Cloning and expression of rat 25-hydroxyvitamin D ₃ -1α-hydroxylase cDNA

• Toshimasa Shinki

  Department of Biochemistry, School of Dentistry, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142, Japan; Tokyo Research Laboratory, Kyowa Hakko Kogyo Co. Ltd., Asahimachi, Machida, Tokyo 194, Japan; Department of Internal Medicine, University of Keio, Shinanomachi, Shinjuku-ku, Tokyo 160, Japan; and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, 420 Henry Mall, Madison, WI 53706

• Hiroko Shimada

  Department of Biochemistry, School of Dentistry, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142, Japan; Tokyo Research Laboratory, Kyowa Hakko Kogyo Co. Ltd., Asahimachi, Machida, Tokyo 194, Japan; Department of Internal Medicine, University of Keio, Shinanomachi, Shinjuku-ku, Tokyo 160, Japan; and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, 420 Henry Mall, Madison, WI 53706

• Shu Wakino

  Department of Biochemistry, School of Dentistry, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142, Japan; Tokyo Research Laboratory, Kyowa Hakko Kogyo Co. Ltd., Asahimachi, Machida, Tokyo 194, Japan; Department of Internal Medicine, University of Keio, Shinanomachi, Shinjuku-ku, Tokyo 160, Japan; and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, 420 Henry Mall, Madison, WI 53706

• Hideharu Anazawa

  Department of Biochemistry, School of Dentistry, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142, Japan; Tokyo Research Laboratory, Kyowa Hakko Kogyo Co. Ltd., Asahimachi, Machida, Tokyo 194, Japan; Department of Internal Medicine, University of Keio, Shinanomachi, Shinjuku-ku, Tokyo 160, Japan; and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, 420 Henry Mall, Madison, WI 53706

• Matsuhiko Hayashi

  Department of Biochemistry, School of Dentistry, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142, Japan; Tokyo Research Laboratory, Kyowa Hakko Kogyo Co. Ltd., Asahimachi, Machida, Tokyo 194, Japan; Department of Internal Medicine, University of Keio, Shinanomachi, Shinjuku-ku, Tokyo 160, Japan; and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, 420 Henry Mall, Madison, WI 53706

• Takao Saruta

  Department of Biochemistry, School of Dentistry, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142, Japan; Tokyo Research Laboratory, Kyowa Hakko Kogyo Co. Ltd., Asahimachi, Machida, Tokyo 194, Japan; Department of Internal Medicine, University of Keio, Shinanomachi, Shinjuku-ku, Tokyo 160, Japan; and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, 420 Henry Mall, Madison, WI 53706

• Hector F. DeLuca

  Department of Biochemistry, School of Dentistry, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142, Japan; Tokyo Research Laboratory, Kyowa Hakko Kogyo Co. Ltd., Asahimachi, Machida, Tokyo 194, Japan; Department of Internal Medicine, University of Keio, Shinanomachi, Shinjuku-ku, Tokyo 160, Japan; and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, 420 Henry Mall, Madison, WI 53706

• Tatsuo Suda

  Department of Biochemistry, School of Dentistry, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142, Japan; Tokyo Research Laboratory, Kyowa Hakko Kogyo Co. Ltd., Asahimachi, Machida, Tokyo 194, Japan; Department of Internal Medicine, University of Keio, Shinanomachi, Shinjuku-ku, Tokyo 160, Japan; and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, 420 Henry Mall, Madison, WI 53706

抄録

A full-length cDNA for the rat kidney mitochondrial cytochrome P450 mixed function oxidase, 25-hydroxyvitamin D 3 -1α-hydroxylase (P4501α), was cloned from a vitamin D-deficient rat kidney cDNA library and subcloned into the mammalian expression vector pcDNA 3.1(+). When P4501α cDNA was transfected into COS-7 transformed monkey kidney cells, they expressed 25-hydroxyvitamin D 3 -1α-hydroxylase activity. The sequence analysis showed that P4501α was of 2,469 bp long and contained an ORF encoding 501 amino acids. The deduced amino acid sequence showed a 53% similarity and 44% identity to the vitamin D 3 -25-hydroxylase (CYP27), whereas it has 42.6% similarity and 34% identity with the 25-hydroxyvitamin D 3 -24-hydroxylase (CYP24). Thus, it composes a new subfamily of the CYP27 family. Further, it is more closely related to the CYP27 than to the CYP24. The expression of P4501α mRNA was greatly increased in the kidney of vitamin D-deficient rats. In rats with the enhanced renal production of 1α,25-dihydroxyvitamin D 3 (rats fed a low Ca diet), P4501α mRNA was greatly increased in the renal proximal convoluted tubules.

収録刊行物

• Proceedings of the National Academy of Sciences

  Proceedings of the National Academy of Sciences 94 (24), 12920-12925, 1997-11-25

  Proceedings of the National Academy of Sciences

キーワード

• Multidisciplinary

詳細情報

• CRID: 1362825894353740288
• NII論文ID: 80010032768
• DOI: 10.1073/pnas.94.24.12920
• ISSN: 10916490
• ISSN: 00278424
• Web Site: https://pnas.org/doi/pdf/10.1073/pnas.94.24.12920
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