yamanaka H., Kamatani N., and Nishioka K. Screening for adenine and hypoxanthine phosphoribosyltransferase deficiencies in human erythrocytes by high-performance liquid chromatography. Clin. Chim. Acta 170 (1987) 281-289
    • (1987) Clin. Chim. Acta , vol.170 , pp. 281-289
    • Sakuma, R.1    Nishina, T.2    Kitamura, M.3    Yamanaka, H.4    Kamatani, N.5    Nishioka, K.6
  • 38
    • 21244497606 scopus 로고    scopus 로고
    • Biological effects of heavy metals: an overview
    • Sharma R.K., and Agrawal M. Biological effects of heavy metals: an overview. J. Environ. Biol. 26 (2005) 301-313
    • (2005) J. Environ. Biol. , vol.26 , pp. 301-313
    • Sharma, R.K.1    Agrawal, M.2
  • 39
    • 0034058543 scopus 로고    scopus 로고
    • Erythrocyte free radical and energy metabolism
    • Siems W.G., Sommerburg O., and Grune T. Erythrocyte free radical and energy metabolism. Clin. Nephrol. 53 (2000) 9-17
    • (2000) Clin. Nephrol. , vol.53 , pp. 9-17
    • Siems, W.G.1    Sommerburg, O.2    Grune, T.3
  • 40
    • 2942733483 scopus 로고    scopus 로고
    • Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis
    • Silva M., Silva C.H., Iulek J., and Thiemann O.H. Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis. Biochemistry 43 (2004) 7663-7671
    • (2004) Biochemistry , vol.43 , pp. 7663-7671
    • Silva, M.1    Silva, C.H.2    Iulek, J.3    Thiemann, O.H.4
  • 41
    • 0025311410 scopus 로고
    • Determination of sixteen nucleotides, nucleosides and bases using high-performance liquid chromatography and its application to the study of purine metabolism in hearts for transplantation
    • Smolenski R.T., Lachno D.R., Ledingham S.J., and Yacoub M.H. Determination of sixteen nucleotides, nucleosides and bases using high-performance liquid chromatography and its application to the study of purine metabolism in hearts for transplantation. J. Chromatogr. 527 (1990) 414-420
    • (1990) J. Chromatogr. , vol.527 , pp. 414-420
    • Smolenski, R.T.1    Lachno, D.R.2    Ledingham, S.J.3    Yacoub, M.H.4
  • 42
    • 0020383946 scopus 로고
    • Hemolytic anemia in hereditary pyrimidine 5′-nucleotidase deficiency: nucleotide inhibition of G6PD and the pentose phosphate shunt
    • Tomoda A., Noble N.A., Lachant N.A., and Tanaka K.R. Hemolytic anemia in hereditary pyrimidine 5′-nucleotidase deficiency: nucleotide inhibition of G6PD and the pentose phosphate shunt. Blood 60 (1982) 1212-1218
    • (1982) Blood , vol.60 , pp. 1212-1218
    • Tomoda, A.1    Noble, N.A.2    Lachant, N.A.3    Tanaka, K.R.4
  • 43
    • 39049126490 scopus 로고    scopus 로고
    • Hypoxanthine-guanine phosophoribosyltransferase (HPRT) deficiency: Lesch-Nyhan syndrome
    • Torres R.J., and Puig J.G. Hypoxanthine-guanine phosophoribosyltransferase (HPRT) deficiency: Lesch-Nyhan syndrome. Orphanet J. Rare Dis. 2 (2007) 48
    • (2007) Orphanet J. Rare Dis. , vol.2 , pp. 48
    • Torres, R.J.1    Puig, J.G.2
  • 44
    • 0019196862 scopus 로고
    • Erythrocyte disorders of purine and pyrimidine metabolism
    • Valentine W.N., and Paglia D.E. Erythrocyte disorders of purine and pyrimidine metabolism. Hemoglobin 4 (1980) 669-681
    • (1980) Hemoglobin , vol.4 , pp. 669-681
    • Valentine, W.N.1    Paglia, D.E.2
  • 45
    • 33745667074 scopus 로고
    • Standardization of hemoglobinometry. II. The hemiglobincyanide method
    • Van Kampen E., and Zijlstra W.G. Standardization of hemoglobinometry. II. The hemiglobincyanide method. Clin. Chim. Acta 6 (1961) 538-544
    • (1961) Clin. Chim. Acta , vol.6 , pp. 538-544
    • Van Kampen, E.1    Zijlstra, W.G.2
  • 46
    • 0032475913 scopus 로고    scopus 로고
    • Structures of free and complexed forms of Escherichia coli hypoxanthine-guanine phosphoribosyltransferase
    • Vos S., Parry R.J., Burns M.R., de Jersey J., and Martin J.L. Structures of free and complexed forms of Escherichia coli hypoxanthine-guanine phosphoribosyltransferase. J. Mol. Biol. 282 (1998) 875-889
    • (1998) J. Mol. Biol. , vol.282 , pp. 875-889
    • Vos, S.1    Parry, R.J.2    Burns, M.R.3    de Jersey, J.4    Martin, J.L.5
  • 47
    • 0003402823 scopus 로고
    • WHO World Health Organization, Inorganic Lead. Geneva
    • WHO (World Health Organization), 1995. Environmental Health Criteria 165. Inorganic Lead. Geneva.
