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GPI-anchored proteins and glycoconjugates segregate into lipid rafts in Kinetoplastida.

Denny, P.W. and Field, M.C. and Smith, D.F. (2001) 'GPI-anchored proteins and glycoconjugates segregate into lipid rafts in Kinetoplastida.', FEBS letters., 491 (1-2). pp. 148-153.


The plasma membranes of the divergent eukaryotic parasites, Leishmania and Trypanosoma, are highly specialised, with a thick coat of glycoconjugates and glycoproteins playing a central role in virulence. Unusually, the majority of these surface macro-molecules are attached to the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor. In mammalian cells and yeast, many GPI-anchored molecules associate with sphingolipid and cholesterol-rich detergent-resistant membranes, known as lipid rafts. Here we show that GPI-anchored parasite macro-molecules (but not the dual acylated Leishmania surface protein (hydrophilic acylated surface protein) or a subset of the GPI-anchored glycoinositol phospholipid glycolipids) are enriched in a sphingolipid/sterol-rich fraction resistant to cold detergent extraction. This observation is consistent with the presence of functional lipid rafts in these ancient, highly polarised organisms.

Item Type:Article
Keywords:Lipid raft, Kinetoplastida, Glycosylphosphatidylinositol anchor, Sphingolipid, Sterol.
Full text:(AM) Accepted Manuscript
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Record Created:18 Feb 2009
Last Modified:13 Jan 2014 16:52

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