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Journal of Lipid Research, Vol 29, 349-361, Copyright © 1988 by Lipid Research, Inc.
TA Musliner, HJ Michenfelder and RM Krauss
Interactions of high density lipoproteins (HDL) with very low (VLDL) and
low (LDL) density lipoproteins were investigated during in vitro lipolysis
in the presence of limited free fatty acid acceptor. Previous studies had
shown that lipid products accumulating on lipoproteins under these
conditions promote the formation of physical complexes between
apolipoprotein B-containing particles (Biochim. Biophys. Acta, 1987. 919:
97-110). The presence of increasing concentrations of HDL or delipidated
HDL progressively diminished VLDL-LDL complex formation. At the same time,
association of HDL-derived apolipoprotein (apo) A-I with both VLDL and LDL
could be demonstrated by autoradiography of gradient gel electrophoretic
blots, immunoblotting, and apolipoprotein analyses of reisolated
lipoproteins. The LDL increased in buoyancy and particle diameter, and
became enriched in glycerides relative to cholesterol. Both HDL2 and HDL3
increased in particle diameter, buoyancy, and relative glyceride content,
and small amounts of apoA-I appeared in newly formed particles of less than
75 A diameter. Association of apoA- I with VLDL or LDL could be reproduced
by addition of lipid extracts of lipolyzed VLDL or purified free fatty
acids in the absence of lipolysis, and was progressively inhibited by the
presence of increasing amounts of albumin. We conclude that lipolysis
products promote multiple interactions at the surface of triglyceride-rich
lipoproteins undergoing lipolysis, including physical complex formation
with other lipoprotein particles and transfers of lipids and
apolipoproteins. These processes may facilitate remodeling of lipoproteins
in the course of their intravascular metabolism.
ARTICLES
Interactions of high density lipoproteins with very low and low density lipoproteins during lipolysis
Clinical Investigation Center, Naval Hospital, Oakland, CA 94627.
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