Brain neutral lipids mass is increased in α‐synuclein gene‐ablated mice
Open Access
- 4 January 2007
- journal article
- Published by Wiley in Journal of Neurochemistry
- Vol. 101 (1), 132-141
- https://doi.org/10.1111/j.1471-4159.2006.04348.x
Abstract
Because α‐synuclein (Snca) has a role in brain lipid metabolism, we determined the impact that Snca deletion had on whole brain lipid composition. We analysed masses of individual phospholipid (PL) classes and neutral lipid mass as well as PL acyl chain composition in brains from wild‐type and Snca‐/‐ mice. Although total brain PL mass was not altered, cardiolipin and phosphatidylglycerol mass decreased 16% and 27%, respectively, in Snca‐/‐ mice. In addition, no changes were observed in plasmalogen or polyphosphoinositide mass. In ethanolamine glycerophospholipids and phosphatidylserine, docosahexaenoic acid (22 : 6n‐3) was decreased 7%, while 16 : 0 was increased 1.1‐fold and 1.4‐fold, respectively. Surprisingly, brain cholesterol, cholesteryl ester, and triacylglycerol mass were increased 1.1‐fold, 1.6‐fold, and 1.4‐fold, respectively in Snca‐/‐ mice. In isolated myelin, cholesterol mass was also increased 1.3‐fold, but because there was also a net increase in myelin PL mass, the cholesterol to PL ratio was unaltered. No changes in the expression of cholesterogenic enzymes were observed, suggesting these did not account for the observed changes in cholesterol. These data extend our previous results in astrocytes and kinetic studies in vivo demonstrating a role for Snca in brain lipid metabolism and demonstrate a clear impact on brain neutral lipid metabolism.Keywords
This publication has 70 references indexed in Scilit:
- Interactions between fatty acids and α-synucleinJournal of Lipid Research, 2006
- Acyl-CoA Synthetase Activity Links Wild-Type but Not Mutant α-Synuclein to Brain Arachidonate MetabolismBiochemistry, 2006
- The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementiaAnnals of Neurology, 2003
- α-Synuclein Locus Triplication Causes Parkinson's DiseaseScience, 2003
- α-Synuclein Membrane Interactions and Lipid SpecificityJournal of Biological Chemistry, 2000
- Binding of α-Synuclein to Brain Vesicles Is Abolished by Familial Parkinson's Disease MutationPublished by Elsevier BV ,1998
- Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic MembranesJournal of Biological Chemistry, 1998
- AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's diseaseNature Genetics, 1998
- Mutation in the α-Synuclein Gene Identified in Families with Parkinson's DiseaseScience, 1997
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976