Regulation of Phospholipid Scramblase Activity during Apoptosis and Cell Activation by Protein Kinase CÎ
Phospholipid scramblase induces nonspecific bidirectional movement of phospholipids across the membrane during cell activation and has been proposed to mediate the appearance of phosphatidylserine (PS) in the plasma membrane outer leaflet during apoptosis, a cell surface change that is critical for...
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Veröffentlicht in: | The Journal of biological chemistry 2000-07, Vol.275 (30), p.23065 |
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Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Phospholipid scramblase induces nonspecific bidirectional movement of phospholipids across the membrane during cell activation
and has been proposed to mediate the appearance of phosphatidylserine (PS) in the plasma membrane outer leaflet during apoptosis,
a cell surface change that is critical for apoptotic cell removal. We report here that protein kinase C (PKC) δ plays an important
role in activated transbilayer movement of phospholipids and surface PS exposure by directly enhancing the activity of phospholipid
scramblase. Specific inhibition of PKCδ by rottlerin prevented both apoptosis- and activation-induced scramblase activity.
PKCδ was either selectively cleaved and activated in a caspase 3-dependent manner (during apoptosis) or translocated to the
plasma membrane (in stimulated cells) and could directly phosphorylate scramblase immunoprecipitated from Jurkat cells. Furthermore,
reconstitution of PKCδ and scramblase, but not scramblase or PKCδ alone in Chinese hamster ovary cells demonstrated enhanced
scramblase activity. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.M003116200 |