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J. Biol. Chem., Vol. 275, Issue 48, 37504-37509, December 1, 2000
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From the The aim of the present study was to identify the
protein that accounts for the cholesteryl ester transfer protein
(CETP)-inhibitory activity that is specifically associated with human
plasma high density lipoproteins (HDL). To this end, human HDL
apolipoproteins were fractionated by preparative polyacrylamide
gradient gel electrophoresis, and 30 distinct protein fractions with
molecular masses ranging from 80 down to 2 kDa were tested for
their ability to inhibit CETP activity. One single apolipoprotein
fraction was able to completely inhibit CETP activity. The N-terminal
sequence of the 6-kDa protein inhibitor matched the N-terminal sequence
of human apoC-I, the inhibition was completely blocked by specific
anti-apolipoprotein C-I antibodies, and mass spectrometry analysis
confirmed the identity of the isolated inhibitor with full-length human
apoC-I. Pure apoC-I was able to abolish CETP activity in a
concentration-dependent manner and with a high efficiency
(IC50 = 100 nmol/liter). The inhibitory potency of
total delipidated HDL apolipoproteins completely disappeared after a
treatment with anti-apolipoprotein C-I antibodies, and the apoC-I
deprivation of native plasma HDL by immunoaffinity chromatography
produced a mean 43% rise in cholesteryl ester transfer rates. The main
localization of apoC-I in HDL and not in low density lipoprotein in
normolipidemic plasma provides further support for the specific
property of HDL in inhibiting CETP activity.
Human Apolipoprotein C-I Accounts for the Ability of Plasma High
Density Lipoproteins to Inhibit the Cholesteryl Ester Transfer Protein
Activity*
,,,,,¶
Laboratoire de Biochimie des
Lipoprotéines-INSERM U498, Hôpital du Bocage, BP1542, 21034 Dijon Cedex, France and the § Laboratoire de Biologie de la
Communication Cellulaire-INSERM U338, Centre de Neurochimie du CNRS,
67084 Strasbourg Cedex, France
*
This work was supported by the Université de
Bourgogne, the Conseil Régional de Bourgogne, and INSERM.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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