| pubmed-article:12832839 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C0206116 | lld:lifeskim |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C0031308 | lld:lifeskim |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C1565167 | lld:lifeskim |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C0678544 | lld:lifeskim |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C1419227 | lld:lifeskim |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C1421479 | lld:lifeskim |
| pubmed-article:12832839 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:12832839 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12832839 | pubmed:dateCreated | 2003-6-30 | lld:pubmed |
| pubmed-article:12832839 | pubmed:abstractText | Alzheimer's disease (AD) is characterized by the accumulation of extracellular amyloid-beta (A beta) fibrils with microglia. Recently, there has been great interest in the microglial phagocytosis of A beta, because the microglial pathway is considered to be one of the A beta clearance pathways in the brain parenchyma. However, the mechanism of microglial phagocytosis of A beta is not fully understood and, thus, was investigated in this study. At one minute after exposure to A beta(1-42) (A beta 42), A beta immunoreactivity was detected at the cell surface of microglia. After 1 h, marked immunoreactivity was observed in the cytosolic vesicles. At 12 h, delayed phagocytosis of fibrillar A beta 42 was also observed with the formation of a large phagocytic cup. The microglial cell shape rapidly changed to an ameboid form during the process of phagocytosis. Although neither neural Wiskott-Aldrich syndrome protein (N-WASP) nor WASP interacting SH3 protein (WISH) immunoreactivity was co-localized with filamentous actin (F-actin) distribution, both WASP family verprolin-homologous protein (WAVE) and Rac1 immunoreactivity was co-localized with F-actin in the lamellipodia of phogocytic microglia. These results suggest that WAVE and Rac1 participate in the phagocytosis of A beta 42 by microglia. | lld:pubmed |
| pubmed-article:12832839 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12832839 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12832839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12832839 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12832839 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12832839 | pubmed:issn | 1347-8613 | lld:pubmed |
| pubmed-article:12832839 | pubmed:author | pubmed-author:MikiHiroakiH | lld:pubmed |
| pubmed-article:12832839 | pubmed:author | pubmed-author:TakenawaTadao... | lld:pubmed |
| pubmed-article:12832839 | pubmed:author | pubmed-author:ShimohamaShun... | lld:pubmed |
| pubmed-article:12832839 | pubmed:author | pubmed-author:KitamuraYoshi... | lld:pubmed |
| pubmed-article:12832839 | pubmed:author | pubmed-author:TaniguchiTaka... | lld:pubmed |
| pubmed-article:12832839 | pubmed:author | pubmed-author:TakataKazuyuk... | lld:pubmed |
| pubmed-article:12832839 | pubmed:author | pubmed-author:ShibagakiKeii... | lld:pubmed |
| pubmed-article:12832839 | pubmed:author | pubmed-author:Gebicke-Haert... | lld:pubmed |
| pubmed-article:12832839 | pubmed:author | pubmed-author:TsuchiyaDaiju... | lld:pubmed |
| pubmed-article:12832839 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12832839 | pubmed:volume | 92 | lld:pubmed |
| pubmed-article:12832839 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12832839 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12832839 | pubmed:pagination | 115-23 | lld:pubmed |
| pubmed-article:12832839 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:meshHeading | pubmed-meshheading:12832839... | lld:pubmed |
| pubmed-article:12832839 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12832839 | pubmed:articleTitle | Involvement of Wiskott-Aldrich syndrome protein family verprolin-homologous protein (WAVE) and Rac1 in the phagocytosis of amyloid-beta(1-42) in rat microglia. | lld:pubmed |
| pubmed-article:12832839 | pubmed:affiliation | Department of Neurobiology, Kyoto Pharmaceutical University, Kyoto, Japan. | lld:pubmed |
| pubmed-article:12832839 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12832839 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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