A Specific Phospholipase C Activity Regulates Phosphatidylinositol Levels in Lung Surfactant of Patients with Acute Respiratory Distress Syndrome

dc.contributor.authorSpyridakis, S.en
dc.contributor.authorLeondaritis, G.en
dc.contributor.authorNakos, G.en
dc.contributor.authorLekka, M. E.en
dc.contributor.authorGalanopoulou, D.en
dc.date.accessioned2015-11-24T16:38:54Z
dc.date.available2015-11-24T16:38:54Z
dc.identifier.issn1044-1549-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8100
dc.rightsDefault Licence-
dc.subjectphospholipase cen
dc.subjectphosphatidylinositolen
dc.subjectphosphatidylinositol 4,5-bisphosphateen
dc.subjectlung surfactanten
dc.subjectacute respiratory distress syndromeen
dc.subjectpulmonary surfactanten
dc.subjectprotein-den
dc.subjectkinetic-analysisen
dc.subjectbindingen
dc.subjectstimulationen
dc.subjectmacrophagesen
dc.subjectdysfunctionen
dc.subjectmetabolismen
dc.subjectmechanismsen
dc.subjectexpressionen
dc.titleA Specific Phospholipase C Activity Regulates Phosphatidylinositol Levels in Lung Surfactant of Patients with Acute Respiratory Distress Syndromeen
heal.abstractLung surfactant (LS) is a lipid-rich material lining the inside of the lungs. It reduces surface tension at the liquid/air interface and thus, it confers protection of the alveoli from collapsing. The surface-active component of LS is dipalmitoyl-phosphatidylcholine, while anionic phospholipids such as phosphatidylinositol (PtdIns) and primarily phosphatidylglycerol are involved in the stabilization of the LS monolayer. The exact role of PtdIns in this system is not well-understood; however, PtdIns levels change dramatically during the acute respiratory distress syndrome (ARDS) evolution. In this report we present evidence of a phosphoinositide-specific phospholipase C (PI-PLC) activity in bronchoalveolar lavage (BAL) fluid, which may regulate PtdIns levels. Characterization of this extracellular activity showed specificity for PtdIns and phosphatidylinositol 4,5-bisphosphate, sharing the typical substrate concentration-, pH-, and calcium-dependencies with mammalian PI-PLCs. Fractionation of BAL fluid showed that PI-PLC did not co-fractionate with large surfactant aggregates, but it was found mainly in the soluble fraction. Importantly, analysis of BAL samples from control subjects and from patients with ARDS showed that the PI-PLC specific activity was decreased by 4-fold in ARDS samples concurrently with the increase in BAL PtdIns levels. Thus, we have identified for the first time an extracellular PI-PLC enzyme activity that may be acutely involved in the regulation of PtdIns levels in LS.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primaryDOI 10.1165/rcmb.2009-0078OC-
heal.identifier.secondary<Go to ISI>://000275080900013-
heal.identifier.secondaryhttp://ajrcmb.atsjournals.org/content/42/3/357.full.pdf-
heal.journalNameAm J Respir Cell Mol Biolen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2010-
heal.publisherAmerican Thoracic Societyen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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