TY - JOUR
T1 - Increase in membrane cholesterol
T2 - A possible trigger for degradation of HMG CoA reductase and crystalloid endoplasmic reticulum in UT-1 cells
AU - Orci, Lelio
AU - Brown, Michael S.
AU - Goldstein, Joseph L.
AU - Garcia-Segura, Luis M.
AU - Anderson, Richard G W
N1 - Funding Information:
We thank Karen Fagerberg, Deborah Thompson, Debbie Noble, and Katie Hammon for their excellent technical assistance. This research was supported by research grants from the National Institutes of Health and the Swiss National Science Foundation.
PY - 1984/4
Y1 - 1984/4
N2 - The crystalloid endoplasmic reticulum (ER) houses large amounts of HMG CoA reductase, the rate-controlling enzyme in cholesterol synthesis. The crystalloid ER appears in UT-1 cells, a line of Chinese hamster ovary cells that has been chronically starved of cholesterol as a result of growth in the presence of compactin, an inhibitor of reductase. When cholesterol was provided to UT-1 cells in the form of low density lipoprotein (LDL), the reductase and crystalloid ER were destroyed. This destruction was preceded by an increase in the cholesterol content of crystalloid ER membranes, as judged by a 4- to 8-fold increase in their ability to form complexes with filipin, a cholesterol-binding compound that can be visualized in freeze-fracture electron micrographs. Filipin binding to other membranes was unchanged. Thus insertion of cholesterol into the crystalloid ER membrane may trigger the degradation of reductase and the membrane itself.
AB - The crystalloid endoplasmic reticulum (ER) houses large amounts of HMG CoA reductase, the rate-controlling enzyme in cholesterol synthesis. The crystalloid ER appears in UT-1 cells, a line of Chinese hamster ovary cells that has been chronically starved of cholesterol as a result of growth in the presence of compactin, an inhibitor of reductase. When cholesterol was provided to UT-1 cells in the form of low density lipoprotein (LDL), the reductase and crystalloid ER were destroyed. This destruction was preceded by an increase in the cholesterol content of crystalloid ER membranes, as judged by a 4- to 8-fold increase in their ability to form complexes with filipin, a cholesterol-binding compound that can be visualized in freeze-fracture electron micrographs. Filipin binding to other membranes was unchanged. Thus insertion of cholesterol into the crystalloid ER membrane may trigger the degradation of reductase and the membrane itself.
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U2 - 10.1016/0092-8674(84)90033-3
DO - 10.1016/0092-8674(84)90033-3
M3 - Article
C2 - 6705048
AN - SCOPUS:0021417623
SN - 0092-8674
VL - 36
SP - 835
EP - 845
JO - Cell
JF - Cell
IS - 4
ER -