A novel endoproteolytic processing activity in mitochondria of erythroid cells and the role in heme synthesis

Blood

Volumn 96, Issue 2, 2000, Pages 740-746

  Dzikaite, Vijole ^b   Kanopka, Arvydas ^b   Brock, Jeremy H ^b   Kazlauskas, Arunas ^b   Melefors, Öjar ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; ARTICLE; ENZYME ACTIVITY; ERYTHROID CELL; HEME SYNTHESIS; HEMOGLOBIN SYNTHESIS; MITOCHONDRION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION;

EID: 0034661891     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v96.2.740.014k42_740_746     Document Type: Article

References (43)

1. Chen JJ, London IM. Regulation of protein synthesis by heme-regulated elF-2 alpha kinase Trends Biochem Sci. 1995;20:105.
2. Meguro K, Igarashi K, Yamamoto M, Fujita H, Sassa S. The role of the erythroid-specific δ-aminolevulinate synthase gene expression in erythroid heme synthesis. Blood. 1995;86:940.
3. Sassa S, Nagai T. The role of heme in gene expression. Int J Hematol. 1996;63:167.
4. Dierks P. Molecular biology of eukaryotic 5-aminolevulinate synthase. In: Dailey HA, ed. Biosynthesis of Heme and Chlorophylls. New York: McGraw-Hill; 1990:201.
5. Ferreira GC, Gong JJ. 5-Aminolevulinate synthase and the first step of heme biosynthesis. J Bioenerg Biomemb. 1995;27:151.
6. May BK, Dogra SC, Sadlon TJ, Bhasker CR, Cox TC, Bottomley SS. Molecular regulation of heme biosynthesis in higher vertebrates. Prog Nucleic Acids Res Mol Biol. 1995;51:1.
7. Gardner LC, Smith SJ, Cox TM. Biosynthesis of 5-aminolevulinic acid and the regulation of heme formation by immature erythroid cells in man. J Biol Chem. 1991;266:22010.
8. Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood. 1997;89:1.
9. Fujita H, Yamamoto M, Yamagami T, Hayashi N, Sassa S. Erythroleukemia differentiation: distinctive responses of the erythroid-specific and the nonspecific delta-aminolevulinate synthase mRNA. J Biol Chem. 1991;266:17494.
10. Cox TC, Bawden MJ, Martin A, May BK. Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 1991;10:1891.
11. Dandekar T, Stripecke R, Gray NK, Goossen B, Constable A, Johansson HE, Hentze MW. Identification of a novel iron-responsive element in murine and human erythroid δ-aminolevulinic acid synthase mRNA. EMBO J. 1991;10:1903.
12. Hentze MW, Kühn LC. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci U S A. 1996;93: 8175.
13. Haile DJ. Regulation of genes of iron metabolism by iron-response proteins. Am J Med Sci. 1999; 318:230.
14. Rafferty SP, Domachowske JB, Malech HL. Inhibition of hemoglobin expression by heterologous production of nitric oxide synthase in the K562 erythroleukemic cell line. Blood. 1996;88:1070.
15. Weiss G, Houston T, Kastner S, Jöhrer K, Grünewald K, Brock JH. Regulation of cellular iron metabolism by erythropoietin: activation of iron-regulatory protein and upregulation of transferrin receptor expression in erythroid cells. Blood. 1997;89:680.
16. Lathrop JT, Timko MP. Regulation by heme of mitochondrial protein transport through a conserved amino acid motif. Science. 1993;259:522.
17. Ponka P, Schulman HM, Cox TM. Iron metabolism in relation to heme synthesis. In: Dailey HA, ed. Biosynthesis of Heme and Chlorophylls. New York: McGraw-Hill; 1990:393.
18. Ikuta K, Kina T, MacNeil I, et al. A developmental switch in thymic lymphocyte maturation potential occurs at the level of hematopoietic stem cells. Cell. 1990;62:863.
19. Hestdal K, Ruscetti FW, Ihle JN, et al. Characterization and regulation of RB6-8C5 antigen expression on murine bone marrow cells. J Immunol. 1991;147:22.
20. Melefors Ö, Goossen B, Johansson HE, Stripecke R, Gray NK, Hentze MW. Translational control of 5-aminolevulinate synthase mRNA by iron-responsive elements in erythroid cells. J Biol Chem. 1993;268:5974.
