NB-598: a potent competitive inhibitor of squalene epoxidase.
نویسندگان
چکیده
منابع مشابه
Effect of a novel squalene epoxidase inhibitor, NB-598, on the regulation of cholesterol metabolism in Hep G2 cells.
We have reported previously that NB-598 competitively inhibits human squalene epoxidase and strongly inhibits cholesterol synthesis from [14C]acetate in cultured cells. Furthermore, multiple oral administration of NB-598 decreased serum cholesterol levels in dogs (Horie, M., Tsuchiya, Y., Hayashi, M., Iida, Y., Iwasawa, Y., Nagata, Y., Sawasaki, Y., Fukuzumi, H., Kitani, K., and Kamei, T. (1990...
متن کاملSqualene Epoxidase of Rat Liver*
The microsomal enzyme system from rat liver which catalyzes the epoxidation of squalene to 2,3-oxidosqualene (squalene epoxidase) has been investigated further with 10 ,ll-dihydrosqualene as the artacial substrate. Liver supernatant contributes two essential components to the epoxidase system, one heat stable and the other heat labile (YAMAMOTO, S., AND BLOCH, K. (1970) J. Biol. Chem. 245, 1670...
متن کاملPurification and characterization of recombinant squalene epoxidase.
Recombinant rat squalene epoxidase (rSE) was expressed in E. coli and purified to an apparent homogeneity. This expression system was constructed using squalene epoxidase (SE) cDNA in which nucleotides coding 99 amino acids in the N-terminal were deleted and nucleotides coding hexa-histidine in the C-terminal were added. Purification was carried out using Ni-chelate affinity agarose and Cibacro...
متن کاملStudies on Squalene Epoxidase of Rat Liver*
Rat liver microsomes previously heated to 50” for 5 mm accumulate 2,3-oxidosqualene on incubation with squalene. Squalene epoxidase activity can be assayed either with squalene and heated microsomes or with lO,ll-dihydrosqualene and intact microsomes. In common with other monooxygenases, the epoxidase requires TPNH and molecular oxygen. Both a soluble fraction of rat liver and microsomes are ne...
متن کاملRegulation of squalene epoxidase in HepG2 cells.
Regulation of squalene epoxidase in the cholesterol biosynthetic pathway was studied in a human hepatoma cell line, HepG2 cells. Since the squalene epoxidase activity in cell homogenates was found to be stimulated by the addition of Triton X-100, enzyme activity was determined in the presence of this detergent. Incubation of HepG2 cells for 18 h with L-654,969, a potent competitive inhibitor of...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)44716-8