Volume 66, Issue 1 p. 277-285

Lipid Composition in Scrapie-Infected Mouse Brain: Prion Infection Increases the Levels of Dolichyl Phosphate and Ubiquinone

Zhizhong Guan

Zhizhong Guan

Division of Medical Cell Biology, Clinical Research Center, Novum, Karolinska Institutet and

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Magnus Söderberg

Magnus Söderberg

Division of Medical Cell Biology, Clinical Research Center, Novum, Karolinska Institutet and

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Pavel Sindelar

Corresponding Author

Pavel Sindelar

Division of Medical Cell Biology, Clinical Research Center, Novum, Karolinska Institutet and

Address correspondence and reprint requests to Dr. P. Sindelar at Clinical Research Center, Novum, S-14186 Huddinge, Sweden.Search for more papers by this author
Stanley B. Prusiner

Stanley B. Prusiner

Department of Neurology, University of California, San Francisco, California, U.S.A.

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Krister Kristensson

Krister Kristensson

Department of Neuroscience, Karolinska Institutet, Stockholm, Sweden; and

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Gustav Dallner

Gustav Dallner

Division of Medical Cell Biology, Clinical Research Center, Novum, Karolinska Institutet and

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First published: January 1996
Citations: 36

Abstract

Abstract: The neutral and phospholipid composition of mouse brain infected with scrapie prions was investigated. During the later stages of this disease, the level of dolichol decreased by 30% whereas the level of dolichyl phosphate increased by 30%. In terminally ill mice, there was also a 2.5-fold increase in both total ubiquinone and its reduced form. Furthermore, α-tocopherol was elevated at this stage by 50%. In contrast, no changes were observed in phospholipid amount, in phospholipid composition, and in phosphatidylethanolamine plasmalogen content during the entire disease process. The fatty acid and aldehyde composition of individual phospholipids remained unaltered as well. No modifications could be detected in cholesterol content. Thus, the majority of membrane lipids in scrapie-infected mouse brain are modified in neither quantity nor structure, but specific changes occur to a few polyisoprenoid lipids. This specificity indicates that, although prions accumulate in lysosomes, the infection process is not associated with a general membrane destruction caused by lysosomal enzyme leakage.

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