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FcγRIIB mediates the inhibitory effect of aggregated α-synuclein on microglial phagocytosis.

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dc.contributor.authorChoi, YR-
dc.contributor.authorKang, SJ-
dc.contributor.authorKim, JM-
dc.contributor.authorLee, SJ-
dc.contributor.authorJou, I-
dc.contributor.authorJoe, EH-
dc.contributor.authorPark, SM-
dc.date.accessioned2017-04-04T08:04:55Z-
dc.date.available2017-04-04T08:04:55Z-
dc.date.issued2015-
dc.identifier.issn0969-9961-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/13771-
dc.description.abstractParkinson's disease (PD) is the second most prevalent neurodegenerative disease. Although the etiology of PD has not yet been fully understood, accumulating evidence indicates that neuroinflammation plays a critical role in the progression of PD. α-Synuclein (α-Syn) has been considered to be a key player of the pathogenesis of PD, and recent reports that prion-like propagation of misfolded α-syn released from neurons may play an important role in the progression of PD have led to increased attention to the studies elucidating the roles of extracellular α-syn in the CNS. Extracellular α-syn has also been reported to regulate microglial inflammatory response. In this study, we demonstrated that aggregated α-syn inhibited microglial phagocytosis by activating SHP-1. SHP-1 activation was also observed in A53T α-syn transgenic mice. In addition, aggregated α-syn bound to FcγRIIB on microglia, inducing SHP-1 activation, further inhibiting microglial phagocytosis. Aggregated α-syn upregulated FcγRIIB expression in microglia and upregulated FcγRIIB was also observed in A53T α-syn transgenic mice. These data suggest that aggregated α-syn released from neurons dysregulates microglial immune response through inhibiting microglial phagocytosis, further causing neurodegeneration observed in PD. The interaction of aggregated α-syn and FcγRIIB and further SHP-1 activation can be a new therapeutic target against PD.-
dc.language.isoen-
dc.subject.MESHAnimals-
dc.subject.MESHBrain-
dc.subject.MESHCells, Cultured-
dc.subject.MESHMice-
dc.subject.MESHMice, Inbred C57BL-
dc.subject.MESHMice, Transgenic-
dc.subject.MESHMicroglia-
dc.subject.MESHPhagocytosis-
dc.subject.MESHProtein Aggregates-
dc.subject.MESHProtein Tyrosine Phosphatase, Non-Receptor Type 6-
dc.subject.MESHRats-
dc.subject.MESHRats, Sprague-Dawley-
dc.subject.MESHReceptors, IgG-
dc.subject.MESHalpha-Synuclein-
dc.titleFcγRIIB mediates the inhibitory effect of aggregated α-synuclein on microglial phagocytosis.-
dc.typeArticle-
dc.identifier.pmid26342897-
dc.identifier.urlhttps://linkinghub.elsevier.com/retrieve/pii/S0969-9961(15)30045-0-
dc.contributor.affiliatedAuthor주, 일로-
dc.contributor.affiliatedAuthor조, 은혜-
dc.contributor.affiliatedAuthor박, 상면-
dc.type.localJournal Papers-
dc.identifier.doi10.1016/j.nbd.2015.08.025-
dc.citation.titleNeurobiology of disease-
dc.citation.volume83-
dc.citation.date2015-
dc.citation.startPage90-
dc.citation.endPage99-
dc.identifier.bibliographicCitationNeurobiology of disease, 83. : 90-99, 2015-
dc.identifier.eissn1095-953X-
dc.relation.journalidJ009699961-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Pharmacology
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