L773:1470 8728
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- Araya, ZufanUppsala universitet,Institutionen för farmaceutisk biovetenskap,Pharm Biochemistry (author)
Hormonal regulation of the human sterol 27-hydroxylase gene CYP27A1.
- Article/chapterEnglish2003
Publisher, publication year, extent ...
- 2003
- printrdacarrier
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- LIBRIS-ID:oai:DiVA.org:uu-64404
- https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-64404URI
- https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-95809URI
- https://doi.org/10.1042/BJ20021651DOI
Supplementary language notes
- Language:English
- Summary in:English
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- The mitochondrial sterol 27-hydroxylase (CYP27A1) is a multifunctional cytochrome P450 enzyme that catalyses important hydroxylations in the biosynthesis of bile acids and bioactivation of vitamin D3. Previous results [Babiker, Andersson, Lund, Xiu, Deeb, Reshef, Leitersdorf, Diczfalusy and Bj¨orkhem (1997) J. Biol. Chem. 272, 26253–26261] suggest that CYP27A1 plays an important role in cholesterol homoeostasis and affects atherogenesis. In the present study, the regulation of the human CYP27A1 gene by growth hormone (GH), insulin-like growth factor-1 (IGF-1), dexamethasone, thyroid hormones and PMA was studied. HepG2 cells were transfected transiently with luciferase reporter gene constructs containing DNA fragments flanking the 5_-region of the human CYP27A1 gene. GH, IGF-1 and dexamethasone increased the promoter activity by 2–3-fold, whereas thyroxine (T4) and PMA repressed the activity significantly when measured with luciferase activity expressed in the cells. The endogenous CYP27A1 enzyme activity in the cells was stimulated by GH, IGF-1 and dexamethasone, whereas T4 and PMA inhibited the activity. Experiments with progressive deletion/luciferase reporter gene constructs indicated that the response elements for GH may be localized in a region upstream to position −1094 bp. The putative response elements for dexamethasone were mapped to positions between −792 and −1095 bp. The −451 bp fragment of the human CYP27A1 gene was found to confer the activation by IGF-1, and the inhibition by T4 and PMA. Results of the present study suggest that CYP27A1 is regulated in human cells by hormones and signal-transduction pathways.
Subject headings and genre
- MEDICIN OCH HÄLSOVETENSKAP Medicinska och farmaceutiska grundvetenskaper Farmaceutiska vetenskaper hsv//swe
- MEDICAL AND HEALTH SCIENCES Basic Medicine Pharmaceutical Sciences hsv//eng
- Bile acid biosynthesis
- cholesterol homoeostasis
- growth hormone
- PMA
- thyroid hormone
- MEDICINE
- MEDICIN
- PHARMACY
Added entries (persons, corporate bodies, meetings, titles ...)
- Tang, WanjinUppsala universitet,Institutionen för farmaceutisk biovetenskap,Pharm Biochemistry (author)
- Wikvall, KjellUppsala universitet,Institutionen för farmaceutisk biovetenskap,Pharm Biochemistry(Swepub:uu)kwi24506 (author)
- Uppsala universitetInstitutionen för farmaceutisk biovetenskap (creator_code:org_t)
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- In:Biochemical Journal372:2, s. 529-5340264-60211470-8728
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