| pubmed-article:12847272 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12847272 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:12847272 | lifeskim:mentions | umls-concept:C0031676 | lld:lifeskim |
| pubmed-article:12847272 | lifeskim:mentions | umls-concept:C0143146 | lld:lifeskim |
| pubmed-article:12847272 | lifeskim:mentions | umls-concept:C2756983 | lld:lifeskim |
| pubmed-article:12847272 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:12847272 | lifeskim:mentions | umls-concept:C0038891 | lld:lifeskim |
| pubmed-article:12847272 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:12847272 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12847272 | pubmed:dateCreated | 2003-7-8 | lld:pubmed |
| pubmed-article:12847272 | pubmed:abstractText | Hydrolysis of surfactant phospholipids by secreted phospholipases A(2) (sPLA(2)) contributes to surfactant dysfunction in acute respiratory distress syndrome. The present study demonstrates that sPLA(2)-IIA, sPLA(2)-V, and sPLA(2)-X efficiently hydrolyze surfactant phospholipids in vitro. In contrast, sPLA(2)-IIC, -IID, -IIE, and -IIF have no effect. Since purified surfactant protein A (SP-A) has been shown to inhibit sPLA(2)-IIA activity, we investigated the in vitro effect of SP-A on the other active sPLA(2) and the consequences of sPLA(2)-IIA inhibition by SP-A on surfactant phospholipid hydrolysis. SP-A inhibits sPLA(2)-X activity, but fails to interfere with that of sPLA(2)-V. Moreover, in vitro inhibition of sPLA(2)-IIA-induces surfactant phospholipid hydrolysis correlates with the concentration of SP-A in surfactant. Intratracheal administration of sPLA(2)-IIA to mice causes hydrolysis of surfactant phosphatidylglycerol. Interestingly, such hydrolysis is significantly higher for SP-A gene-targeted mice, showing the in vivo inhibitory effect of SP-A on sPLA(2)-IIA activity. Administration of sPLA(2)-IIA also induces respiratory distress, which is more pronounced in SP-A gene-targeted mice than in wild-type mice. We conclude that SP-A inhibits sPLA(2) activity, which may play a protective role by maintaining surfactant integrity during lung injury. | lld:pubmed |
| pubmed-article:12847272 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12847272 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12847272 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12847272 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:12847272 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12847272 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12847272 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:12847272 | pubmed:author | pubmed-author:GelbMichael... | lld:pubmed |
| pubmed-article:12847272 | pubmed:author | pubmed-author:LambeauGérard... | lld:pubmed |
| pubmed-article:12847272 | pubmed:author | pubmed-author:WhitsettJeffr... | lld:pubmed |
| pubmed-article:12847272 | pubmed:author | pubmed-author:ChignardMiche... | lld:pubmed |
| pubmed-article:12847272 | pubmed:author | pubmed-author:TouquiLhousse... | lld:pubmed |
| pubmed-article:12847272 | pubmed:author | pubmed-author:ChabotSophieS | lld:pubmed |
| pubmed-article:12847272 | pubmed:author | pubmed-author:BalloyViviane... | lld:pubmed |
| pubmed-article:12847272 | pubmed:author | pubmed-author:KoumanovKamen... | lld:pubmed |
| pubmed-article:12847272 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12847272 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:12847272 | pubmed:volume | 171 | lld:pubmed |
| pubmed-article:12847272 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12847272 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12847272 | pubmed:pagination | 995-1000 | lld:pubmed |
| pubmed-article:12847272 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:12847272 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12847272 | pubmed:articleTitle | Inhibitory effects of surfactant protein A on surfactant phospholipid hydrolysis by secreted phospholipases A2. | lld:pubmed |
| pubmed-article:12847272 | pubmed:affiliation | Unité de Défense Innée et Inflammation, Institut Pasteur, Institut National de la Santé et de la Recherche Médicale E 336, Paris, France. | lld:pubmed |
| pubmed-article:12847272 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12847272 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12847272 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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