In ferrochelatase-deficient protoporphyria patients, ALAS2 expression is enhanced and erythrocytic protoporphyrin concentration correlates with iron availability

Blood Cells, Molecules, and Diseases

Volumn 54, Issue 1, 2015, Pages 71-77

  Barman Aksözen, Jasmin ^a   Minder, Elisabeth I ^a   Schubiger, Carina ^a   Biolcati, Gianfranco ^b   Schneider Yin, Xiaoye ^a  

^a TRIEMLI HOSPITAL   (Switzerland)

^b SAN GALLICANO DERMATOLOGICAL INSTITUTE   (Italy)

Author keywords

5 Aminolevulinic acid synthase; Cutaneous porphyria; Ferrochelatase; Iron; Protoporphyria

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; FERROCHELATASE; HEMOGLOBIN; IRON; LIVER ENZYME; MESSENGER RNA; PROTOPORPHYRIN; TRANSFERRIN RECEPTOR; ALAS2 PROTEIN, HUMAN;

ADULT; ARTICLE; ATTENTION DISTURBANCE; BLOOD SAMPLING; CELL CULTURE; CELL LEVEL; CHILD; CLINICAL ARTICLE; CONTROLLED STUDY; DISEASE ASSOCIATION; DIZZINESS; ENZYME ACTIVITY; ENZYME BLOOD LEVEL; ERYTHROCYTE; ERYTHROPOIETIC PROTOPORPHYRIA; FATIGUE; FEMALE; HEMOGLOBIN BLOOD LEVEL; HUMAN; HUMAN CELL; IN VITRO STUDY; IRON DEFICIENCY ANEMIA; MALE; MIDDLE AGED; PHOTOSENSITIVITY; PRESCHOOL CHILD; PRIORITY JOURNAL; PROTEIN EXPRESSION; REGULATORY MECHANISM; SCHOOL CHILD; TREATMENT WITHDRAWAL; YOUNG ADULT; ADOLESCENT; BIOSYNTHESIS; CASE REPORT; CLINICAL TRIAL; ENZYMOLOGY; GENE EXPRESSION REGULATION; METABOLISM; PATHOLOGY;

5-AMINOLEVULINATE SYNTHETASE; ADOLESCENT; ADULT; ERYTHROCYTES; FEMALE; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HUMANS; IRON; MALE; MIDDLE AGED; PROTOPORPHYRIA, ERYTHROPOIETIC; PROTOPORPHYRINS; RNA, MESSENGER;

EID: 84926659285     PISSN: 10799796     EISSN: 10960961     Source Type: Journal    
DOI: 10.1016/j.bcmd.2014.07.017     Document Type: Article

References (40)

