| pubmed-article:18451726 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18451726 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:18451726 | lifeskim:mentions | umls-concept:C0007332 | lld:lifeskim |
| pubmed-article:18451726 | lifeskim:mentions | umls-concept:C0285890 | lld:lifeskim |
| pubmed-article:18451726 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:18451726 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:18451726 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:18451726 | pubmed:dateCreated | 2008-5-2 | lld:pubmed |
| pubmed-article:18451726 | pubmed:abstractText | alpha-Synuclein (alpha-syn) is the major component of pathologic inclusions that characterize neurodegenerative disorders such as Parkinson disease, dementia with Lewy body disease, and multiple system atrophy. The present study uses novel phospho-specific antibodies to assess the presence and regulation of phosphorylated Ser87 and Ser129 in alpha-syn in human brain samples and in a transgenic mouse model of alpha-synucleinopathies. By immunohistochemistry, alpha-syn phosphorylated at Ser129, but not at Ser87, was abundant in alpha-syn inclusions. Under normal conditions, Ser129 phosphorylation, but not Ser87 phosphorylation, was detected at low levels in the soluble biochemical fractions in human alpha-syn transgenic mice and stably transfected cultured cells. Therefore, a role for Ser87 phosphorylation in alpha-synucleinopathies is unlikely, and in vitro assays showed that phosphorylation at this site would inhibit polymerization. In vitro studies also indicated that hyperphosphorylation of Ser129 alpha-syn in pathologic inclusions may be due in part to the intrinsic properties of aggregated alpha-syn to act as substrates for kinases but not phosphatases. Further studies in transgenic mice and cultured cells suggest that cellular toxicity, including proteasomal dysfunction, increases casein kinase 2 activity, which results in elevated Ser129 alpha-syn phosphorylation. These data provide novel explanations for the presence of hyperphosphorylated Ser129 alpha-syn in pathologic inclusions. | lld:pubmed |
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| pubmed-article:18451726 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18451726 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18451726 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18451726 | pubmed:month | May | lld:pubmed |
| pubmed-article:18451726 | pubmed:issn | 0022-3069 | lld:pubmed |
| pubmed-article:18451726 | pubmed:author | pubmed-author:GiassonBenoit... | lld:pubmed |
| pubmed-article:18451726 | pubmed:author | pubmed-author:WaxmanElisa... | lld:pubmed |
| pubmed-article:18451726 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18451726 | pubmed:volume | 67 | lld:pubmed |
| pubmed-article:18451726 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18451726 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18451726 | pubmed:pagination | 402-16 | lld:pubmed |
| pubmed-article:18451726 | pubmed:dateRevised | 2011-5-24 | lld:pubmed |
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| pubmed-article:18451726 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18451726 | pubmed:articleTitle | Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein. | lld:pubmed |
| pubmed-article:18451726 | pubmed:affiliation | Department of Pharmacology, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6084, USA. | lld:pubmed |
| pubmed-article:18451726 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18451726 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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