Plasma and blood lead in humans: Capacity-limited binding to δ- aminolevulinic acid dehydratase and other lead-binding components

Toxicological Sciences

Volumn 46, Issue 2, 1998, Pages 247-253

  Bergdahl, I A ^a   Sheveleva, M ^a   Schutz, A ^a   Artamonova, V G ^a   Skerfving, S ^a  

^a UMEÅ UNIVERSITY HOSPITAL   (Sweden)

Author keywords

ALAD; Blood; Lead; Lead binding proteins; Model; Plasma; Proteins; aminolevulinic acid dehydratase

Indexed keywords

BINDING PROTEIN; LEAD; PORPHOBILINOGEN SYNTHASE; ZINC;

ADULT; ARTICLE; BINDING AFFINITY; CLINICAL ARTICLE; DISSOCIATION CONSTANT; ENZYME BINDING; ERYTHROCYTE; FEMALE; GEL CHROMATOGRAPHY; HUMAN; LEAD BLOOD LEVEL; MALE; MASS SPECTROMETRY; METAL BINDING; MODEL;

EID: 0032444974     PISSN: 10966080     EISSN: None     Source Type: Journal    
DOI: 10.1006/toxs.1998.2535     Document Type: Article

References (39)

1. A. Amici M. Emanuelli E. Ferretti N. Raffaelli S. Ruggieri G. Magni Homogeneous pyrimidine nucleotidase from human erythrocytes: Enzymic and molecular properties Biochem. J. 304 1994 987 992
2. S. Araki K. Murata E. Uchida H. Aono H. Ozawa Radial and median nerve conduction velocities in workers exposed to lead, copper, and zinc: A follow-up study for 2 years Environ. Res. 61 1993 308 316
3. D. Barltrop A. Smith Interaction of lead with erythrocytes Experientia 27 1971 92 93
4. I.A. Bergdahl A. Schütz A. Grubb Application of liquid chromatography-inductively coupled plasma mass spectrometry to the study of protein-bound lead in human erythrocytes J. Anal. Atom. Spectrom. 11 1996 735 738
5. I.A. Bergdahl A. Schütz L. Gerhardsson A. Jensen S. Skerfving Lead concentrations in human plasma, urine, and whole blood Scand. J. Work Environ. Health 23 1997 359 363
6. I.A. Bergdahl A. Grubb A. Schütz R.J. Desnick J.G. Wetmur S. Sassa S. Skerfving Lead binding to δ-aminolevulinic acid dehydratase (ALAD) in erythrocytes Pharmacol. Toxicol. 81 1997 153 158
7. Bergdahl, I. A. Vahter, M. Counter, S. A. Schütz, A. Buchanan, L. Ortega, F. Laurell, G. Skerfving, S. Lead in plasma and whole blood from lead-exposed children, Environ. Res.
8. C. Boudene N. Despaux-Pages E. Comoy C. Bohuon Immunological and enzymatic studies of erythrocytic δ-aminolevulinate dehydratase: Comparison of results obtained in normal and lead-exposed subjects Int. Arch. Occup. Environ. Health 55 1984 87 96
9. 210 Health Phys. 25 1973 37 42
10. H.J. Church P. Day R.A. Braithwaite S.S. Brown Binding of lead to a metallothionein-like protein in human erythrocytes J. Inorg. Biochem. 49 1993 55 68
11. A.J. Dent D. Beyersmann C. Block S.S. Hasnain Two different zinc sites in bovine 5-aminolevulinate dehydratase distinguished by extended X-ray absorption fine structure Biochemistry 29 1990 7822 7828
12. P.E. deSilva Determination of lead in plasma and studies on its relationship to lead in erythrocytes Br. J. Ind. Med. 38 1981 209 217
13. H. Fujita K. Sato S. Sano Increase in the amount of erythrocyte. δ-aminolevulinic acid dehydratase in workers with moderate lead exposure Int. Arch. Occup. Environ. Health 50 1982 287 297
14. H. Fyrst J. Knudsen M.A. Schott B.H. Lubin F.A. Kuypers Detection of acyl-CoA-binding protein in human red blood cells and investigation of its role in membrane phopholipid renewal Biochem. J. 306 1995 793 799
15. B. Haeger-Aronsen A. Schütz M. Abdulla Antagonistic effect in vivo of zinc on inhibition of δ-aminolevulinic acid dehydratase by lead Arch. Environ. Health 31 1976 215 220
16. M. Kolmer A. Rovio H. Alho The characterization ot two diazepam binding inhibitor (DBI) transcripts in humans Biochem. J. 306 1995 327 330