1. Anderson K., Sassa S., Bishop D.F., Desnick R.J. Disorders of heme biosynthesis: X-linked sideroblastic anemia and the porphyrias. The Metabolic and Molecular Basis of Inherited Disease 2001, 2991-3062. McGraw-Hill, New York. C.R. Scriver, M. Beaugrand, W.S. Sly, D. Valle (Eds.).
2. Anderson K.E., Sassa S., Peterson C.M., Kappas A. Increased erythrocyte uroporphyrinogen-l-synthetase, delta-aminolevulinic acid dehydratase and protoporphyrin in hemolytic anemias. Am. J. Med. 1977, 63:359-364.
3. Atamna H., Liu J., Ames B.N. Heme deficiency selectively interrupts assembly of mitochondrial complex IV in human fibroblasts: revelance to aging. J. Biol. Chem. 2001, 276:48410-48416.
4. Baker H. Erythropoietic protoporphyria provoked by iron therapy. Proc. R. Soc. Med. 1971, 64:610-611.
5. Barman-Aksozen J., Beguin C., Dogar A.M., et al. Iron availability modulates aberrant splicing of ferrochelatase through the iron- and 2-oxoglutarate dependent dioxygenase Jmjd6 and U2AF(65). Blood Cells Mol. Dis. 2013, 51:151-161.
6. Bhasker C.R., Burgiel G., Neupert B., et al. The putative iron-responsive element in the human erythroid 5-aminolevulinate synthase mRNA mediates translational control. J. Biol. Chem. 1993, 268:12699-12705.
7. Bishop D.F., Henderson A.S., Astrin K.H. Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome. Genomics 1990, 7:207-214.
8. Clark K.G., Nicholson D.C. Erythrocyte protoporphyrin and iron uptake in erythropoietic protoporphyria. Clin. Sci. 1971, 41:363-370.
9. Constable A., Quick S., Gray N.K., Hentze M.W. Modulation of the RNA-binding activity of a regulatory protein by iron in vitro: switching between enzymatic and genetic function?. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:4554-4558.
10. Cox T.C., Bawden M.J., Abraham N.G., et al. Erythroid 5-aminolevulinate synthase is located on the X chromosome. Am. J. Hum. Genet. 1990, 46:107-111.
11. Cox T.C., Bawden M.J., Martin A., May B.K. Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 1991, 10:1891-1902.
12. Dailey H.A., Meissner P.N. Erythroid heme biosynthesis and its disorders. Cold Spring Harb. Perspect. Med. 2013, 3:a011676.
13. Dandekar T., Stripecke R., Gray N.K., et al. Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA. EMBO J. 1991, 10:1903-1909.
14. Delaby C., Lyoumi S., Ducamp S., et al. Excessive erythrocyte PPIX influences the hematologic status and iron metabolism in patients with dominant erythropoietic protoporphyria. Cell Mol. Biol. (Noisy-le-grand) 2009, 55:45-52.
15. Doss M.O., Frank M. Hepatobiliary implications and complications in protoporphyria, a 20-year study. Clin. Biochem. 1989, 22:223-229.
16. Goossen B., Hentze M.W. Position is the critical determinant for function of iron-responsive elements as translational regulators. Mol. Cell. Biol. 1992, 12:1959-1966.
17. Granick S., Sinclair P., Sassa S., Grieninger G. Effects by heme, insulin, and serum albumin on heme and protein synthesis in chick embryo liver cells cultured in a chemically defined medium, and a spectrofluorometric assay for porphyrin composition. J. Biol. Chem. 1975, 250:9215-9225.
18. Holme S.A., Thomas C.L., Whatley S.D., et al. Symptomatic response of erythropoietic protoporphyria to iron supplementation. J. Am. Acad. Dermatol. 2007, 56:1070-1072.
19. Holme S.A., Worwood M., Anstey A.V., et al. Erythropoiesis and iron metabolism in dominant erythropoietic protoporphyria. Blood 2007, 110:4108-4110.
20. Horiguchi H., Franklin B.H. Erythropoietin induction in Hep3B cells is not affected by inhibition of heme biosynthesis. Biochim. Biophys. Acta 2000, 1495:231-236.
21. Hunter G.A., Ferreira G.C. Molecular enzymology of 5-aminolevulinate synthase, the gatekeeper of heme biosynthesis. Biochim. Biophys. Acta 2011, 1814:1467-1473.
22. Kniffen J. Protoporphyrin removal in intrahepatic porphyrastasis. Gastroenterology 1970, 58:1027.
23. Kohgo Y., Ikuta K., Ohtake T., et al. Body iron metabolism and pathophysiology of iron overload. Int. J. Hematol. 2008, 88:7-15.
24. Lecha M., Puy H., Deybach J.C. Erythropoietic protoporphyria. Orphanet J. Rare Dis. 2009, 4:19.
25. Lyoumi S., Abitbol M., Andrieu V., et al. Increased plasma transferrin, altered body iron distribution, and microcytic hypochromic anemia in ferrochelatase-deficient mice. Blood 2007, 109:811-818.
26. May B.K., Dogra S.C., Sadlon T.J., et al. Molecular regulation of heme biosynthesis in higher vertebrates. Prog. Nucleic Acid Res. Mol. Biol. 1995, 51:1-51.
27. McClements B.M., Bingham A., Callender M.E., Trimble E.R. Erythropoietic protoporphyria and iron therapy. Br. J. Dermatol. 1990, 122:423-424.
28. McGuire B.M., Bonkovsky H.L., Carithers R.L., et al. Liver transplantation for erythropoietic protoporphyria liver disease. Liver Transpl. 2005, 11:1590-1596.
29. Meerman L. Erythropoietic protoporphyria. An overview with emphasis on the liver. Scand. J. Gastroenterol. 2000, 79-85. (Suppl.).
30. Melefors O., Goossen B., Johansson H.E., et al. Translational control of 5-aminolevulinate synthase mRNA by iron-responsive elements in erythroid cells. J. Biol. Chem. 1993, 268:5974-5978.
31. Milligan A., Graham-Brown R.A., Sarkany I., Baker H. Erythropoietic protoporphyria exacerbated by oral iron therapy. Br. J. Dermatol. 1988, 119:63-66.
32. Minder E.I., Schneider-Yin X. Porphyrins, porphobilinogen, and δ-aminolevulinic acid. Laboratory Guide to the Methods in Biochemical Genetics 2008, 751-780. Springer, Berlin-Heidelbarg. N. Blau, M. Duran, K. Michael Gibson (Eds.).
33. Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood 1997, 89:1-25.
34. Sadlon T.J., Dell'Oso T., Surinya K.H., May B.K. Regulation of erythroid 5-aminolevulinate synthase expression during erythropoiesis. Int. J. Biochem. Cell Biol. 1999, 31:1153-1167.
35. Sassa S. Modern diagnosis and management of the porphyrias. Br. J. Haematol. 2006, 135:281-292.
36. Schneider-Yin X., Harms J., Minder E.I. Porphyria in Switzerland, 15years experience. Swiss Med. Wkly. 2009, 139:198-206.
37. Shi Z., Ferreira G.C. Modulation of inhibition of ferrochelatase by N-methylprotoporphyrin. Biochem. J. 2006, 399:21-28.
38. Sutherland G.R., Baker E., Callen D.F., et al. 5-Aminolevulinate synthase is at 3p21 and thus not the primary defect in X-linked sideroblastic anemia. Am. J. Hum. Genet. 1988, 43:331-335.
39. Turnbull A., Baker H., Vernon-Roberts B., Magnus I.A. Iron metabolism in porphyria cutanea tarda and in erythropoietic protoporphyria. Q. J. Med. 1973, 42:341-355.
40. Wahlin S., Floderus Y., Stal P., Harper P. Erythropoietic protoporphyria in Sweden: demographic, clinical, biochemical and genetic characteristics. J. Intern. Med. 2011, 269:278-288.