Mutational analysis of CYP27A1: assessment of 27-hydroxylation of cholesterol and 25-hydroxylation of vitamin D

Metabolism: Clinical and Experimental

Volumn 56, Issue 9, 2007, Pages 1248-1255

  Gupta, Ram P ^a   Patrick, Kennerly ^b   Bell, Norman H ^a  

^a MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

^b MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

25 HYDROXYVITAMIN D; COLECALCIFEROL; COMPLEMENTARY DNA; CYTOCHROME P450; CYTOCHROME P450 CYP27 A1; UNCLASSIFIED DRUG; VITAMIN D;

ARTICLE; AUTOSOMAL RECESSIVE DISORDER; BIOSYNTHESIS; CEREBROTENDINOUS XANTHOMATOSIS; ESCHERICHIA COLI; GENE MUTATION; HYDROXYLATION; MUTATIONAL ANALYSIS; OSTEOPOROSIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; VITAMIN D DEFICIENCY;

AMINO ACID SEQUENCE; ANIMALS; CERCOPITHECUS AETHIOPS; CHOLESTEROL; COS CELLS; CYTOCHROME P-450 CYP27A1; DNA MUTATIONAL ANALYSIS; HUMANS; HYDROXYLATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; TRANSFECTION; VITAMIN D; XANTHOMATOSIS, CEREBROTENDINOUS;

EID: 34547699510     PISSN: 00260495     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.metabol.2007.04.023     Document Type: Article

References (34)

