Cited 15 times in
Calpain-resistant fragment(s) of α-synuclein regulates the synuclein-cleaving activity of 20S proteasome
DC Field | Value | Language |
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dc.contributor.author | 김종선 | - |
dc.date.accessioned | 2015-06-10T12:58:30Z | - |
dc.date.available | 2015-06-10T12:58:30Z | - |
dc.date.issued | 2006 | - |
dc.identifier.issn | 0003-9861 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/110783 | - |
dc.description.abstract | α-Synuclein is a pathological component of Parkinson’s disease by participating in Lewy body formation. Imbalance in protein turnover could result in the abnormal protein aggregation responsible for eventual neuronal cell death. This in vitro digestion study showed that both m-calpain and 20S proteasome preferentially hydrolyzed the N-terminal half of α-synuclein, which made the hydrophobic NAC and following acidic C-terminal region resistant against the proteolyses. Since the acidic C-terminal region contains the PEST segment—a protein degradation signal enriched with amino acids of proline (P), glutamate (E), serine (S), and threonine (T)—, the PEST segment has not been processed or even required for the proteolyses. α-Synuclein would be recognized primarily by m-calpain since the common substrate was processed by m-calpain five times more effectively than 20S proteasome with kcat/Km of 1.64 × 104 M−1 s−1 and 0.32 × 104 M−1 s−1, respectively. The N-terminally truncated protease-resistant C-terminal fragment of α-syn61–140 was demonstrated to stimulate the 20S proteasome-mediated breakdown of α-synuclein and its mutant forms of Ala53Thr and Ala30Pro. The stimulation for Ala53Thr, however, was noticeably less efficient than those for the other proteins, which might support the previous observation of the prolonged intracellular life span of Ala53Thr by 1.5-fold compared to that of wild-type form. We have hypothesized that the N-terminally truncated C-terminal fragment derived from the abundant α-synuclein through intracellular proteolyses could be involved in various physiological or pathological effects which might be related to the formation of abnormal protein aggregation and subsequent neuronal degeneration by influencing the intracellular protein turnover or directly participating in the aggregate formation. | - |
dc.description.statementOfResponsibility | open | - |
dc.format.extent | 40~47 | - |
dc.relation.isPartOf | ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.subject.MESH | Amino Acid Sequence | - |
dc.subject.MESH | Amino Acid Substitution/genetics | - |
dc.subject.MESH | Amino Acids/genetics | - |
dc.subject.MESH | Amino Acids/metabolism* | - |
dc.subject.MESH | Animals | - |
dc.subject.MESH | Calpain/metabolism* | - |
dc.subject.MESH | Electrophoresis, Polyacrylamide Gel | - |
dc.subject.MESH | Glutamates/genetics | - |
dc.subject.MESH | Glutamates/metabolism | - |
dc.subject.MESH | Hydrolysis | - |
dc.subject.MESH | Models, Biological | - |
dc.subject.MESH | Molecular Sequence Data | - |
dc.subject.MESH | Mutation/genetics | - |
dc.subject.MESH | Proline/genetics | - |
dc.subject.MESH | Proline/metabolism | - |
dc.subject.MESH | Proteasome Endopeptidase Complex/metabolism* | - |
dc.subject.MESH | Serine/genetics | - |
dc.subject.MESH | Serine/metabolism | - |
dc.subject.MESH | Substrate Specificity | - |
dc.subject.MESH | Swine | - |
dc.subject.MESH | Threonine/genetics | - |
dc.subject.MESH | Threonine/metabolism | - |
dc.subject.MESH | alpha-Synuclein/genetics | - |
dc.subject.MESH | alpha-Synuclein/metabolism* | - |
dc.title | Calpain-resistant fragment(s) of α-synuclein regulates the synuclein-cleaving activity of 20S proteasome | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Microbiology (미생물학) | - |
dc.contributor.googleauthor | Hyun Jin Kim | - |
dc.contributor.googleauthor | Daekyun Lee | - |
dc.contributor.googleauthor | Choong-Hwan Lee | - |
dc.contributor.googleauthor | Kwang Chul Chung | - |
dc.contributor.googleauthor | Jongsun Kim | - |
dc.contributor.googleauthor | Seung R. Paik | - |
dc.identifier.doi | 10.1016/j.abb.2006.08.019 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A00921 | - |
dc.relation.journalcode | J00211 | - |
dc.identifier.eissn | 1096-0384 | - |
dc.identifier.pmid | 17005155 | - |
dc.identifier.url | http://www.sciencedirect.com/science/article/pii/S0003986106003092 | - |
dc.contributor.alternativeName | Kim, Jong Sun | - |
dc.contributor.affiliatedAuthor | Kim, Jong Sun | - |
dc.rights.accessRights | not free | - |
dc.citation.volume | 455 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 40 | - |
dc.citation.endPage | 47 | - |
dc.identifier.bibliographicCitation | ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, Vol.455(1) : 40-47, 2006 | - |
dc.identifier.rimsid | 54430 | - |
dc.type.rims | ART | - |
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