Formation of zinc protoporphyrin in cultured hepatocytes: Effects of ferrochelatase inhibition, iron chelation or lead

Toxicology

Volumn 125, Issue 2-3, 1998, Pages 95-105

  Jacobs, Judith M ^b   Sinclair, Peter R ^a,b   Sinclair, Jacqueline F ^a,b   Gorman, Nadia ^b   Walton, Heidi S ^b   Wood, Sheryl G ^a   Nichols, Calen ^a  

^a VA MEDICAL CENTER   (United States)

^b DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

Ferrochelatase; Hepatocytes; Iron; Lead; Zinc protoporphyrin

Indexed keywords

CATALASE; HEME; IRON; LEAD; PROTOPORPHYRIN ZINC;

ANIMAL TISSUE; ARTICLE; CHICK EMBRYO; EMBRYO; ERYTHROID CELL; EXTRAMEDULLARY HEMATOPOIESIS; HEME SYNTHESIS; IRON CHELATION; LEAD POISONING; LIVER CELL; NONHUMAN; PRIORITY JOURNAL;

AMINOLEVULINIC ACID; ANIMALS; CELLS, CULTURED; CHICK EMBRYO; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ENZYME INHIBITORS; FERROCHELATASE; HEME; IRON CHELATING AGENTS; LEAD; LIVER; MALE; PROTOPORPHYRINS; RATS; RATS, INBRED F344;

EID: 0032489060     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-483X(97)00164-9     Document Type: Article

References (36)

