Molecular Cloning of cDNA and Genomic DNA for Human 25-hydroxyvitamin D₃1α-hydroxylase

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• 作者：Monkawa ; Toshiaki ; Yoshida ; Tadashi ; Wakino ; Shu ; Shinki ; Toshimasa ; Anazawa ; Hideharu ; Deluca ; Hector F. ; et. al.
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：1997
• 出版时间：October 20, 1997
• 年：1997
• 卷：239
• 期：2
• 页码：527-533
• 全文大小：280 K

文摘

The 25-hydroxyvitamin D₃1α-hydroxylase (1α-hydroxylase) is a cytochrome P450 enzyme that catalyzes the conversion of 25-hydroxyvitamin D₃to 1α,25-dihydroxyvitamin D₃. This enzyme plays an important role in calcium homeostasis. Here we report the molecular cloning of cDNA and gene for human 1α-hydroxylase. The cDNA clone was obtained from a human kidney cDNA library by cross-hybridization with a previously cloned rat cDNA probe. The cDNA consists of 2469 bp and encodes a protein of 508 amino acids that shows 82.5 % sequence identity with the rat enzyme. A computer-aided homology search revealed that 1α-hydroxylase shares a relatively high homology with vitamin D₃25-hydroxylase (about 40 % amino acid identity). Northern blot analysis showed that the 2.5-kb mRNA is most abundant in kidney. The gene for human 1α-hydroxylase spans approximately 6 kb, is composed of nine exons, and is present as a single copy. This molecular cloning makes it possible to investigate the genetic mechanism of diseases related to calcium metabolism, including vitamin D-dependency rickets type I.