A novel compound heterozygous mutation of K494_V495 deletion plus R496L and D487_F489 deletion in extreme C-terminus of cytochrome P450c17 causes 17α-hydroxylase deficiency

Molecular and Cellular Endocrinology

Volumn 249, Issue 1-2, 2006, Pages 16-20

  Lee, Long Shyong ^a   Shu, Wei Jane ^a   Wu, Chen Ming ^a   Hsieh, Chia Hsing ^a   Chen, Su Mei ^a   Hu, Chaur Jong ^a   Chen, Wei Yi ^b   Chung, Bon chu ^b  

^a TAIPEI CITY HOSPITAL   (Taiwan)

^b INSTITUTE OF MOLECULAR BIOLOGY   (Taiwan)

Author keywords

17 Hydroxylase deficiency; Congenital adrenal hyperplasia; CYP17; Mutation

Indexed keywords

CYTOCHROME P450C17; STEROID 17,20 LYASE; STEROID 17ALPHA MONOOXYGENASE;

ADULT; ALLELE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CASE REPORT; CLINICAL FEATURE; CODON; CONGENITAL ADRENAL HYPERPLASIA; DIAGNOSTIC TEST; DISEASE COURSE; EMBRYO; ENZYME ACTIVITY; ENZYME DEFICIENCY; FEMALE; GENE DELETION; GENE MUTATION; GENE SEQUENCE; HUMAN; HUMAN CELL; LABORATORY TEST; MISSENSE MUTATION; NUCLEOTIDE SEQUENCE; PHYSICAL EXAMINATION; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; STEROID 17ALPHA MONOOXYGENASE DEFICIENCY;

ADRENAL HYPERPLASIA, CONGENITAL; ADULT; ALLELES; CELL LINE; DNA MUTATIONAL ANALYSIS; FEMALE; HUMANS; MUTAGENESIS, SITE-DIRECTED; PEDIGREE; RARE DISEASES; SEQUENCE DELETION; STEROID 17-ALPHA-HYDROXYLASE; TAIWAN;

EID: 33645858285     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2006.01.003     Document Type: Article

References (25)

