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A more recent version of this article appeared on September 1, 2003

Papers In Press, published online ahead of print June 16, 2003
J. Lipid Res., doi:10.1194/jlr.M300059-JLR200
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Submitted on February 4, 2003
Revised on May 16, 2003
Accepted on June 5, 2003

Phospholipid transfer protein (PLTP) secreted by HepG2 cells resembles the high-activity PLTP form in human plasma

Sarah Siggins, Matti Jauhiainen, Vesa M. Olkkonen, Jukka Tenhunen, and Christian Ehnholm

Department of Molecular Medicine, National Public Health Institute, Helsinki FIN-00251

Corresponding Author: sarah.siggins{at}ktl.fi

Plasma phospholipid transfer protein (PLTP) is an important regulator of plasma high density lipoprotein (HDL) levels and HDL particle distribution. The protein is present in the circulation in two forms, one with high and the other with low phospholipid transfer activity. We have used the human hepatoma cell line, HepG2, as a model to study the PLTP secreted from hepatic cells. PLTP activity was secreted by the cells into serum-free culture medium as a function of time. However, modification of a previously established ELISA mass assay to include a denaturing sample pre-treatment with the anionic detergent sodium dodecyl sulphate (SDS) was required for the detection of the secreted PLTP protein. The HepG2 PLTP could be enriched by Heparin-Sepharose affinity chromatography and eluted in size-exclusion chromatography at a position corresponding to the size of 160 kDa. PLTP co-eluted with apoE but not with apoB-100 or apoA-I. A portion of PLTP was retained by an anti-apoE immunoaffinity column together with apoE, suggesting an interaction between these two proteins. Furthermore, antibodies against apoE but not those against apoB-100 or apoA-I were capable of inhibiting PLTP activity. These results show that the HepG2-derived PLTP resembles in several aspects the high-activity form of PLTP found in human plasma. The findings support a model in which PLTP is secreted by the liver as an active form that is, during lipid transfer processes between lipolysed chylomicrons/VLDL and HDL, converted into the low-activity complex.


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