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On the mechanism of internalization of alpha-synuclein into microglia: roles of ganglioside GM1 and lipid raft.

DC Field Value Language
dc.contributor.authorPark, JY-
dc.contributor.authorKim, KS-
dc.contributor.authorLee, SB-
dc.contributor.authorRyu, JS-
dc.contributor.authorChung, KC-
dc.contributor.authorChoo, YK-
dc.contributor.authorJou, I-
dc.contributor.authorKim, J-
dc.contributor.authorPark, SM-
dc.date.accessioned2010-11-12T05:48:30Z-
dc.date.available2010-11-12T05:48:30Z-
dc.date.issued2009-
dc.identifier.issn0022-3042-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/195-
dc.description.abstractALpha-synuclein (alpha-syn) has been known to be a key player of the pathogenesis of Parkinson's disease and has recently been detected in extracellular biological fluids and shown to be rapidly secreted from cells. The penetration of alpha-syn into cells has also been observed. In this study, we observed that dl-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol, a glucosyltransferase inhibitor, and proteinase K inhibited the internalization of extracellular monomeric alpha-syn into BV-2 cells, and the addition of monosialoganglioside GM1 ameliorated the inhibition of alpha-syn internalization in dl-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol-treated BV-2 cells. Furthermore, inhibition of clathrin-, caveolae-, and dynamin-dependent endocytosis did not prevent the internalization of alpha-syn, but disruption of lipid raft inhibited it. Inhibition of macropinocytosis and disruption of actin and microtubule structures also did not inhibit the internalization of alpha-syn. In addition, we further confirmed these observations by co-culture system of BV-2 cells and alpha-syn-over-expressing SH-SY5Y cells. These findings suggest that extracellular alpha-syn is internalized into microglia via GM1 as well as hitherto-unknown protein receptors in clathrin-, caveolae-, and dynamin-independent, but lipid raft-dependent manner. Elucidation of the mechanism involved in internalization of alpha-syn should be greatly helpful in the development of new treatments of alpha-syn-related neurodegenerative diseases.-
dc.formattext/plain-
dc.language.isoen-
dc.subject.MESHAnimals-
dc.subject.MESHCaveolins-
dc.subject.MESHCell Line-
dc.subject.MESHCell Line, Tumor-
dc.subject.MESHClathrin-
dc.subject.MESHCoculture Techniques-
dc.subject.MESHDynamins-
dc.subject.MESHEncephalitis-
dc.subject.MESHEndocytosis-
dc.subject.MESHEndopeptidase K-
dc.subject.MESHEnzyme Inhibitors-
dc.subject.MESHExtracellular Space-
dc.subject.MESHG(M1) Ganglioside-
dc.subject.MESHGlucosyltransferases-
dc.subject.MESHHumans-
dc.subject.MESHMembrane Microdomains-
dc.subject.MESHMice-
dc.subject.MESHMicroglia-
dc.subject.MESHNeurodegenerative Diseases-
dc.subject.MESHParkinson Disease-
dc.subject.MESHProtein Transport-
dc.subject.MESHalpha-Synuclein-
dc.titleOn the mechanism of internalization of alpha-synuclein into microglia: roles of ganglioside GM1 and lipid raft.-
dc.typeArticle-
dc.identifier.pmid19457104-
dc.contributor.affiliatedAuthor주, 일로-
dc.contributor.affiliatedAuthor박, 상면-
dc.type.localJournal Papers-
dc.identifier.doi10.1111/j.1471-4159.2009.06150.x-
dc.citation.titleJournal of neurochemistry-
dc.citation.volume110-
dc.citation.number1-
dc.citation.date2009-
dc.citation.startPage400-
dc.citation.endPage411-
dc.identifier.bibliographicCitationJournal of neurochemistry, 110(1). : 400-411, 2009-
dc.identifier.eissn1471-4159-
dc.relation.journalidJ000223042-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Pharmacology
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