1. 5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer. J. Biol. Chem. 273 (1998) 3158-3165
2. Auchus R.J., and Miller W.L. Molecular modeling of human P450c17 (17α-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol. Endocrinol. 13 (1999) 1169-1182
3. Auchus R.J. The genetics, pathophysiology, and management of human deficiencies of P450c17. Endocrinol. Metab. Clin. N. Am. 30 (2001) 101-119
4. Biason-Lauber A., Kempken B., Weder E., Forest M.G., Einaudi S., Ranke M.B., Matsuo N., Brunelli V., Schönle E.J., and Eachmann M. 17α-Hydroxylase/17,20-lyase as a model to study enzymatic activity regulation: role of phosphorylation. J. Clin. Endocrinol. Metab. 85 (2000) 1226-1231
5. Biglieri E.G., Herron M.A., and Brust N. 17-Hydroxylation deficiency in man. J. Clin. Invest. 45 (1966) 1946-1954
6. Chung B.C., Picado-Lenonard J., Haniu M., Bienkowski M., Hall P.F., Shively J.E., and Miller W.L. Cytochrome P450c17 (steroid 17α-hydroxylase/17,20-lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc. Natl. Acad. Sci. U.S.A. 84 (1987) 407-411
7. Costa-Santos M., Kater C.E., Dias E.P., and Auchus R.J. Two intronic mutations cause 17-hydroxylase deficiency by disrupting splice acceptor sites: direct demonstration of aberrant splicing and absent enzyme activity by expression of the entire CYP17 gene in HEK-293 cells. J. Clin. Endocrinol. Metab. 89 (2004) 43-48
8. Costa-Santos M., Kater C.E., Archus R.J., and Brazilian Congenital Adrenal Hyperplasia Multicenter Study Group. Two prevalent CYP17 mutations and genotype-phenotype correlations in 24 Brazilian patients with 17α-hydroxylase. J. Clin. Endocrinol. Metab. 89 (2004) 49-60
9. 17α) to 10q24.3 by fluorescence in situ hybridization and simultaneous chromosome banding. Genomics 14 (1992) 1110-1111
10. 489 in human cytochrome P450c17 causes 17α-hydroxylase deficiency. J. Clin. Endocrinol. Metab. 77 (1993) 489-493
11. Fardella C.E., Hum D.W., Homoki J., and Miller W.L. Point mutation of Arg 440 to His in cytochrome P450c17 causes severe 17α-hydroxylase deficiency. J. Clin. Endocrinol. Metab. 79 (1994) 160-164
12. Geller D.H., Auchus R.J., Mendonca B.B., and Miller W.L. The Genetic and functionl basis of isolated 17,20-lyase deficiency. Nat. Genet. 17 (1997) 201-205
13. Imai T., Yanase T., Waterman M.R., Simpson E.R., and Pratt J.J. Canadian mennonites and individuals residing in Friesland region of the Netherlands share the same molecular basis of 17α-hydroxylase deficiency. Hum. Genet. 89 (1992) 95-96
14. Kater C.E., and Biglieri E.G. Disorders of steroid 17α-hydroxylase deficiency. Endocrinol. Metab. Clin. N. Am. 23 (1994) 341-357
15. Lam C.W., Arlt W., Chan C.K., Honour J.W., Lin C.J., Tong S.F., Choy K.W., and Miller W.L. Mutation of proline 409 to arginine in the meander region of cytochrome P450c17 causes severe 17α-hydroxylase deficiency. Mol. Genet. Metab. 72 (2001) 254-259
16. 5: endocrinological and mechanistic implications. Biochem. J. (1995) 901-908
17. Miller W.L. Editorial: steroid 17α-hydroxylase deficiency-not rare everywhere. J. Clin. Endocrinol. Metab. 89 (2004) 40-42
18. Monno S., Mizushima Y., Toyoda N., Kashii T., and Kobayashi M. A new variant of the cytochrome P450c17 (CYP17) gene mutation in the three patients with 17α-hydroxylase deficiency. Ann. Hum. Genet. 61 (1997) 275-279
19. Oshiro C., Takasu N., Wakugami T., Komiya I., Yamada T., Eguchi Y., and Takei H. 17α-Hydroxylase deficiency with one base pair deletion of the cytochrome P450c17 (CYP17) gene. J. Clin. Endocrinol. Metab. 80 (1995) 2526-2529
20. Picado-Leonard J., and Miller W.L. Cloning and sequence of the human gene for P450c17 (steroid 17α-hydroxylase/17,20-lyase): similarity with the gene for P450c21. DNA 6 (1987) 439-448
21. 489 deletion in human cytochrome P450c17 causes 17α-hydroxylase/17,20-lyase deficiency in three Chinese sisters. Mol. Cell. Endocrinol. 201 (2003) 189-195
22. Takeda Y., Yoneda T., Demura M., Furukawa K., Koshida H., Miyamori I., and Mabuchi H. Genetic analysis of the cytochrome P-450c17α (CYP17) and aldosterone synthase (CYP11B2) in Japanese patients with 17α-hydroxylase deficiency. Clin. Endocrinol. 54 (2001) 751-758
23. Wu D.A., and Chung B.C. Mutations of P450c21 (steroid 21-hydroxylase) at Cys428, Val1281, and Ser268 results in complete, partial, or no loss of enzymatic activity, respectively. J. Clin. Invest. 88 (1991) 519-523
24. Yanase T., Waterman M.R., Zachmann M., Winter J.S.D., Simpson E.R., and Kagimoto M. Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)→Cys, Gln(461)→stop) actually cause combined 17α-hydroxylase/17,20-lyase deficiency. Biochem. Biophys. Acta 1139 (1992) 275-279
25. Yanase T. 17α-Hydroxylase/17,20-lyase defects. J. Steroid Biochem. Mol. Biol. 53 (1995) 153-157