Micellar Lipoproteins as the Possible Storage and Translocation Form of Intracellular Diacylglycerol

Previous work indicated that diacylglycerol (DG) molecules translocate across the cytoplasm of mammalian cells, a process relevant to the signalling role of this lipid as protein kinase C activator. Here we investigated the possible mechanism underlying DG translocation. We examined the interaction...

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Published in:Biochemical and biophysical research communications 1998-02, Vol.243 (3), p.669-673
Main Authors: Florin-Christensen, J., D'Alessio, C., Arighi, C., Caramelo, J., Florin-Christensen, M., Delfino, J.M.
Format: Article
Language:English
Subjects:
Animals
Biological Transport
Chromatography, Agarose
Cytosol - metabolism
Dextrans - metabolism
Diglycerides - metabolism
Female
Lipoproteins - metabolism
Liver - ultrastructure
Micelles
Oleic Acid - metabolism
Rats
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Summary:Previous work indicated that diacylglycerol (DG) molecules translocate across the cytoplasm of mammalian cells, a process relevant to the signalling role of this lipid as protein kinase C activator. Here we investigated the possible mechanism underlying DG translocation. We examined the interaction between 1,2-di-[1-14C]oleoyl-sn-glycerol and rat liver cytosol (rlc) using assays based on Lipidex-1000 and on coelution on Sepharose CL 6B. We measured high DG binding activity and found that it resides in cytosolic proteins and not in cytosolic lipids. Chromatography of rlc proteins on Sepharose CL 6B showed profiles in which the activity measured by either method coincided. Further, we showed that the DG-rlc protein interaction results in the stabilization of DG in a micellar form, eluting in the void volume of Sepharose CL 6B. Such stabilized micelles are reminiscent of insect lipophorins and may represent a new, thus far unrecognized, mode of lipid transport within living cells.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1998.8155