ALAD porphyria is a conformational disease

American Journal of Human Genetics

Volumn 80, Issue 2, 2007, Pages 329-337

  Jaffe, Eileen K ^a   Stith, Linda ^a  

^a FOX CHASE CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEME; PORPHOBILINOGEN SYNTHASE;

ALZHEIMER DISEASE; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME DEFICIENCY; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; GENE MUTATION; HETEROLOGOUS EXPRESSION; HETEROZYGOTE; HUMAN; ION EXCHANGE CHROMATOGRAPHY; MICHAELIS MENTEN KINETICS; PORPHYRIA; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN QUATERNARY STRUCTURE; RECESSIVE INHERITANCE; SITE DIRECTED MUTAGENESIS; WILD TYPE; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI;

EID: 33846574157     PISSN: 00029297     EISSN: None     Source Type: Journal    
DOI: 10.1086/511444     Document Type: Article

References (47)

1. Sassa S (2002) The porphyrias. Photodermatol Photoimmunol Photomed 18:56-67
2. Doss M, Schmidt A (1972) Zwei Suchteste fur Porphyrein. Z Klin Chem Klin Biochem 10:230-231
3. Battistuzzi G, Petrucci R, Silvagni L, Urbani FR, Caiola S (1981) δ-Aminolevulinate dehydrase: a new genetic polymorphism in man. Ann Hum Genet 45:223-229
4. 2) allele: implications for molecular screening of individuals for genetic susceptibility to lead poisoning. Am J Hum Genet 49:757-763
5. Montenegro MF, Barbosa F Jr, Sandrim VC, Gerlach RF, Tanus-Santos JE (2006) Ethnicity affects the distribution of δ-aminolevulinic acid dehydratase (ALAD) genetic variants. Clin Chim Acta 367:192-195
6. Parra EJ, Ribeiro JC, Caeiro JL, Riveiro A (1995) Genetic structure of the population of Cabo Verde (west Africa): evidence of substantial European admixture. Am J Phys Anthropol 97: 381-389
7. Shen XM, Wu SH, Yan CH, Zhao W, Ao LM, Zhang YW, He JM, Ying JM, Li RQ, Wu SM, et al (2001) Delta-aminolevulinate dehydratase polymorphism and blood lead levels in Chinese children. Environ Res 85:185-190
8. Suzen HS, Duydu Y, Aydin A (2004) Molecular analysis of δ-aminolevulinic acid dehydratase (ALAD) gene polymorphism in a Turkish population. Biochem Genet 42:461-467
9. Wetmur JG, Lehnert G, Desnick RJ (1991) The delta-aminolevulinate dehydratase polymorphism: higher blood lead levels in lead workers and environmentally exposed children with the 1-2 and 2-2 isozymes. Environ Res 56:109-119
10. Weuve J, Kelsey KT, Schwartz J, Bellinger D, Wright RO, Rajan P, Spiro A III, Sparrow D, Aro A, Hu H (2006) Delta-amino-levulinic acid dehydratase (ALAD) polymorphism and the relation between low-level lead exposure and the Mini-Mental Status Examination in older men: the Normative Aging Study. Occup Environ Med 63:746-753
11. Zheng Y, Song W, Wang Y (2001) The gene polymorphism of delta-aminolevulinate dehydratase (ALAD) in 530 cases of Chinese Han population [in Chinese]. Zhonghua Yu Fang Yi Xue Za Zhi 35:16-18
12. Maruno M, Furuyama K, Akagi R, Horie Y, Meguro K, Garbaczewski L, Chiorazzi N, Doss MO, Hassoun A, Mercelis R, et al (2001) Highly heterogeneous nature of δ-aminolevulinate dehydratase (ALAD) deficiencies in ALAD porphyria. Blood 97:2972-2978
13. Akagi R, Inoue R, Muranaka S, Tahara T, Shigeru T, Anderson KE, Phillips JD, Sassa S (2006) Dual gene defects involving δ-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient. Br J Haematol 132:237-243
14. Akagi R, Kato N, Inoue R, Anderson KE, Jaffe EK, Sassa S (2006) δ-Aminolevulinate dehydratase (ALAD) porphyria: the first case in North America with two novel ALAD mutations. Mol Genet Metab 87:329-336
15. Doss MO, Stauch T, Gross U, Renz M, Akagi R, Doss-Frank M, Seelig HP, Sassa S (2004) The third case of Doss porphyria (δ-amino-levulinic acid dehydratase deficiency) in Germany. J Inherit Metab Dis 27:529-536
16. Sakamoto D, Kudo H, Inohaya K, Yokoi H, Narita T, Naruse K, Mitani H, Araki K, Shima A, Ishikawa Y, et al (2004) A mutation in the gene for δ-aminolevulinic acid dehydratase (ALAD) causes hypochromic anemia in the medaka, Oryzias latipes. Mech Dev 121:747-752
17. Akagi R, Nishitani C, Harigae H, Horie Y, Garbaczewski L, Hassoun A, Mercelis R, Verstraeten L, Sassa S (2000) Molecular analysis of δ-aminolevulinate dehydratase deficiency in a patient with an unusual late-onset porphyria. Blood 96:3618-3623
18. Akagi R, Shimizu R, Furuyama K, Doss MO, Sassa S (2000) Novel molecular defects of the δ-aminolevulinate dehydratase gene in a patient with inherited acute hepatic porphyria. Hepatology 31:704-708
19. Gross U, Sassa S, Jacob K, Deybach JC, Nordmann Y, Frank M, Doss MO (1998) 5-Aminolevulinic acid dehydratase deficiency porphyria: a twenty-year clinical and biochemical follow-up. Clin Chem 44:1892-1896
