A case of methemoglobinemia type II due to NADH-cytochrome b5 reductase deficiency: Determination of the molecular basis

Human Mutation

Volumn 16, Issue 1, 2000, Pages 18-22

  Aalfs, Cora M ^a   Salieb Beugelaar, Georgette B ^a   Wanders, Ronald J A ^a   Mannens, Marcel M A M ^a   Wijburg, Frits A ^a  

^a ACADEMIC MEDICAL CENTER   (Netherlands)

Author keywords

DIA1; Diaphorase; Methemoglobinemia type II; Molecular analysis; NADH cytochrome b5 reductase

Indexed keywords

CYTOCHROME B5 REDUCTASE; METHEMOGLOBIN;

ARTICLE; CASE REPORT; CHROMOSOME 22; ENZYME DEFICIENCY; FEMALE; GENE LOCATION; GENE MUTATION; HEREDITARY METHEMOGLOBINEMIA; HUMAN; INFANT; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL;

CHILD; CHROMOSOMES, HUMAN, PAIR 22; CODON, TERMINATOR; CYTOCHROME REDUCTASES; CYTOCHROME-B(5) REDUCTASE; DNA MUTATIONAL ANALYSIS; DNA PRIMERS; EXONS; FEMALE; HUMANS; METHEMOGLOBINEMIA; MUTAGENESIS, SITE-DIRECTED; MUTATION; POLYMORPHISM, SINGLE-STRANDED CONFORMATIONAL; RESTRICTION MAPPING;

EID: 0033948250     PISSN: 10597794     EISSN: None     Source Type: Journal    
DOI: 10.1002/1098-1004(200007)16:1<18::AID-HUMU4>3.0.CO;2-N     Document Type: Article

References (23)

1. Fisher RA, Povey S, Bobrow M, Solomon E, Boyd Y, Carritt B. 1977. Assignment of the DIA-1 locus to chromosome 22. Ann Hum Genet 41:151-155.
2. François. 1845. Cas de cyanose congéniale sans cause apparente. Bull Acad Roy Med Belg 4:698.
3. Golterman LK, Maaswinkel-Mooy PD. 1989. Een zuigeling met erfelijke methemoglobinemie. Ned Tijdschr Geneesk 57:60-62.
4. Higasa K, Manabe J-I, Yubusui T, Sumimoto H, Pung-Amritt P, Tanphaichitr VS, Fukumaki Y. 1998. Molecular basis of hereditary methaemoglobinaemia, types I and II: two novel mutations in the NADH-cytochrome b5 reductase gene. Br J Haematol 102:922-930.
5. Jaffé ER, Neumann G, Rothberg H, Wilson T, Webster RM, Wolff JA. 1966. Hereditary methemoglobinemia with and without mental retardation. Am J Med 41:42-55.
6. Jaffé ER, Hultquist DE. 1995. Cytochrome b5 reductase deficiency and enzymopenic hereditary methemoglobinemia. In: The metabolic and molecular bases of inherited disease. Scriver CR, Beaudet AL, Sly WS, Valle D, eds. New York: McGraw-Hill, Inc. p 3399-3415.
7. Jenkins MM, Prchal JT. 1996. A novel mutation found in the 3′domain of NADH-cytochrome b5 reductase in an African-American family with type I congenital methemoglobinemia. Blood 87:2993-2999.
8. Kaftory A, Freundlich E, Manaster J, Shukri A, Hegesh E. 1986. Prenatal diagnosis of congenital methemoglobinemia with mental retardation. Israel J Med Sci 22:837-840.
9. Katubse T, Sakamoto N, Kobayashi Y, Seki R, Hirano M, Tanishima K, Tomoda A, Takazakura E, Yubisui T, Takeshita M, Sakaki Y, Fukumaki Y. 1991. Exonic point mutations in NADH-cytochrome b5 reductase genes of homozygotes for hereditary methemoglobinemia types I and III: putative mechanisms of tissue dependent enzyme deficiency. Am J Hum Genet 48:799-808.
10. Keyes SR, Cinti DL. 1980. Biochemical properties of cytochrome b5 dependent microsomal fatty acid elongation and identification of products. J Biol Chem 255:11357-11364.
11. Kobayashi Y, Fukumaki Y, Yubisui T, Inoue J, Sakaki Y. 1990. Serine-proline replacement at residue 127 of NADH-cytochrome b5 reductase causes hereditary methemoglobinemia, generalized type. Blood 75:1408-1413.
12. Manabe J, Arya R, Sumimoto H, Yubisui T, Bellingham A, Layton DM, Fukumaki Y. 1996. Two novel mutations in the reduced nicotinamide adenine dinucleotide (NADH)-cytochrome b5 reductase gene of a patient with generalized type, hereditary methemoglobinemia. Blood 88:3208-3215.
13. Nagai T, Shirabe K, Yubisui T, Takeshita M. 1993. Analysis of mutant NADH-cytochrome b5 reductase: Apparent Atype III@ methemoglobinemia can be explained as type I with an unstable reductase. Blood 81:808-814.
14. Owen EP, Berens J, Marinaki AM, Ipp H, Harley EH. 1997. Recessive congenital methemoglobinemia type II, a new mutation which causes incorrect splicing in the NADH-cytochrome b5 reductase gene. J Inher Metab Dis 20:610.
15. Pietrini G, Aggujaro D, Carrera P, Malyszko J, Vitale A, Borgese N. 1992. A single mRNA, transcribed from an alternative, erythroid-specific promoter, codes for two non-myristylated forms of NADH-cytochrome b5 reductase. J Cell Biol 117:975-986.
16. Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning; a laboratory manual. 2nd ed. New York: Cold Spring Harbor.
17. Schafer DA, Hultquist DE. 1981. Isolation of an acid protease from rabbit reticulocytes and evidence for its role in processing redox proteins during erythroid maturation. Biochem Biophys Res Commun 100:1555.
18. Shirabe K, Yubisui T, Borgese N, Tang C, Hultquist DE, Takeshita M. 1992. Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). J Biol Chem 267:20416-20421.
19. Shirabe K, Fujimoto Y, Yubisui T, Takeshita M. 1994. An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). J Biol Chem 269:5952-5957.
20. Shirabe K, Landi MT, Takeshita M, Uziel G, Fedrizzi E, Borgese N. 1995. A novel point mutation in a 3′ splice site of the NADH-cytochrome b5 reductase gene results in immunologically undetectable enzyme and impaired NADH-dependent ascorbate regeneration in cultured fibroblasts of a patient with type II hereditary methemoglobinemia. Am J Hum Genet 57:302-310.
21. Tomatsu S, Kobayashi Y, Fukumaki Y, Yubisui T, Orii T, Sakaki Y. 1989. The organization and the complete nucleotide sequence of the human NADH-cytochrome b5 reductase gene. Gene 80:353-361.
22. Viera LM, Kaplan JC, Kahn A, Leroux A. 1995. Four new mutations in the NADH-cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II. Blood 85:2254-2262.
23. Wu Y-S, Huang C-H, Wan Y, Huang Q-J, Zhu Z-Y. 1998. Identification of a novel point mutation (Leu72Pro) in the NADH-cytochrome b5 reductase gene of a patient with hereditary methaemoglobinaemia typeI. Br J Haematol 102:575-577.