A possible role for CYP27 as a major renal mitochondrial 25-hydroxyvitamin D-3 1 alpha-hydroxylase

被引：10

作者：

Araya, Z

Norlin, M

Postlind, H

机构：

[1] Division of Biochemistry, Dept. of Pharmaceutical Biosciences, University of Uppsala

来源：

FEBS LETTERS | 1996年 / 390卷 / 01期

关键词：

cytochrome P450; renal mitochondrial 1 alpha-hydroxylation; 24-hydroxylation;

D O I：

10.1016/0014-5793(96)00617-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A mitochondrial cytochrome P450 fraction catalyzing 1 alpha- and 27-hydroxylation but not 24-hydroxylation of 25-hydroxyvitamin D-3 was purified from pig kidney. The ratio between the 1 alpha- and 27-hydroxylase activities was the same in all purification steps including a side fraction. Attempts to separate the 1 alpha- and 27-hydroxylase activities were unsuccessful. A monoclonal antibody directed against purified pig liver CYP27 recognized a protein of the same apparent M(r) and immunoprecipitated both the 1 alpha- and 27-hydroxylase activities towards 25-hydroxyvitamin D-3 in the purified kidney enzyme fraction as well as in a solubilized, crude cytochrome P450 extract considered to represent the major part of the 25-hydroxyvitamin D-3 hydroxylases in kidney mitochondria. Taken together, the results from the purification and the experiments with CYP27 antibody, substrate inhibition, and recombinant expressed human liver CYP27 strongly indicate that CYP27 is able to catalyze 1 alpha-hydroxylation but not 24-hydroxylation of 25-hydroxyvitamin D-3 in kidney. In conclusion, the results provide evidence for a role for CYP27 as major renal mitochondrial 25-hydroxyvitamin D-3 1 alpha-hydroxylase.

引用

页码：10 / 14

页数：5

共 29 条

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ANDERSSON S, 1989, J BIOL CHEM, V264, P8222

[2]

ANDERSSON S, 1986, J BIOL CHEM, V261, P6932

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