20. Yano Y, Kondo M (1998) ALAD deficiency porphyria (ADP) [in Japanese]. Ryoikibetsu Shokogun Shirizu 19:139-140
21. Sassa S (1998) ALAD porphyria. Semin Liver Dis 18:95-101
22. Fujita H, Ishida N, Akagi R (1995) delta-Aminolevulinate dehydratase deficiency [in Japanese]. Nippon Rinsho 53:1408-1417
23. Sithisarankul P, Schwartz BS, Lee BK, Kelsey KT, Strickland PT (1997) Aminolevulinic acid dehydratase genotype mediates plasma levels of the neurotoxin, 5-aminolevulinic acid, in lead-exposed workers. Am J Ind Med 32:15-20
24. Muraoka A, Suehiro I, Fujii M, Murakami K (1995) delta-Aminolevulinic acid dehydratase deficiency porphyria (ADP) with syndrome of inappropriate secretion of antidiuretic hormone (SIADH) in a 69-year-old woman. Kobe J Med Sci 41:23-31
25. Ishida N, Fujita H, Fukuda Y, Noguchi T, Doss M, Kappas A, Sassa S (1992) Cloning and expression of the defective genes from a patient with δ-aminolevulinate dehydratase poiphyria. J Clin Invest 89:1431-1437
26. Sassa S, Ishida N, Fujita H, Fukuda Y, Noguchi T, Doss M, Kappas A (1992) Cloning and expression of the defective genes in delta-aminolevulinate dehydratase porphyria: compound heterozygosity in this hereditary liver disease. Trans Assoc Am Physicians 105:250-259
27. Thunell S, Holmberg L, Lundgren J (1987) Aminolaevulinate dehydratase porphyria in infancy: a clinical and biochemical study. J Clin Chem Clin Biochem 25:5-14
28. Shemin D, Russell CS, Abramsky T (1955) The succinate-glycine cycle. I. The mechanism of pyrrole synthesis. J Biol Chem 215:613-626
29. Shemin D, Russell CS (1953) δ-Aminolevulinic acid, its role in the biosynthesis of porphyrins and purines. J Am Chem Soc 75:4873-4874
30. Shemin D (1972) δ-Aminolevulinic acid dehydratase. In: Boyer PD (ed) Enzymes. Academic Press, New York, pp 323-337
31. Guo GG, Gu M, Etlinger JD (1994) 240-kDa proteasome inhibitor (CF-2) is identical to δ-aminolevulinic acid dehydratase. J Biol Chem 269:12399-12402
32. Gross M, Hessefort S, Olin A (1999) Purification of a 38-kDa protein from rabbit reticulocyte lysate which promotes protein renaturation by heat shock protein 70 and its identification as δ-aminolevulinic acid dehydratase and as a putative DnaJ protein. J Biol Chem 274:3125-3134
33. Jaffe EK (2000) The porphobilinogen synthase family of metalloenzymes. Acta Crystallogr D Biol Crystallogr 56:115-128
34. Liedgens W, Grutzmann R, Schneider HA (1980) Highly efficient purificaton of the labile plant enzyme 5-aminolevulinate dehydratase (EC 4.2.1.24) by means of monoclonal antibodies. Z Naturforsch [C] 35:958-962
35. Van Heyningen S, Shemin D (1971) Quaternary structure of δ-aminolevulinate dehydratase from Rhodopseudomonas spheroides. Biochemistry 10:4676-4682
36. Breinig S, Kervinen J, Stith L, Wasson AS, Fairman R, Wlodawer A, Zdanov A, Jaffe EK (2003) Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase. Nat Struct Biol 10:757-763
37. Akagi R, Yasui Y, Harper P, Sassa S (1999) A novel mutation of δ-aminolaevulinate dehydratase in a healthy child with 12% erythrocyte enzyme activity. Br J Haematol 106:931-937
38. Tang L, Breinig S, Stith L, Mischel A, Tannir J, Kokona B, Fairman R, Jaffe E (2006) Single amino acid mutations alter the distribution of human porphobilinogen synthase quaternary structure isoforms (morpheeins). J Biol Chem 281: 6682-6690
39. Tang L, Stith L, Jaffe EK (2005) Substrate-induced interconversion of protein quaternary structure isoforms. J Biol Chem 280:15786-15793
40. Jaffe EK (2004) The porphobilinogen synthase catalyzed reaction mechanism. Bioorg Chem 32:316-325
41. Jaffe EK (2005) Morpheeins-a new structural paradigm for allosteric regulation. Trends Biochem Sci 30:490-497
42. Carrell RW, Lomas DA (1997) Conformational disease. Lancet 350:134-138
43. Fishbein L (1998) Transmissible spongiform encephalopathies, hypotheses and food safety: an overview. Sci Total Environ 217:71-82
44. Jaffe EK, Martins J, Li J, Kervinen J, Dunbrack RL Jr (2001) The molecular mechanism of lead inhibition of human porphobilinogen synthase. J Biol Chem 276:1531-1537
45. Jaffe EK, Volin M, Bronson-Mullins CR, Dunbrack RL Jr, Kervinen J, Martins J, Quinlan JF Jr, Sazinsky MH, Steinhouse EM, Yeung AT (2000) An artificial gene for human porphobilinogen synthase allows comparison of an allelic variation implicated in susceptibility to lead poisoning. J Biol Chem 275:2619-2626
46. Ponka P (1999) Cell biology of heme. Am J Med Sci 318:241-256
47. Hamosh A, Scott AF, Amberger J, Valle D, McKusick VA (2000) Online Mendelian Inheritance in Man (OMIM). Hum Mutat 15:57-61