{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T09:31:24Z","timestamp":1791279084688,"version":"4.1.0"},"reference-count":64,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2004,4,1]],"date-time":"2004-04-01T00:00:00Z","timestamp":1080777600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2004,4,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>The human hepatic microsomal vitamin D 25-hydroxylase protein and gene have not been identified with certainty. Sixteen hepatic recombinant microsomal enzymes were screened for 25-hydroxylase activity; 11 had some 25-hydroxylase activity, but CYP3A4 had the highest activity. In characterized liver microsomes, 25-hydroxylase activity correlated significantly with CYP3A4 testosterone 6\u03b2-hydroxylase activity. Activity in pooled liver microsomes was inhibited by known inhibitors of CYP3A4 and by an antibody to CYP3A2. Thus, CYP3A4 is a hepatic microsomal vitamin D 25-hydroxylase.<\/jats:p>\n               <jats:p>Introduction: Studies were performed to identify human microsomal vitamin D-25 hydroxylase.<\/jats:p>\n               <jats:p>Materials and Methods: Sixteen major hepatic microsomal recombinant enzymes derived from cytochrome P450 cDNAs expressed in baculovirus-infected insect cells were screened for 25-hydroxylase activity with 1\u03b1-hydroxyvitamin D2 [1\u03b1(OH)D2], 1\u03b1-hydroxyvitamin D3 [1\u03b1(OH)D3], vitamin D2, and vitamin D3 as substrates. Activity was correlated with known biological activities of enzymes in a panel of 12 characterized human liver microsomes. The effects of known inhibitors and specific antibodies on activity also were determined.<\/jats:p>\n               <jats:p>Results: CYP3A4, the most abundant cytochrome P450 enzyme in human liver and intestine, had 7-fold greater activity than that of any of the other enzymes with 1\u03b1(OH)D2 as substrate. CYP3A4 25-hydroxylase activity was four times higher with 1\u03b1(OH)D2 than with 1\u03b1(OH)D3 as substrate, was much less with vitamin D2, and was not detected with vitamin D3. 1\u03b1(OH)D2 was the substrate in subsequent experiments. In a panel of characterized human liver microsomes, 25-hydroxylase activity correlated with CYP3A4 testosterone 6\u03b2-hydroxylase activity (r = 0.93, p &amp;lt; 0.001) and CYP2C91 diclofenac 4\u2032-hydroxylase activity (r = 0.65, p &amp;lt; 0.05), but not with activity of any of the other enzymes. Activity in recombinant CYP3A4 and pooled liver microsomes was dose-dependently inhibited by ketoconazole, troleandomycin, isoniazid, and \u03b1-naphthoflavone, known inhibitors of CYP3A4. Activity in pooled liver microsomes was inhibited by antibodies to CYP3A2 that are known to inhibit CYP3A4 activity.<\/jats:p>\n               <jats:p>Conclusion: CYP3A4 is a vitamin D 25-hydroxylase for vitamin D2 in human hepatic microsomes and hydroxylates both 1\u03b1(OH)D2 and 1\u03b1(OH)D3.<\/jats:p>","DOI":"10.1359\/jbmr.0301257","type":"journal-article","created":{"date-parts":[[2006,4,27]],"date-time":"2006-04-27T06:10:44Z","timestamp":1146118244000},"page":"680-688","source":"Crossref","is-referenced-by-count":131,"title":["CYP3A4 is a Human Microsomal Vitamin D 25-Hydroxylase"],"prefix":"10.1093","volume":"19","author":[{"given":"Ram P","family":"Gupta","sequence":"first","affiliation":[{"name":"Department of Medicine, Medical University of South Carolina, Charleston, South Carolina, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruce W","family":"Hollis","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, Medical University of South Carolina, Charleston, South Carolina, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shailendra B","family":"Patel","sequence":"additional","affiliation":[{"name":"Department of Medicine, Medical University of South Carolina, Charleston, South Carolina, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kennerly S","family":"Patrick","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, Medical University of South Carolina, Charleston, South Carolina, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norman H","family":"Bell","sequence":"additional","affiliation":[{"name":"Department of Medicine, Medical University of South Carolina, Charleston, South Carolina, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2009,12,2]]},"reference":[{"key":"2024013019210233200_bib1","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1016\/S0021-9258(17)38181-4","article-title":"Assay and properties of a mitochondrial 25-hydroxylase active on vitamin D","volume":"253","author":"Bj\u00f6rkhem","year":"1978","journal-title":"J Biol Chem"},{"key":"2024013019210233200_bib2","doi-asserted-by":"crossref","first-page":"10936","DOI":"10.1016\/S0021-9258(18)90603-4","article-title":"Subcellular localization of vitamin D3 25-hydroxylase in human liver","volume":"259","author":"Saarem","year":"1984","journal-title":"J Biol Chem"},{"key":"2024013019210233200_bib3","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1038\/230228a0","article-title":"Identification of 1,25-dihydroxycholecalciferol, a new kidney hormone controlling calcium metabolism","volume":"230","author":"Lawson","year":"1971","journal-title":"Nature"},{"key":"2024013019210233200_bib4","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1073\/pnas.68.4.803","article-title":"Identification of 1,25-dihydroxycholecal-ciferol, a form of vitamin D3 metabolically active in the intestine","volume":"68","author":"Holick","year":"1971","journal-title":"Proc Natl Acad Sci USA"},{"key":"2024013019210233200_bib5","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1126\/science.173.3991.51","article-title":"1,25-Dihydroxycholecalciferol: Identification of the proposed active form of vitamin D3 in the intestine","volume":"173","author":"Norman","year":"1971","journal-title":"Science"},{"key":"2024013019210233200_bib6","doi-asserted-by":"crossref","first-page":"4521","DOI":"10.1021\/bi00773a009","article-title":"Isolation and identification of 24,25-dihydroxycholecalciferol, a metabolite of vitamin D3 made in kidney","volume":"11","author":"Holick","year":"1972","journal-title":"Biochemistry"},{"key":"2024013019210233200_bib7","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1046\/j.1432-1327.1999.00375.x","article-title":"Metabolic studies using recombinant Escherichia coli cells producing rat mitochondrial CYP24: CYP24 can convert 1\u03b1,25-dihydroxyvitamin D3 to calcitroic acid","volume":"262","author":"Sakaki","year":"1999","journal-title":"Eur J Biochem"},{"key":"2024013019210233200_bib8","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1006\/abbi.2001.2419","article-title":"Calcitroic acid is a major catabolic metabolite in the metabolism of 1\u03b1,25-dihydroxyvitamin D2","volume":"392","author":"Zimmerman","year":"2001","journal-title":"Arch Biochem Biophys"},{"key":"2024013019210233200_bib9","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1080\/00498250110057369","article-title":"Metabolic activation of 1\u03b1-hydroxyvitamin D3 in human liver microsomes","volume":"31","author":"Kamachi","year":"2001","journal-title":"Xenobiotica"},{"key":"2024013019210233200_bib10","doi-asserted-by":"crossref","first-page":"7774","DOI":"10.1016\/S0021-9258(20)89517-9","article-title":"Characterization of human sterol 27-hydroxylase. 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