6533b824fe1ef96bd1280c43
RESEARCH PRODUCT
18-hydroxylation in the Y-1 adrenal cell line: response to ACTH and to culture conditions.
Leyla C. RamirezPaulette BournotMalika Es-sounisubject
medicine.medical_specialtyCytochromeEndocrinology Diabetes and Metabolismmedicine.medical_treatmentClinical BiochemistryHydroxylationBiochemistryHydroxylationchemistry.chemical_compoundMiceEndocrinologyAdrenocorticotropic HormoneCytochrome P-450 Enzyme SystemInternal medicineAdrenal GlandsmedicineAnimalsCytochrome P-450 CYP11B2DesoxycorticosteroneMolecular BiologyIncubationCells CulturedFetusbiologyDose-Response Relationship DrugSubstrate (chemistry)Cell BiologyFetal BloodIn vitroCulture MediaSteroid hormoneEndocrinologyBloodchemistryCell cultureSteroid Hydroxylasesbiology.proteinMolecular MedicineSteroid 11-beta-Hydroxylasedescription
The 18-hydroxylation of deoxycorticosterone in the Y-1 adrenal cell line was studied under various incubation and cell culture conditions and compared to 11 beta-hydroxylation. Repeated incubation of the substrate increased both 18- and 11 beta-hydroxylation in the Y-1 cells. Furthermore, both 18- and 11 beta-hydroxylation were increased with increased serum concentration and prolonged incubation time. While the increase in 11 beta-hydroxylation seemed to be independent of the type of serum, 18-hydroxylation was much more important in cells cultured in fetal or newborn calf serum supplemented medium than in those cultured in horse serum supplemented medium. As expected, ACTH treatment increased 11 beta-hydroxylation; however, it decreased 18-hydroxylation. The different regulation of these two hydroxylating pathways by ACTH, point to a heterogeneity of the cytochrome P-450(11) beta of the Y-1 cell line.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1992-11-01 | The Journal of steroid biochemistry and molecular biology |