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The Parkinson's disease-associated protein a-synuclein (a-syn) is not only expressed in the cytoplasm of neurons, but also secreted in the extracellular space and internalized into glial cells through a lipid raft dependent process. Two distinct cholesterol-binding domains in a-synuclein were identified by Fantini and coworkers. The tilted peptide of a-synuclein (67-78) bound cholesterol with high affinity and was toxic for cultured astrocytes. A cholesterol recognition consensus motif with lower affinity for cholesterol and devoid of toxicity, is encased in the glycosphingolipid-binding domain (34-45) of a-synuclein. The authors propose that the association of a-synuclein with lipid rafts involves both the binding of a-synuclein (34-45) to glycosphingolipids, and the interaction of a-synuclein (67-78) with cholesterol.
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Technical inquiry about: 01-4107368 α-Synuclein (67-78) (human)
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