| pubmed-article:19643079 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19643079 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:19643079 | lifeskim:mentions | umls-concept:C0024367 | lld:lifeskim |
| pubmed-article:19643079 | lifeskim:mentions | umls-concept:C0031672 | lld:lifeskim |
| pubmed-article:19643079 | lifeskim:mentions | umls-concept:C1749570 | lld:lifeskim |
| pubmed-article:19643079 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:19643079 | pubmed:dateCreated | 2009-10-5 | lld:pubmed |
| pubmed-article:19643079 | pubmed:abstractText | Phospholipase A(2) (PLA(2)) not only plays a role in the membrane vesiculation system but also mediates membrane-raft budding and fission in artificial giant liposomes. This study aimed to demonstrate the same effects in living cells. Differentiated Caco-2 cells were cultured on filter membranes. MDCK cells were challenged with Influenza virus. The MDCK cultures were harvested for virus titration with a plaque assay. Alkaline phosphatase (ALP), a membrane-raft associated glycosylphosphatidylinositol (GPI)-anchored protein, was 70% released by adding 0.2 mmol/l lysophosphatidylcholine, which was abolished by treatment with a membrane-raft disrupter, methyl-beta-cyclodextrin. Activation of calcium-independent PLA(2) (iPLA(2)) by brefeldin A increased the apical release of ALP by approximately 1.5-fold (p<0.01), which was blocked by PLA(2) inhibitor bromoenol lactone (BEL). BEL also reduced Influenza virus production into the media (<10%) in the MDCK culture. These results suggest that cells utilize inverted corn-shaped lysophospholipids generated by PLA(2) to modulate plasma membrane structure and assist the budding of raft-associated plasma membrane particles, which virus utilizes for its budding. Brush borders are enriched with membrane-rafts and undergo rapid turnover; thus, PLA(2) may be involved in the regulatory mechanism in membrane dynamism. Further, iPLA(2) may provide a therapeutic target for viral infections. | lld:pubmed |
| pubmed-article:19643079 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19643079 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19643079 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19643079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19643079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19643079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19643079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19643079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19643079 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19643079 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19643079 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:19643079 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:InoueIkuoI | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:KatayamaShige... | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:KomodaTsugika... | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:HokariShigeru... | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:MatsuiMasanor... | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:AkatsukaToshi... | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:TanakaKayokoK | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:AkitaMasumiM | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:NakanoTakanar... | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:TakahashiSeii... | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:SeoMakotoM | lld:pubmed |
| pubmed-article:19643079 | pubmed:author | pubmed-author:ShinozakiRina... | lld:pubmed |
| pubmed-article:19643079 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19643079 | pubmed:volume | 1788 | lld:pubmed |
| pubmed-article:19643079 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19643079 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19643079 | pubmed:pagination | 2222-8 | lld:pubmed |
| pubmed-article:19643079 | pubmed:meshHeading | pubmed-meshheading:19643079... | lld:pubmed |
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| pubmed-article:19643079 | pubmed:meshHeading | pubmed-meshheading:19643079... | lld:pubmed |
| pubmed-article:19643079 | pubmed:meshHeading | pubmed-meshheading:19643079... | lld:pubmed |
| pubmed-article:19643079 | pubmed:meshHeading | pubmed-meshheading:19643079... | lld:pubmed |
| pubmed-article:19643079 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19643079 | pubmed:articleTitle | A possible role of lysophospholipids produced by calcium-independent phospholipase A(2) in membrane-raft budding and fission. | lld:pubmed |
| pubmed-article:19643079 | pubmed:affiliation | Department of Biochemistry, Faculty of Medicine, Saitama Medical University, Saitama 350-0455, Japan. nk.takanari@gmail.com | lld:pubmed |
| pubmed-article:19643079 | pubmed:publicationType | Journal Article | lld:pubmed |