1. Oftebro H., Saarem K., Bjorkhem I., et al. Side chain hydroxylation of C27-steroids and vitamin D3 by a cytochrome P-450 enzyme system isolated from human liver mitochondria. J Lipid Res 22 (1981) 1254-1264
2. Saarem K., Bergseth S., Oftebro H., et al. Subcellular localization of vitamin D3 25-hydroxylase in human liver. J Biol Chem 259 (1984) 10936-10940
3. Guo Y.-D., Strugnell S., Back D.W., et al. Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions. Proc Natl Acad Sci U S A 90 (1993) 8668-8672
4. Sawada N., Sakaki T., Ohta M., et al. Metabolism of vitamin D(3) by human CYP27A1. Biochem Biophys Res Commun 273 (2000) 977-984
5. Cheng J.B., Motola D.L., Mangelsdorf D.J., et al. Deorphanization of cytochrome P450 CYP2R1, a microsomal vitamin D 25-hydroxylase. J Biol Chem 278 (2003) 38084-38093
6. Shinkyo R., Sakaki T., Kamakura M., et al. Metabolism of vitamin D by human microsomal CYP2R1. Biochem Biophys Res Commun 324 (2004) 451-457
7. Cheng J.B., Levine M.A., Bell N.H., et al. Genetic evidence that human CYP2R1 is a key vitamin D 25-hydroxylase. Proc Natl Acad Sci U S A 101 (2005) 711-715
8. Dong Q., and Miller W. Vitamin D 25-hydroxylase deficiency. Mol Genet Metab 83 (2004) 197-198
9. Fuchs M. Bile acid regulation of hepatic physiology: III. Regulation of bile acid synthesis: past progress and future challenges. Am J Physiol Gastrointest Liver Physiol 284 (2003) 551-557
10. Cali J.J., and Russell D.W. Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis. J Biol Chem 266 (1991) 7774-7778
11. Pikuleva I.A., Babiker A., Waterman M.R., et al. Activities of recombinant human cytochrome P450c27 (CYP27) which produce intermediates of alternative bile acid biosynthetic pathways. J Biol Chem 273 (1981) 18153-18160
12. Cali J.J., Hsieh C.L., Francke U., et al. Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis. J Biol Chem 266 (1991) 7779-7783
13. Verrips A., Hoefsloot L.H., Steenbergen G.C.H., et al. Clinical and molecular genetic characteristics of cerebrotendinous xanthomatosis. Brain 123 (2000) 908-919
14. Lee M.H., Hazard S., Carpten J.D., et al. Fine-mapping, mutation analyses, and structural mapping of cerebrotendinous xanthomatosis in U.S. pedigrees. J Lipid Res 42 (2001) 159-169
15. Berginer V.M., Shany S., Aklalay D., et al. Osteoporosis and increased bone fractures in cerebrotendinous xanthomatosis. Metabolism 42 (1993) 69-74
16. Federico A., Dotti M.T., Lore F., et al. Cerebrotendinous xanthomatosis: pathophysiological study on bone metabolism. J Neurol Sci 115 (1993) 67-70
17. Sagara Y., Hara T., Ariyasu Y., et al. Direct expression in Escherichia coli and characterization of bovine adrenodoxins with modified amino-terminal regions. FEBS Lett 300 (1992) 208-212
18. Sagara Y., Wada A., Takata Y., et al. Direct expression of adrenodoxin reductase in Escherichia coli and the functional characterization. Bio Pharm Bull 16 (1993) 627-637
19. Murtazina D., Puchkaev A.V., Schein C.H., et al. Membrane-protein interactions contribute to efficient 27-hydroxylation of cholesterol by mitochondrial cytochrome P450 27A1. J Biol Chem 277 (2002) 37582-37589
20. Pikuleva I.A., Cao C., and Waterman M.R. An additional electrostatic interaction between adrenodoxin and P450c27 (CYP27A1) results in tighter binding than between adrenodoxin and p450scc (CYP11A1). J Biol Chem 274 (2002) 2045-2052
21. Omura T., and Sato R. The carbon monoxide-binding pigment of liver microsomes II. Solubilization, purification and properties. J Biol Chem 239 (1964) 2379-2385
22. Smith P.K., Krohn R.I., Hermanson G.T., et al. Measurement of protein using bicinchoninic acid. Anal Biochem 150 (1985) 76-85
23. Gupta R.P., Hollis B.W., Patel S.P., et al. CYP3A4 is a human microsomal vitamin D-25-hydroxylase. J Bone Miner Res 19 (2004) 680-688
24. Gupta R.P., He Y.A., Patrick K.S., et al. CYP3A4 is a vitamin D-24- and 25-hydroxylase: analysis of structure function by site-directed mutagenesis. J Clin Endocrinol Metab 90 (2005) 1210-1219
25. Prosser D.E., and Jones G. Enzymes involved in the activation and inactivation of vitamin D. Trends Biochem Sci 29 (2004) 664-673
26. Prosser D.E., Guo Y.D., Jia Z., et al. Structural motif-based homology modeling of CYP27A1 and site-directed mutational analyses affecting vitamin D hydroxylation. Biophys J 90 (2006) 3389-3409
27. Axelson M., and Larsson O. Low density lipoprotein (LDL) cholesterol is converted to 27-hydroxycholesterol in human fibroblasts. Evidence that 27-hydroxycholesterol can be an important intracellular mediator between LDL and the suppression of cholesterol production. J Biol Chem 270 (1995) 15102-15110
28. Chen W., Kubota S., Kim K.-S., et al. Alternative pre-mRNA splicing of the sterol 27-hydroxylase gene (CYP 27) caused by a G to A mutation at the last nucleotide of exon 6 in a patient with cerebrotendinous xanthomatosis (CTX). J Lipid Res 38 (1997) 870-879
29. Sawada N., Sakaki T., Kitanaka S., et al. Structure-function analysis of CYP27B1 and CYP27A1. Studies on mutants from patients with vitamin D-dependent rickets type I (VDDR-I) and cerebrotendinous xanthomatosis (CTX). Eur J Biochem 268 (2001) 6607-6615
30. Mast N., Murtazina D., Liu H., et al. Distinct binding of cholesterol and 5β-cholestane-3α,7α,12α-triol to cytochrome P450-27A1: Evidence from modeling and site-directed mutagenesis studies. Biochemistry 45 (2006) 4396-4404
31. Hasemann C.A., Kurumbail R.G., Bodddupalli S.S., et al. Structure and function of cytochromes P450: a comparative analysis of three crystal structures. Structure 3 (1995) 41-62
32. Clements M.R., Chalmers T.M., and Fraser D.R. Enterohepatic circulation of vitamin D: a reappraisal of the hypothesis. Lancet 1 (1984) 1376-1379
33. Gascon-Barre M., Demers C., Ghrab O., et al. Expression of CYP27A, a gene encoding a vitamin D-25 hydroxylase in human liver and kidney. Clin Endocrinol 54 (2001) 107-115
34. Chen W., Kubota S., Ujike H., et al. A novel Arg362Ser mutation in the sterol 27-hydroxylase gene (CYP27): its effects on pre-mRNA splicing and enzyme activity. Biochemistry 37 (1998) 15050-15056