N-linked glycosylation of macrophage-derived PAF-AH is a major determinant of enzyme association with plasma HDL
| dc.contributor.author | Tselepis, A. D. | en |
| dc.contributor.author | Karabina, S. A. P. | en |
| dc.contributor.author | Stengel, D. | en |
| dc.contributor.author | Piedagnel, R. | en |
| dc.contributor.author | Chapman, M. J. | en |
| dc.contributor.author | Ninio, E. | en |
| dc.date.accessioned | 2015-11-24T16:42:44Z | |
| dc.date.available | 2015-11-24T16:42:44Z | |
| dc.identifier.issn | 0022-2275 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8587 | |
| dc.rights | Default Licence | - |
| dc.subject | atherogenesis | en |
| dc.subject | lipoproteins | en |
| dc.subject | macrophages | en |
| dc.subject | platelet-activating-factor | en |
| dc.subject | low-density-lipoprotein | en |
| dc.subject | factor acetylhydrolase | en |
| dc.subject | endoplasmic-reticulum | en |
| dc.subject | degrading acetylhydrolase | en |
| dc.subject | catalytic activity | en |
| dc.subject | brefeldin-a | en |
| dc.subject | degradation | en |
| dc.subject | expression | en |
| dc.subject | relevance | en |
| dc.title | N-linked glycosylation of macrophage-derived PAF-AH is a major determinant of enzyme association with plasma HDL | en |
| heal.abstract | Human 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.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.secondary | <Go to ISI>://000171803100015 | - |
| heal.identifier.secondary | http://www.jlr.org/content/42/10/1645.full.pdf | - |
| heal.journalName | Journal of Lipid Research | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2001 | - |
| heal.publisher | Lipid Research Inc. | en |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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