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J. Biol. Chem., Vol. 275, Issue 43, 33480-33486, October 27, 2000
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From the Lipoprotein and Atherosclerosis Research Group and the
Departments of Pathology & Laboratory Medicine and Biochemistry,
Microbiology & Immunology, University of Ottawa Heart Institute,
Ottawa, Ontario K1Y 4W7, Canada
Association of hepatic lipase (HL) with pure
heparan sulfate proteoglycans (HSPG) has little effect on hydrolysis of
high density lipoprotein (HDL) particles, but significantly inhibits (>80%) the hydrolysis of low (LDL) and very low density lipoproteins (VLDL). Lipolytic inhibition is associated with a differential ability
of the lipoproteins to remove HL from the HSPG. LDL and VLDL are unable
to displace HL, whereas HDL readily displaces HL from the HSPG. These
data show that HSPG-bound HL is inactive. Purified apolipoprotein (apo)
A-I is more efficient than HDL at liberating HL from HSPG, and HL
displacement is associated with the direct binding of apoA-I to HSPG.
However, displacement of HL by apoA-I does not enhance hydrolysis of
VLDL particles. This appears due to the direct inhibition of HL by
apoA-I. Both apoA-I and HDL are able to inhibit VLDL lipid hydrolysis
by up to 60%. Inhibition of VLDL hydrolysis is associated with the
binding of apoA-I to the surface of the VLDL particle and a concomitant
decreased affinity for HL. These data show that apoA-I can regulate
lipid hydrolysis by HL by liberating/activating the enzyme from cell surface proteoglycans and by directly modulating lipoprotein binding and hydrolysis.
Apolipoprotein A-I Regulates Lipid Hydrolysis by Hepatic
Lipase*
,
*
This work was supported by a grant from the Medical Research
Council of Canada.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.
Supported by a postgraduate scholarship from the Ontario Graduate
Scholarship Program and the Natural Sciences and Engineering Research
Council of Canada.
§
To whom correspondence should be addressed: Lipoprotein and
Atherosclerosis Research Group, University of Ottawa Heart Inst., 40 Ruskin St., Ottawa, Ontario K1Y 4W7, Canada. Tel.: 613-761-4822; Fax:
613-761-5281; E-mail: dsparks@ottawaheart.ca.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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