17. Y. Lolin P. O'Gorman An intra-erythrocytic low molecular weight lead-binding protein in acute and chronic lead exposure and its possible protective role in lead toxicity Ann. Clin. Biochem. 25 1988 688 697
18. W.I. Manton C.R. Malloy Distribution of lead in body fluids after ingestion of soft solder Br. J. Ind. Med. 40 1983 51 57
19. Marcus, A. H. 1985a, Testing alternative nonlinear kinetic models in compartmental analysis, Mathematics and Computers in Biomedical Applications, 259, 267, Elsevier, Amsterdam
20. A.H. Marcus Multicompartment kinetic model for lead. III. Lead in blood plasma and erythrocytes Environ. Res. 36 1985 473 489
21. M.T. Martin Metal-free chromatographic media Methods Enzymol. 158 1988 15 21
22. Measuring Lead Exposure in Infants, Children, and Other Sensitive Populations 1993 National Academy Press Washington
23. E.J. O'Flaherty Physiologically based models for bone-seeking elements. IV. Kinetics of lead disposition in humans Toxicol. Appl. Phamracol. 118 1993 16 29
24. E.J. O'Flaherty Physiologically based models for bone-seeking elements. V. Lead absorption and disposition in childhood Toxicol. Appl. Pharmacol. 131 1995 297 308
25. E.J. O'Flaherty M.J. Inskip A.P. Yagminas C.A. Franklin Plasma and blood lead concentrations, lead absorption, and lead excretion in nonhuman primates Toxicol. Appl. Pharmacol. 138 1996 121 130
26. C.N. Ong W.R. Lee Distribution of lead-203 in human peripheral blood in vitro Br. J. Ind. Med. 37 1980 78 84
27. L.M.W. Owen H.M. Crews R.C. Hutton A. Walsh Preliminary study of metals in proteins by high-performance liquid chromatography-inductively coupled plasma mass spectrometry using multi-element time-resolved analysis Analyst 117 1992 649 655
28. D.E. Paglia W.N. Valentine K. Fink Lead poisoning. Further observations on erythrocyte pyrimidine-nucleotidase deficiency and intracellular accumulation of pyrimidine nucleotides J. Clin. Invest. 60 1977 1362 1366
29. I. Palminger Hallén S. Jönsson M.O. Karlsson A. Oskarsson Toxicokinetics of lead in lactating and nonlactating mice Toxicol. Pharmacol. 136 1996 342 347
30. S.R.V. Raghavan H.C. Gonick Isolation of low-molecular-weight lead-binding protein from human erythrocytes Proc. Soc. Exp. Biol. Med. 155 1977 164 167
31. S.R.V. Raghavan B.D. Culver H.C. Gonick Erythrocyte lead-binding protein after occupational exposure. I. Relationship to lead toxicity Environ. Res. 22 1980 264 270
32. + J. Toxicol. Environ. Health 7 1981 561 568
33. T. Sakai S. Yanagihara Y. Kunugi K. Ushio Relationships between distribution of lead in erythrocytes in vivo and in vitro and inhibition of ALA-D Br. J. Ind. Med. 39 1982 382 387
34. A. Schütz S. Skerfving Effect of a short, heavy exposure to lead dust upon blood lead level, erythrocyte δ-aminolevulinic acid dehydratase activity and urinary excretion of lead, δ-aminolveulinic acid and coproporphyrin: Results of a 6-month follow-up of two male subjects Scand. J. Work Environ. Health 3 1976 176 184
35. A. Schütz I.A. Bergdahl A. Ekholm S. Skerfving Measurement by ICP-MS of lead in plasma and whole blood of lead workers and controls Occup. Environ. Med. 53 1996 736 740
36. T.J.B. Simons Lead transport and binding by human erythrocytes in vitro Pflügers Arch. 423 1993 307 313
37. T.J.B. Simons The affinity of human erythrocyte porphobilinogen synthase for Zn2+ and Pb2+ Eur. J. Biochem. 234 1995 178 183
38. D.R. Smith M.W. Kahng B. Quintanilla B.A. Fowler Lead-binding polypeptides in human kidney cytosol: diazepam binding inhibitor and thymosin beta-4 Toxicologist 14 1994 84
39. WHO, 1995, Environmental health criteria 165 Inorganic lead, World Health Organization, Geneva