Compound heterozygosity of two missense mutations in the NADH-cytochrome b5 reductase gene of a Polish patient with type I recessive congenital methaemoglobinaemia

European Journal of Haematology

Volumn 70, Issue 6, 2003, Pages 404-409

  Grabowska, Dorota ^a   Plochocka, Danuta ^a   Jablonska Skwiecinska, Ewa ^b   Chelstowska, Anna ^a   Lewandowska, Irmina ^a   Staniszewska, Krystyna ^b   Majewska, Zofia ^b   Witos, Iwona ^b   Burzynska, Beata ^a  

^a INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

^b MEDICAL CENTER FOR POSTGRADUATE EDUCATION   (Poland)

Author keywords

b5R; Methaemoglobinaemia; Molecular modelling; Mutation

Indexed keywords

CYTOCHROME B5 REDUCTASE; ISOLEUCINE; THREONINE;

AMINO ACID SUBSTITUTION; ARTICLE; AUTOSOMAL RECESSIVE INHERITANCE; CATALYSIS; ENZYME DEFICIENCY; ERYTHROCYTE MEMBRANE; HEREDITARY METHEMOGLOBINEMIA; HETEROZYGOSITY; HUMAN; HUMAN CELL; MISSENSE MUTATION; MOLECULAR MODEL; POLAND; PRIORITY JOURNAL; PROTEIN STRUCTURE; RECEPTOR GENE;

ADULT; AMINO ACID SEQUENCE; CYTOCHROME REDUCTASES; CYTOCHROME-B(5) REDUCTASE; DNA MUTATIONAL ANALYSIS; FAMILY HEALTH; HETEROZYGOTE; HUMANS; MALE; METHEMOGLOBINEMIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION, MISSENSE; PEDIGREE; POLAND; SEQUENCE ALIGNMENT;

EID: 0038133424     PISSN: 09024441     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0609.2003.00070.x     Document Type: Article

References (20)

1. SCOTT EM, GRIFFITH IV. The enzymatic defect of hereditary methemoglobinemia: diaphorase. Biochim Biophys Acta 1959;34:584-586.
2. LEROUX A, JUNIEN C, KAPLAN J-C, BAMBERGER J. Generalized deficiency of cytochrome b5 reductase in congenital methaemoglobinaemia with mental retardation. Nature. 1975;258:619-620.
3. SHIRABE K, YUBISUI T, BORGESE N, TANG CY, HULTQUIST DE, TAKESHITA M. Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). J Biol Chem 1992;267:20416-20421.
4. HIGASA K, MANABE JI, YUBIDUI T, SUMIMOTO H, PUNGAMRITT P, TANPHAICHITR VS, FUKUMAKI Y. Molecular basis of hereditary methaemoglobinaemia, types I and II: two novel mutations in the NADH-cytochrome b5 reductase gene. Br J Haematol 1998;103:922-930.
5. DEKKER J, EPPINK MHM, van ZWIETEN R, de RIJK T, REMACHA AF, LAW LK, LI AM, CHEUNG KL, van BERKEL WJH, ROOS D. Seven new mutations in the nicotinamide adenine dinucieotide reduced-cytochrome b5 reductase gene leading to methemoglobinemia type I. Biood 2001;97:1106-1114.
6. 2-terminal structures of human and rat liver microsomal NADH-cytochrome b5 reductase. J Biochem 1989;105:312-317.
7. YUBISUI T, MIYATA T, IWANAGA S, TAMURA M, TAKESHITA M. Complete amino acid sequence of NADH-cytochrome b5 reductase purified from human erythrocytes. J Biochem 1986;99:407-422.
8. NISHIDA H, INAKA K, YMANAKA M, KAIDA S, KOBAYASHI K, MIKI K. Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 Å resolution. Biochemistry 1995;34:2763-2767.
9. BEWLEY MC, MAROHNIC CHC, BARBER MJ. The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent. Biochemistry 2001;40:13574-13582.
10. LU G, LINDQVIST Y, SCHNEIDER G, DWIVEDI U, CAMPBELL W. Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 Å, its ADP complex and an active-site mutant and modeling of the cytochrome b domain. J Mol Biol 1995;248:931-948.
11. EVELYN KA, MALLOY HT. Microdetermination of oxyhemoglobin, methemoglobin and sulfhemoglobin in a single sample of blood. J Biol Chem 1938;126:655-662.
12. BEUTLER E. Red Cell Metabolism; A Manual of Biochemical Methods. Orlando, FL: Grune and Stratton, 1984:81-82.
13. GUEX N, PEITSCH MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis 1997;18:2714-2723.
14. PEITSCH MC. Protein modeling by e-mail. Bio/Technology 1995;13:658-660.
15. PEITSCH MC. ProMod and Swiss-model: internet-based tools for automated comparative protein modelling. Biochem Soc Trans 1996;24:274-279.
16. WANG Y, WU YS, ZHENG PZ, YANG WX, FANG GA, TANG YC, XIE F, LAN FH, ZHU ZY. A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia. Blood. 2000;95:3250-3255.
17. TOMATSU S, KOBAYASHI Y, FUKUMAKI Y, YUBISUI T, ORII T, SAKAKI Y. The organization and the complete nucleotide sequence of the human NADH cytochrome b5 reductase gene. Gene 1989;80:353-361.
18. PERCY MJ, GILLESPIE MJ, SAVAGE G, HUGHES AE, MCMULLIN MF, LAPPIN TR. Familial idiopathic methemoglobinemia revisited: original cases reveal 2 novel mutations in NADH-cytochrome b5 reductase. Blood 2002;100:3447-3449.
19. AALFS CM, SALIEB-BEUGELAAR GB, WANDERS RJ, MANNENS MM, WIJBURG FA. A case of methemoglobinemia type II due to NADH-cytochrome b5 reductase deficiency: determination of the molecular basis. Hum Mutat 2000;16:18-22.
20. KUGLER W, PEKRUN A, LASPE P, ERDLENBRUCH B, LAKOMEK M. Molecular basis of recessive congenital methemoglobinemia, types I and II: exon skipping and three novel missense mutations in the NADH-cytochrome b5 reductase (diaphorase 1) gene. Hum Murat 2001;17:348.