21. Melefors Ö. Translational regulation in vivo of the drosophila melanogaster mRNA encoding succinate dehydrogenase iron protein via iron responsive elements. Biochem Biophys Res Comm. 1996;221:437.
22. Larsson NG, Garman JD, Oldfors A, Barsh GS, Clayton DA A single mouse gene encodes the mitochondrial transcription factor A and a testis-specific nuclear HMG-box protein. Nat Genet. 1996;13:296.
23. Hayashi N, Terasawa M, Kikuchi G. Immunochemical studies of the turnover of delta-aminolevulinate synthase in rat liver mitochondria and the effect of hemin on it. J Biochem. 1980;88: 921.
24. Schoenhaut DS, Curtis PJ. Structure of a mouse erythroid 5-aminolevulinate synthase gene and mapping of erythroid specific DNAse I hypersensitive sites. Nucleic Acids Res. 1989;17:7013.
25. Conboy JG, Cox TC, Bottomley SS, Bawden MJ, May BK. Human erythroid 5-aminolevulinate synthase: gene structure and species-specific differences in alternative RNA splicing. J Biol Chem. 1992;267:18753.
26. Smith SJ, Cox TM. Translational control of erythroid δ-aminolevulinate synthase in immature human erythroid cells by heme. Cell Mol Biol. 1997;43:103.
27. Prades E, Chambon C, Dailey TA, Dailey HA, Briére J, Grandchamp B. A new mutation of the ALAS2 gene in a large family with X-linked sideroblastic anemia. Hum Genet. 1995;95:424.
28. Munakata H, Yamagami T, Nagai T, Yamamoto M, Hayashi N. Purification and structure of rat erythroid-specific delta-aminolevulinate synthase. J Biochem. 1993;114:103.
29. Gong J, Kay CJ, Barber MJ, Ferreira GC. Mutations at a glycine loop in aminolevulinate synthase affect pyridoxal phosphate cofactor binding and catalysis. Biochemistry. 1996;35:14109.
30. May BK, Borthwick IA, Srivastava G, Piroia BA, Elliot WH. Control of 5-aminolevulinate synthase in animals. Curr Top Cell Regul. 1986;28:233-262.
31. Furuyama K, Sassa S. Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia. J Clin Invest. 2000;105:757.
32. Gutteridge JM. Free radicals in disease processes: a compilation of cause and consequence. Free Radic Res Commun. 1993;19:141.
33. Cotter PD, May A, Li L, et al. Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. Blood. 1999;93:1757.
34. Furuyama K, Fujita H, Nagai T, et al. Pyridoxine refractory X-linked sideroblastic anemia caused by a point mutation in the erythroid 5-aminolevulinate synthase gene. Blood. 1997;90:822.
35. Houston T, Moore M, Porter D, Sturrock R, Fitzsimons E. Abnormal haem biosynthesis in the chronic anaemia of rheumatoid arthritis. Ann Rheum Dis. 1994;53:167.
36. Schatz G. The protein import system of mitochondria. J Biol Chem. 1996;271:31763.
37. Neupert W. Protein import into mitochondria. Annu Rev Biochem. 1997;66:863.
38. Omura T. Mitochondria-targeting sequence, a multi-role sorting sequence recognized at all steps of protein import into mitochondria. J Biochem. 1998;123:1010.
39. Tanner AJ, Dice JF. Batten disease and mitochondrial pathways of proteolysis. Biochem Mol Med. 1996;57:1.
40. Ito A. Mitochondrial processing peptidase: multiple-site recognition of precursor proteins. Biochem Biophys Res Comm. 1999;265:611.
41. Aoki Y, Urata G, Takaku F, Katunuma N. A new protease inactivating δ-aminolevulinic acid synthetase in mitochondria of human bone marrow cells. Biochem Biophys Res Comm. 1975;65:567.
42. Parley D, Salvesen G, Travis J. Molecular cloning of human neutrophil elastase. Biol Chem Hoppe Seyler. 1988;369:(suppl 3-7).
43. Okano K, Aoki Y, Shimizu H, Naruto M. Functional expression of human leukocyte elastase (HLE)/ medullasin in eukaryotic cells. Biochem Biophys Res Commun. 1990;167:1326.