    • (1995) Environmental Health Criteria , vol.165
  • 48
    • 0020356107 scopus 로고
    • Human hypoxanthine-guanine phosphoribosyltransferase. Tryptic peptides and post-translational modification of the erythrocyte enzyme
    • Wilson J.M., Landa L.E., Kobayashi R., and Kelley W.N. Human hypoxanthine-guanine phosphoribosyltransferase. Tryptic peptides and post-translational modification of the erythrocyte enzyme. J. Biol. Chem. 257 (1982) 14830-14834
    • (1982) J. Biol. Chem. , vol.257 , pp. 14830-14834
    • Wilson, J.M.1    Landa, L.E.2    Kobayashi, R.3    Kelley, W.N.4
  • 49
    • 0022981631 scopus 로고
    • Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme
    • Wilson J.M., O'Toole T.E., Argos P., Shewach D.S., Daddona P.E., and Kelley W.N. Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J. Biol. Chem. 261 (1986) 13677-13683
    • (1986) J. Biol. Chem. , vol.261 , pp. 13677-13683
    • Wilson, J.M.1    O'Toole, T.E.2    Argos, P.3    Shewach, D.S.4    Daddona, P.E.5    Kelley, W.N.6
  • 51
    • 0023235334 scopus 로고
    • Impaired nicotinamide adenine dinucleotide synthesis in pyruvate kinase-deficient human erythrocytes: a mechanism for decreased total NAD content and a possible secondary cause of hemolysis
    • Zerez C.R., and Tanaka K.R. Impaired nicotinamide adenine dinucleotide synthesis in pyruvate kinase-deficient human erythrocytes: a mechanism for decreased total NAD content and a possible secondary cause of hemolysis. Blood 69 (1987) 999-1005
    • (1987) Blood , vol.69 , pp. 999-1005
    • Zerez, C.R.1    Tanaka, K.R.2
  • 52
    • 0023813394 scopus 로고
    • Impaired erythrocyte phosphoribosylpyrophosphate formation in hemolytic anemia due to pyruvate kinase deficiency
    • Zerez C.R., Wong M.D., Lachant N.A., and Tanaka K.R. Impaired erythrocyte phosphoribosylpyrophosphate formation in hemolytic anemia due to pyruvate kinase deficiency. Blood 72 (1988) 500-506
    • (1988) Blood , vol.72 , pp. 500-506
    • Zerez, C.R.1    Wong, M.D.2    Lachant, N.A.3    Tanaka, K.R.4
  • 53
    • 0025263919 scopus 로고
    • Partial purification and properties of nicotinamide adenine dinucleotide synthetase from human erythrocytes: evidence that enzyme activity is a sensitive indicator of lead exposure
    • Zerez C.R., Wong M.D., and Tanaka K.R. Partial purification and properties of nicotinamide adenine dinucleotide synthetase from human erythrocytes: evidence that enzyme activity is a sensitive indicator of lead exposure. Blood 75 (1990) 1576-1582
    • (1990) Blood , vol.75 , pp. 1576-1582
    • Zerez, C.R.1    Wong, M.D.2    Tanaka, K.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.