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Papers In Press, published online ahead of print February 19, 2002
Department of Molecular Medicine, National Public Health Institute, Helsinki FIN-00251
Corresponding Author: christian.ehnholm{at}ktl.fi
Plasma phospholipid transfer protein (PLTP) plays an important role in lipoprotein metabolism. Two forms of PLTP exist in human plasma, one catalytically active (high activity form, HA-PLTP) and the other inactive (low activity form, LA-PLTP) [Oka et al. (2000) J. Lipid Res. 41, 1651-1657]. The two forms are associated with macromolecular complexes of different size. The apparent size of LA-PLTP is 520 kDa and that of HA-PLTP 160 kDa. Of the circulating PLTP mass only a minor portion is in the HA-PLTP form in normolipidemic subjects. In the present study we have isolated and partially characterized the LA and HA forms of PLTP. Both LA- and HA-PLTP bind to Heparin-Sepharose and can be separated by elution with 0-0.5 M NaCl gradient, with HA-PLTP displaying higher affinity for the matrix. LA-PLTP was further purified using hydrophobic butyl sepharose and anti-PLTP immunoaffinity chromatography steps. HA-PLTP was subjected to a second Heparin-Sepharose step and hydroxylapatite chromatography. Analysis of the two forms of PLTP by SDS-PAGE, Western blotting, immunoprecipitation and gel filtration demonstrates that LA-PLTP is complexed with apoA-I while HA-PLTP is not. Instead, HA-PLTP copurified with apoE. Based on these findings we suggest a model in which nascent PLTP enters the circulation as a high specific activity form not associated with apoA-I. During or after the transfer of lipolytic surface remnants to HDL, PLTP is transferred to apoA-I-containing HDL particles and thereby becomes part of the low-activity complex.
J. Biol. Chem, 10.1074/jbc.M112247200
Submitted on December 21, 2001
Revised on February 5, 2002
Accepted on February 15, 2002
Isolation and partial characterization of the inactive and active forms of human plasma phospholipid transfer protein (PLTP)
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