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J Biol Chem, Vol. 274, Issue 36, 25913-25920, September 3, 1999
From the The presence of a lipoprotein profile
with abundance of small, dense low density lipoproteins (LDL), low
levels of high density lipoproteins (HDL), and elevated levels of
triglyceride-rich very low density lipoproteins is associated with an
increased risk for coronary heart disease. The atherogenicity of small,
dense LDL is believed to be one of the main reasons for this
association. This particle contains less phospholipids (PL) and
unesterified cholesterol than large LDL, and the apoB-100 appears to
occupy a more extensive area at its surface. Although there are
experiments that suggest a metabolic pathway leading to the
overproduction of small, dense LDL, no clear molecular model exists to
explain its association with atherogenesis. A current hypothesis is
that small, dense LDL, because of its higher affinity for
proteoglycans, is entrapped in the intima extracellular matrix and is
more susceptible to oxidative modifications than large LDL. Here we
describe how a specific reduction of approximately 50% of the PL of a
normal buoyant LDL by immobilized phospholipase A2
(PLA2) (EC 3.1.1.4) produces smaller and denser particles
without inducing significant lipoprotein aggregation (<5%). These
smaller LDL particles display a higher tendency to form nonsoluble
complexes with proteoglycans and glycosaminoglycans than the parent
LDL. Binding parameters of LDL and glycosaminoglycans and proteoglycans
produced by human arterial smooth muscle cells were measured at near to
physiological conditions. The PLA2-modified LDL has about 2 times higher affinity for the sulfated polysaccharides than control
LDL. In addition, incubation of human plasma in the presence of
PLA2 generated smaller LDL and HDL particles compared with
the control plasma incubated without PLA2. These in
vitro results indicate that the reduction of surface PL
characteristic of small, dense LDL subfractions, besides contributing
to its small size and density, may enhance its tendency to be retained
by proteoglycans.
Phospholipase A2 Modification of Low Density
Lipoproteins Forms Small High Density Particles with Increased Affinity
for Proteoglycans and Glycosaminoglycans
,¶,
Wallenberg Laboratory for
Cardiovascular Research,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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