Mild stretch activates cPLA(2) in alveolar type II epithelial cells independently through the MEK/ERK and PI3K pathways

dc.contributor.authorLetsiou, E.en
dc.contributor.authorKitsiouli, E.en
dc.contributor.authorNakos, G.en
dc.contributor.authorLekka, M. E.en
dc.date.accessioned2015-11-24T16:41:53Z
dc.date.available2015-11-24T16:41:53Z
dc.identifier.issn1388-1981-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8484
dc.rightsDefault Licence-
dc.subjectmechanical stretchen
dc.subjecta549 cellsen
dc.subjectcytosolic pla(2)en
dc.subjecterk1/2en
dc.subjectpi3 kinaseen
dc.subjectalveolar epithelial cellsen
dc.subjectcytosolic phospholipase a(2)en
dc.subjectprotein-kinase kinaseen
dc.subjectinduced lung injuryen
dc.subjectsurfactant secretionen
dc.subjectarachidonic-aciden
dc.subjectmap kinaseen
dc.subjectin-vitroen
dc.subjectinhibitoren
dc.subjectapoptosisen
dc.subjectreleaseen
dc.titleMild stretch activates cPLA(2) in alveolar type II epithelial cells independently through the MEK/ERK and PI3K pathwaysen
heal.abstractAlveolar epithelial type II cells (AT II) in which lung surfactant synthesis and secretion take place, are subjected to low magnitude stretch during normal breathing. The aim of the study was to explore the effect of mild stretch on phospholipase A(2) (PLA(2)) activation, an enzyme known to be involved in surfactant secretion. In A549 cells (a model of AT II cells), we showed, using a fluorometric assay, that stretch triggers an increase of total PLA(2) activity. Western blot experiments revealed that the cytosolic isoform cPLA(2) is rapidly phosphorylated under stretch, in addition to a modest increase in cPLA(2) mRNA levels. Treatment of A549 cells with selective inhibitors of the MEK/ERK pathway significantly attenuated the stretch-induced cPLA(2) phosphotylation. A strong interaction of cPLA(2) and pERK enzymes was demonstrated by immunoprecipitation. We also found that inhibition of PI3K pathway attenuated cPLA(2) activation after stretch, without affecting pERK levels. Our results suggest that low magnitude stretch can induce cPLA(2) phosphorylation through the MEK/ERK and PI3K-Akt pathways, independently. (C) 2010 Elsevier B.V. All rights reserved.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primaryDOI 10.1016/j.bbalip.2010.12.007-
heal.identifier.secondary<Go to ISI>://000291192600002-
heal.identifier.secondaryhttp://ac.els-cdn.com/S1388198110002556/1-s2.0-S1388198110002556-main.pdf?_tid=0eb6a866b490af30cb571543ab478662&acdnat=1333033907_1199deab89a7dc93c432e4cd67896c78-
heal.journalNameBiochimica Et Biophysica Acta-Molecular and Cell Biology of Lipidsen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2011-
heal.publisherElsevieren
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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