Source:http://linkedlifedata.com/resource/pubmed/id/12832839
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2003-6-30
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochalasin D,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/VRP1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Wiskott-Aldrich Syndrome Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/amyloid beta-protein (1-42),
http://linkedlifedata.com/resource/pubmed/chemical/rac1 GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1347-8613
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
92
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-23
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12832839-Amyloid beta-Peptides,
pubmed-meshheading:12832839-Animals,
pubmed-meshheading:12832839-Cells, Cultured,
pubmed-meshheading:12832839-Cytochalasin D,
pubmed-meshheading:12832839-Microfilament Proteins,
pubmed-meshheading:12832839-Microglia,
pubmed-meshheading:12832839-Peptide Fragments,
pubmed-meshheading:12832839-Phagocytosis,
pubmed-meshheading:12832839-Rats,
pubmed-meshheading:12832839-Rats, Wistar,
pubmed-meshheading:12832839-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12832839-Wiskott-Aldrich Syndrome,
pubmed-meshheading:12832839-Wiskott-Aldrich Syndrome Protein Family,
pubmed-meshheading:12832839-rac1 GTP-Binding Protein
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pubmed:year |
2003
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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.
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pubmed:affiliation |
Department of Neurobiology, Kyoto Pharmaceutical University, Kyoto, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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