TY - JOUR
T1 - Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1α-hydroxylase
AU - Monkawa, Toshiaki
AU - Yoshida, Tadashi
AU - Wakino, Shu
AU - Shinki, Toshimasa
AU - Anazawa, Hideharu
AU - DeLuca, Hector F.
AU - Suda, Tatsuo
AU - Hayashi, Matsuhiko
AU - Saruta, Takao
N1 - Funding Information:
This work was supported in part by grants from the Ministry of Education, Science and Culture of Japan, and a Research Fellowship of the Japan Society for the Promotion of Science for Young Scien- tists. T. M. is a Research Fellow of the Japan Society for the Promotion of Science.
PY - 1997/10/20
Y1 - 1997/10/20
N2 - The 25-hydroxyvitamin D3 1α-hydroxylase (1α-hydroxylase) is a cytochrome P450 enzyme that catalyzes the conversion of 25-hydroxyvitamin D3 to 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 D3 25-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.
AB - The 25-hydroxyvitamin D3 1α-hydroxylase (1α-hydroxylase) is a cytochrome P450 enzyme that catalyzes the conversion of 25-hydroxyvitamin D3 to 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 D3 25-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.
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U2 - 10.1006/bbrc.1997.7508
DO - 10.1006/bbrc.1997.7508
M3 - Article
C2 - 9344864
AN - SCOPUS:0031581091
SN - 0006-291X
VL - 239
SP - 527
EP - 533
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -
