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Defensin stimulates the binding of lipoprotein (a) to human vascular
endothelial and smooth muscle cells
AA Higazi, E Lavi, K Bdeir, AM Ulrich, DG Jamieson, DJ Rader, DC Usher, W Kane, T Ganz and DB Cines
Department of Pathology, University of Pennsylvania Medical Center,
Philadelphia, USA.
There is evidence to suggest that elevated plasma levels of lipoprotein (a)
[Lp(a)] represent a risk factor for the development of atherosclerotic
vascular disease, but the mechanism by which this lipoprotein localizes to
involved vessels is only partially understood. In view of studies
suggesting a link between inflammation and atherosclerosis and our previous
finding that leukocyte defensin modulates the interaction of plasminogen
and tissue-type plasminogen activator with cultured human endothelial
cells, we examined the effect of this peptide on the binding of Lp(a) to
cultured vascular endothelium and vascular smooth muscle cells. Defensin
increased the binding of Lp(a) to endothelial cells approximately fourfold
and to smooth muscle cells approximately sixfold. Defensin caused a
comparable increase in the amount of Lp(a) internalized by each cell type,
but Lp(a) internalized as a consequence of defensin being present was not
degraded, resulting in a marked increase in the total amount of cell-
associated lipoprotein. Abundant defensin was found in endothelium and in
intimal smooth muscle cells of atherosclerotic human cerebral arteries,
regions also invested with Lp(a). These studies suggest that defensin
released from activated or senescent neutrophils may contribute to the
localization and persistence of Lp(a) in human vessels and thereby
predispose to the development of atherosclerosis.
Volume 89,
Issue 12,
pp. 4290-4298,
06/15/1997
Copyright © 1997 by The American Society of Hematology
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