The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Depletion of plasma-membrane sphingomyelin rapidly alters the distribution of cholesterol between plasma membranes and intracellular cholesterol pools in cultured fibroblasts
Abstract
This study examines the relationship between cellular sphingomyelin content and the distribution of unesterified cholesterol between the plasma-membrane pool and the putative intracellular regulatory pool. The sphingomyelin content of cultured human skin fibroblasts was reduced by treatment of intact cells with extracellularly added neutral sphingomyelinase, and subsequent changes in the activities of cholesterol-metabolizing enzymes were determined. Exposure of fibroblasts to 0.1 unit of sphingomyelinase/ml for 60 min led to the depletion of more than 90% of the cellular sphingomyelin, as determined from total lipid extracts. In a time-course study, it was found that within 10 min of the addition of sphingomyelinase to cells, a dramatic increase in acyl-CoA:cholesterol acyltransferase activity could be observed, whether measured from the appearance of plasma membrane-derived [3H]cholesterol or exogenously added [14C]oleic acid, in cellular cholesteryl esters. In addition, the cholesteryl ester mass was significantly higher in sphingomyelin-depleted fibroblasts at 3 h after exposure to sphingomyelinase compared with that in untreated fibroblasts [7.1 +/- 0.4 nmol of cholesterol/mg equivalents of esterified cholesterol compared with 4.2 +/- 0.1 nmol of cholesterol/mg equivalents of cholesteryl ester in control cells (P less than 0.05)]. The sphingomyelin-depleted cells also showed a reduction in the rate of endogenous synthesis of cholesterol, as measured by incorporation of sodium [14C]acetate into [14C]cholesterol. These results are consistent with a rapid movement of cholesterol from sphingomyelin-depleted plasma membranes to the putative intracellular regulatory pool of cholesterol. This mass movement of cholesterol away from the plasma membranes presumably resulted from a decreased capacity of the plasma membranes to solubilize cholesterol, since sphingomyelin-depleted cells also had a decreased capacity to incorporate nanomolar amounts of [3H]cholesterol from the extracellular medium, as compared with control cells. These findings confirm previous assumptions that the membrane sphingomyelin content is an important determinant of the overall distribution of cholesterol within intact cells.
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Increases in plasma membrane cholesterol beyond a threshold, or liberation of plasma membrane cholesterol from sequestration, result in transient expansions in the accessible pool of plasma membrane cholesterol.
“Increases in the level of PM cholesterol beyond a certain threshold (or liberation of PM cholesterol from sequestration) result in transient expansions in the accessible pool of PM cholesterol.”
From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Slotte & Bierman, 1988
The Discussion (page unavailable) reports that depleting sphingomyelin reduces the plasma membrane’s capacity to retain cholesterol and rapidly moves cholesterol to intracellular pools. It also describes fibroblast plasma membranes as saturated with respect to cholesterol solubilization. The paper does not show that adding cholesterol beyond a threshold, or releasing sequestered cholesterol, transiently expands an accessible plasma-membrane pool. (LLM, conf=0.84)
Experimental — accuracy not yet measuredCells respond to expanded accessible plasma membrane cholesterol by rapidly transporting it to the endoplasmic reticulum to suppress SREBPs, shutting down cholesterol biosynthesis and uptake.
“Cells respond by rapidly transporting the newly expanded pool of accessible cholesterol to the ER to suppress the activities of SREBPs, shutting down cholesterol biosynthesis and uptake, thereby avoiding cholesterol overaccumulation and maintaining PM cholesterol levels”
From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Slotte & Bierman, 1988
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Brown, M. S., Ho, Y. K., & Goldstein, J. L. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70568-7 · Cited by 722
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Research works printed but not linked: 1
- Jain, M. K. (1975) in Current Topics in Membranes and Transport (Bronner, F. & Kleinzeller, A., eds.), vol. 6, pp. 1-17, Academic Press, New York
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Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b
Ercan, B., Naito, T., Koh, D. H. Z., Dharmawan, D., & Saheki, Y. (2021) · The EMBO Journal · doi:10.15252/embj.2020106524 · Cited by 132
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Metadata
- Authors
- Slotte, J. P., & Bierman, E. L.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1988-03-15
- Volume
- 250
- Issue
- 3
- Pages
- 653-658
- ISSN
- 0264-6021
- 1470-8728
- Cited by
- 288
- References
- 1
- Language
- en
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