Activation of cholesterol synthesis in preference to fatty acid synthesis in liver and adipose tissue of transgenic mice overproducing sterol regulatory element-binding protein-2.
Open Access
- 1 June 1998
- journal article
- Published by American Society for Clinical Investigation in Journal of Clinical Investigation
- Vol. 101 (11), 2331-2339
- https://doi.org/10.1172/jci2961
Abstract
We produced transgenic mice that express a dominant-positive truncated form of sterol regulatory element-binding protein-2 (SREBP-2) in liver and adipose tissue. The encoded protein lacks the membrane-binding and COOH-terminal regulatory domains, and it is therefore not susceptible to negative regulation by cholesterol. Livers from the transgenic mice showed increases in mRNAs encoding multiple enzymes of cholesterol biosynthesis, the LDL receptor, and fatty acid biosynthesis. The elevations in mRNA for 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) synthase and HMG CoA reductase were especially marked (13-fold and 75-fold, respectively). As a result, the transgenic livers showed a 28-fold increase in the rate of cholesterol synthesis and a lesser fourfold increase in fatty acid synthesis, as measured by intraperitoneal injection of [3H]water. These results contrast with previously reported effects of dominant-positive SREBP-1a, which activated fatty acid synthesis more than cholesterol synthesis. In adipose tissue of the SREBP-2 transgenics, the mRNAs for cholesterol biosynthetic enzymes were elevated, but the mRNAs for fatty acid biosynthetic enzymes were not. We conclude that SREBP-2 is a relatively selective activator of cholesterol synthesis, as opposed to fatty acid synthesis, in liver and adipose tissue of mice.This publication has 23 references indexed in Scilit:
- Physiological and molecular mechanisms involved in nutritional regulation of fatty acid synthesisPhysiological Reviews, 1995
- Assignment of the membrane attachment, DNA binding, and transcriptional activation domains of sterol regulatory element-binding protein-1 (SREBP-1).Journal of Biological Chemistry, 1994
- Reevaluation and application of the dual-isotope plasma ratio method for the measurement of intestinal cholesterol absorption in the hamster.Journal of Lipid Research, 1994
- SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element.Proceedings of the National Academy of Sciences, 1993
- Cloning of a new member of the peroxisome proliferator-activated receptor gene family from mouse liver.Journal of Biological Chemistry, 1993
- SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor geneCell, 1993
- Cloning and gene defects in microsomal triglyceride transfer protein associated with abetalipoproteinaemiaNature, 1993
- ADD1: a novel helix-loop-helix transcription factor associated with adipocyte determination and differentiation.Molecular and Cellular Biology, 1993
- Tissue-specific, developmental, hormonal, and dietary regulation of rat phosphoenolpyruvate carboxykinase-human growth hormone fusion genes in transgenic mice.Molecular and Cellular Biology, 1992
- Rapid separation of neutral lipids, free fatty acids and polar lipids using prepacked silica sep‐Pak columnsLipids, 1988