1. Abraham N.G., Camadro J.-M., Hoffstein S.T., Levere R.D. Effects of iron deficiency and chronic iron overloading on the mitochondrial enzymes of heme synthesis. Biochim. Biophys. Acta. 870:1986;339-349.
2. Barnam-Huckins A.M., Martinez A.O., Rivera E.V., Adrian E.K., Herbert D.C., Weaker F.J., Walter C.A., Adriam G.S. A comparison of the suppression of human transferrin synthesis by lead and lipopolysaccharide. Toxicology. 118:1997;11-22.
3. Bissell D.M., Guzelian P. Phenotypic stability of adult rat hepatocytes in primary hepatocyte cultures. Ann. NY Acad. Sci. 349:1980;85-87.
4. Bloomer J.R., Reuter R.J., Morton K.O., Wehner J.M. Enzymatic formation of zinc protoporphyrin by rat liver and its potential effect on hepatic heme metabolism. Gastroenterology. 85:1983;663-668.
5. Buchet J.P., Roels H., Hubermont G., Lauwerys R. Effect of lead on some parameters of the heme biosynthesis pathway in rat tissues in vivo. Toxicology. 6:1976;21-31.
6. Camadro J.-M., Labbe P. Kinetic studies of ferrochelatase in yeast. Zinc and iron as competing substrates. Biochim. Biophys. Acta. 707:1982;280-288.
7. Camadro J.-M., Ibraham N.G., Levere R.D. Kinetic studies of human ferrochelatase. J. Biol. Chem. 259:1984;5678-5682.
8. Dailey H.A., Fleming J.E. Bovine ferrochelatase. Kinetic analysis of inhibition by N-methylprotoporphyrin, manganese and heme. J. Biol. Chem. 257:1983;11453-11459.
9. De Matteis F., Gibbs A.H., Harvey C. Studies on the inhibition of ferrochelatase by N-alkylated dicarboxylic porphyrins. Steric factors involved and evidence that the inhibition is reversible. Biochem. J. 226:1985;537-544.
10. Fabri, G. Castellino, N., 1995. Lead and the erythropoietic system. In: Castellino, N., Castellino, P., Sannolo, N. (Eds.), Inorganic Lead Exposure: Metabolism and Intoxication. CRC Press Inc, Salem, MA, pp. 369-402.
11. Grandchamp B., Deybach J., Grelier M., Nordman Y. Studies of porphyrin synthesis in fibroblasts of patients with congenital erythropoietic porphyria and one patient with homozygous coproporphyria. Biochim. Biophys. Acta. 629:1980;577-586.
12. Granick S., Sinclair P.R., Sassa S., Grieninger G. Effect of heme, insulin, and serum albumin on heme and protein synthesis in chick embryo liver cells cultured in a chemically defined medium. J. Biol. Chem. 250:1975;9215-9225.
13. Healey J.F., Bonkowsky H.L., Sinclair P.R., Sinclair J.F. Conversion of 5-aminolaevulinate into haem by liver homogenates. Biochem. J. 198:1981;595-604.
14. Jaffe E.K., Bagla S., Michini P.A. Reevaluation of a sensitive indicator of early lead exposure. Measurement of porphobilinogen synthase in blood. Biol. Trace Elem. Res. 28:1991;223-231.
15. Jones M.S., Jones O.T. The structural organization of haem synthesis in rat liver mitochondria. Biochem. J. 113:1969;507-514.
16. Labbe R.F., Rettmer R.L. Zinc Protoporphyrin: a product of iron-deficient erythropoiesis. Semin. Hematol. 26:1989;40-46.
17. Lamola A.A., Yamane T. Zinc protoporphyrin in the erythrocytes of patients with lead intoxication and iron deficiency anemia. Science. 186:1974;936-938.
18. Lutton J.D., Abraham N.G., Drummond G.S., Levere R.D., Kappas A. Zinc porphyrins: potent inhibitors of hematopoiesis in animal and human bone marrow. Proc. Natl. Acad. Sci. USA. 94:1997;432-436.
19. Maines M.D. Zinc protoporphyrin as a selective inhibitor of heme oxygenase activity in neonatal rat. Biochim. Biophys. Acta. 673:1981;339-350.
20. Marks G.S., Powles J., Lyon M., McCluskey S., Sutherland E., Zelt E. Patterns of porphyrin accumulation in response to xenobiotics. Ann. NY Acad. Sci. 514:1987;113-127.
21. Marks G.S., Nakatsu K., Brien J.F. Does endogenous zinc protoporphyrin modulate carbon monoxide formation from heme? Implications for long-term potentiation, memory, and cognitive function. Can. J. Physiol. Pharmacol. 71:1993;753-754.
22. Okada D. Zinc protoporphyrin IX suppresses nitric oxide production through a loss of L-arginine in rat cerebellar slices. Neurosci. Res. 25:1996;353-358.
23. Rossi E., Costin K.A., Garcia-Webb P. Ferrochelatase activity in human lymphocytes as quantified by a new high performance liquid chromatographic method. Clin. Chem. 34:1988;2481-2485.
24. Rossi E., Atwood P.V., Garcia-Webb P., Costin K.A. Metal inhibition of ferrochelatase activity in human lymphocytes. Clin. Chim. Acta. 188:1990;1-14.
25. Rossi E., Taketani S., Garcia-Webb P. Lead and the terminal enzymes of haem biosynthesis. Biomed. Chromatogr. 7:1993;1-6.
26. Sano T., Shiomi M., Wakabayashi Y., Shinoda Y., Goda N., Yamaguchi T., Nimura Y., Ishimora Y., Suematsu M. Endogenous carbon monoxide suppression stimulates bile acid-dependent biliary transport in perfused rat liver. Am. J. Physiol. 272:1997;G1268-G1275.
27. Sassa, S., 1978. Toxic effects of lead, with particular reference to porphyrin and heme metabolism. In: De Matteis, F., Aldridge, W.N. (Eds.), Heme and Hemoproteins. Springer-Verlag, New York, NY, pp. 333-4361.
28. Sinclair P.R., Granick S. Heme control on the synthesis of 5-aminolevulinic acid synthase in cultured chick embryo liver cells. Ann. NY Acad. Sci. 244:1975;509-520.
29. Sinclair J.F., Smith E.L., Bement W.J., Sinclair P.R., Bonkowsky H.L. Increases in cytochrome P-450 in cultured hepatocytes mediated by 3- and 4-carbon alcohols. Biochem. Pharmacol. 31:1982;2811-2815.
30. Sinclair P.R., Bement W.J., Bonkosky H.L., Sinclair J.F. Inhibition of uroporphyrinogen decarboxylase by halogenated biphenyls in chick embryo hepatocyte cultures. Biochem. J. 222:1984;737-748.
31. Sinclair J.F., Zaitlin L.M., Smith E.L., Howell S.K., Bonkovsky H.L., Sinclair P.R. Induction of 5-aminolaevulinate synthase by 2- to 5-carbon alcohols in cultured chick embryo hepatocytes: relationship to induction of cytochrome P-450. Biochem. J. 234:1986;405-411.
32. Sinclair P.R., Bement W.J., Haugen S., Sinclair J.F., Guzelian P. Induction of cytochrome P-450 and 5-aminolevulinate synthase in cultured rat hepatocytes. Cancer Res. 50:1990;5219-5224.
33. Taketani S. The effect of lead on iron uptake from transferrin in human erythroleukemia (KL562) cells. BioMetals. 6:1993;77-83.
34. Taketani S., Tokunaga R. Rat liver ferrochelatase. Purification, properties and stimulation by fatty acids. J. Biol. Chem. 256:1981;12748-12753.
35. Taketani S., Tanaka A., Tokunaga R. Reconstitution of heme-synthesizing activity from ferric ion and porphyrins, and the effect of lead on the activity. Arch. Biochem. Biophys. 242:1985;292-296.
36. Yamamoto T., Nozaki-Taguchi N. Zinc protoporphyrin IX, an inhibitor of the enzyme that produces carbon monoxide, blocks spinal nociceptive transmission evoked by formalin injection in the rat. Brain Res. 704:1995;256-262.