Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/8587
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dc.contributor.authorTselepis, A. D.en
dc.contributor.authorKarabina, S. A. P.en
dc.contributor.authorStengel, D.en
dc.contributor.authorPiedagnel, R.en
dc.contributor.authorChapman, M. J.en
dc.contributor.authorNinio, E.en
dc.date.accessioned2015-11-24T16:42:44Z-
dc.date.available2015-11-24T16:42:44Z-
dc.identifier.issn0022-2275-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8587-
dc.rightsDefault Licence-
dc.subjectatherogenesisen
dc.subjectlipoproteinsen
dc.subjectmacrophagesen
dc.subjectplatelet-activating-factoren
dc.subjectlow-density-lipoproteinen
dc.subjectfactor acetylhydrolaseen
dc.subjectendoplasmic-reticulumen
dc.subjectdegrading acetylhydrolaseen
dc.subjectcatalytic activityen
dc.subjectbrefeldin-aen
dc.subjectdegradationen
dc.subjectexpressionen
dc.subjectrelevanceen
dc.titleN-linked glycosylation of macrophage-derived PAF-AH is a major determinant of enzyme association with plasma HDLen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000171803100015-
heal.identifier.secondaryhttp://www.jlr.org/content/42/10/1645.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2001-
heal.abstractHuman plasma PAF-AH (platelet-activating factor-acetylhydrolase) is a Ca2+-independent phospholipase A(2) of hematopoietic origin associated with LDL and HDL; it degrades PAF and oxidizes phospholipids. We show that human macrophages synthesize PAF-AH as a premedial Golgi precursor containing high mannose N-linked glycans. Secreted PAF-AH possesses a molecular mass of similar to 55 kDa and contains mature N-linked glycans. Secreted PAF-AH activity (90 +/- 4% of the total) bound to a wheat germ lectin column and could be eluted with N-acetylglucosamine, whereas digestion with N-acetylneuraminidase II completely abolished enzyme absorption. Tunicamycin significantly reduced cell-associated PAN-AH activity and inhibited enzyme secretion; but it did not alter the ratio of secreted to cell-associated enzyme (1.8 at 6 h and 3.1 at 24 h), suggesting that glycosylation is not essential for PAF-AH secretion. Digestion of cell-associated PAF-AH or secreted PAF-AH with peptide N-glycosidase F affected neither catalytic activity nor its resistance to proteolysis with trypsin or proteinase K, in addition, it did not affect PAF-AH association with LDL, but significantly increased its association with HDL. jlr We suggest that macrophage-derived PAF-AH contains heterogeneous asparagine-conjugated sugar chain(s) involving sialic acid, which hinders its association with HDL but does not influence the secretion, catalytic activity, or resistance of PAF-AH to proteases.en
heal.publisherLipid Research Inc.en
heal.journalNameJournal of Lipid Researchen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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