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Mouse Vitamin D-24-Hydroxylase: Molecular Cloning, Tissue Distribution, and Transcriptional Regulation by 1,25-Dihydroxyvitamin D₃¹

Department of Biochemistry, Ohu University School of Dentistry, Koriyama 963, Japan

Address all correspondence and requests for reprints to: Noboru Horiuchi, Department of Biochemistry, Ohu University School of Dentistry, Koriyama 963, Japan.

Vitamin D-24-hydroxylase (24-OHase) is a cytochrome P-450 enzyme that catalyzes the conversion of 25-hydroxyvitamin D₃ (25OHD₃) and 1,25-dihydroxyvitamin D₃ [1,25-(OH)₂D₃] to 24,25-dihydroxyvitamin D₃ and 1,24,25-trihydroxyvitamin D₃, respectively. A full-length complementary DNA for mouse 24-OHase has now been characterized. The complementary DNA consists of 3309 bp and encodes a protein of 514 amino acids that shows 82% and 95% sequence identity with the human and rat enzymes, respectively. Northern blot analysis of tissues from mice injected with 1,25-(OH)₂D₃ (24 pmol/g) revealed that the 3.4-kb 24-OHase messenger RNA (mRNA) is most abundant in kidney and intestine, with smaller amounts present in skin, thymus, and bone. RT-PCR and Southern blot analysis detected 24-OHase mRNA in several other tissues including lung, testis, spleen, pancreas, and heart. Intraperitoneal injection of 1,25-(OH)₂D₃ induced dose- and time-dependent increases in both 24-OHase mRNA abundance and enzyme activity in mouse kidney. Similarly, 1,25-(OH)₂D₃-induced increases in both 24-OHase mRNA and activity were apparent in the duodenum. Although 1,25-(OH)₂D₃ increased the amount of 24-OHase mRNA in skin, enzyme activity was not detected in this tissue. Pretreatment of mice with cycloheximide (400 µg/g), an inhibitor of protein synthesis, potentiated the increase in 24-OHase mRNA abundance, but blocked the increase in 24-OHase activity, induced by 1,25-(OH)₂D₃ in kidney and duodenum, suggesting that 24-OHase gene expression may be regulated not only by the vitamin D receptor but also by a short-lived repressor protein.

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