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Structural changes in alpha-synuclein affect its chaperone-like activity in vitro
DC Field | Value | Language |
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dc.contributor.author | 김종선 | - |
dc.date.accessioned | 2019-11-11T05:24:00Z | - |
dc.date.available | 2019-11-11T05:24:00Z | - |
dc.date.issued | 2000 | - |
dc.identifier.issn | 0961-8368 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/171846 | - |
dc.description.abstract | Alpha-synuclein, a major constituent of Lewy bodies (LBs) in Parkinson's disease (PD), has been implicated to play a critical role in synaptic events, such as neuronal plasticity during development, learning, and degeneration under pathological conditions, although the physiological function of alpha-synuclein has not yet been established. We here present biochemical evidence that recombinant alpha-synuclein has a chaperone-like function against thermal and chemical stress in vitro. In our experiments, alpha-synuclein protected glutathione S-transferase (GST) and aldolase from heat-induced precipitation, and alpha-lactalbumin and bovine serum albumin from dithiothreitol (DTT)-induced precipitation like other molecular chaperones. Moreover, preheating of alpha-synuclein, which is believed to reorganize the molecular surface of alpha-synuclein, increased the chaperone-like activity. Interestingly, in organic solvents, which promotes the formation of secondary structure, alpha-synuclein aggregated more easily than in its native condition, which eventually might abrogate the chaperone-like function of the protein. In addition, alpha-synuclein was also rapidly and significantly precipitated by heat in the presence of Zn2+ in vitro, whereas it was not affected by the presence of Ca2+ or Mg2+. Circular dichroism spectra confirmed that alpha-synuclein underwent conformational change in the presence of Zn2+. Taken together, our data suggest that alpha-synuclein could act as a molecular chaperone, and that the conformational change of the alpha-synuclein could explain the aggregation kinetics of alpha-synuclein, which may be related to the abolishment of the chaperonic-like activity. | - |
dc.description.statementOfResponsibility | open | - |
dc.language | English | - |
dc.publisher | Cold Spring Harbor Laboratory Press | - |
dc.relation.isPartOf | Protein Science | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.subject.MESH | Albumins/drug effects | - |
dc.subject.MESH | Dimerization | - |
dc.subject.MESH | Dithiothreitol/pharmacology | - |
dc.subject.MESH | Enzymes/drug effects | - |
dc.subject.MESH | Enzymes/metabolism | - |
dc.subject.MESH | Humans | - |
dc.subject.MESH | Molecular Chaperones* | - |
dc.subject.MESH | Nerve Tissue Proteins/chemistry* | - |
dc.subject.MESH | Nerve Tissue Proteins/drug effects | - |
dc.subject.MESH | Nerve Tissue Proteins/pharmacology* | - |
dc.subject.MESH | Parkinson Disease/etiology | - |
dc.subject.MESH | Protein Denaturation/drug effects | - |
dc.subject.MESH | Protein Structure, Secondary | - |
dc.subject.MESH | Recombinant Proteins/chemistry | - |
dc.subject.MESH | Recombinant Proteins/drug effects | - |
dc.subject.MESH | Recombinant Proteins/pharmacology | - |
dc.subject.MESH | Structure-Activity Relationship | - |
dc.subject.MESH | Synucleins | - |
dc.subject.MESH | Temperature | - |
dc.subject.MESH | Zinc/pharmacology | - |
dc.subject.MESH | alpha-Synuclein | - |
dc.title | Structural changes in alpha-synuclein affect its chaperone-like activity in vitro | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Microbiology (미생물학교실) | - |
dc.contributor.googleauthor | Thomas D. Kim | - |
dc.contributor.googleauthor | Seung R. Paik | - |
dc.contributor.googleauthor | Chul-Hak Yang | - |
dc.contributor.googleauthor | Jongsun Kim | - |
dc.identifier.doi | 10.1110/ps.9.12.2489 | - |
dc.contributor.localId | A00921 | - |
dc.relation.journalcode | J03692 | - |
dc.identifier.eissn | 1469-896X | - |
dc.identifier.pmid | 11206070 | - |
dc.subject.keyword | a-synuclein | - |
dc.subject.keyword | molecular chaperone | - |
dc.subject.keyword | Parkinson’s disease | - |
dc.subject.keyword | protein folding | - |
dc.subject.keyword | structural change | - |
dc.contributor.alternativeName | Kim, Jong Sun | - |
dc.contributor.affiliatedAuthor | 김종선 | - |
dc.citation.volume | 9 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 2489 | - |
dc.citation.endPage | 2496 | - |
dc.identifier.bibliographicCitation | Protein Science, Vol.9(12) : 2489-2496, 2000 | - |
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