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J. Lipid Res.
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A more recent version of this article appeared on December 1, 2004 Originally published In Press as doi:10.1194/jlr.M400222-JLR200 on September 16, 2004

Papers In Press, published online ahead of print September 17, 2004
J. Lipid Res., doi:10.1194/jlr.M400222-JLR200
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Submitted on June 14, 2004
Revised on August 20, 2004
Accepted on September 8, 2004

Apolipoprotein A-I induces translocation of protein kinase-Calpha to a cytosolic lipid-protein particle in astrocytes

Jin-ihci Ito, Hao Li, Yuko Nagayasu, Alireza Kheirollah, and Shinji Yokoyama

Biochemistry, Cell Biology and Metabolism, Nagoya City University Graduate School of Medical Sciences, Nagoya, Aichi 467-8601

Corresponding Author: syokoyam{at}med.nagoya-cu.ac.jp

Apolipoprotein (apo) A-I induces translocation of newly synthesized cholesterol as well as caveolin-1 to cytosolic lipid-protein particle (CLPP) fraction in astrocytes, prior to its appearance in high density lipoprotein generated in the medium (J. Biol. Chem. 277, 7929-7935, 2002). We here report association of signal-related molecules with CLPP. ApoA-I induces rapid translocation of protein kinase Calpha to the CLPP fraction and its phosphorylation in astrocytes. ApoA-I also induces translocation of phospholipase Cgamma to CLPP. Diacylglyceride production is increased by apoA-I in the cells having a maximum at 5 min after the stimulation, and the increase takes place also in the CLPP fraction. An inhibitor of receptor-coupled phospholipase C, U73122, inhibited all the apoA-I-induced events, such as diacylglyceride production, cholesterol translocation to the cytosol, release of cholesterol, and translocation of protein kinase Calpha into the CLPP fraction. CLPP may thus be involved in the apoA-I-initiated signal transduction in astrocytes that is related with intracellular cholesterol trafficking for generation of high density lipoprotein in the brain.


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