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Interaction of plasma lipoproteins with human platelets
LK Curtiss and EF Plow
Human plasma low density lipoproteins (LDL) and high density lipoproteins
(HDL) were radioiodinated and their interaction with washed human platelets
was assessed. Both ligands were bound by the platelet at 37 degrees C, and
an apparent equilibrium was attained within two hours. Minimal binding was
observed at 22 degrees C or 4 degrees C. The specificity of these
interactions was indicated by the observations that: (a) labeled and
nonlabeled lipoproteins interacted with the platelet with the same apparent
affinity; (b) nonlabeled lipoproteins inhibited binding, whereas unrelated
plasma proteins did not; and (c) the platelet-bound ligands exhibited the
appropriate apoprotein chain compositions when analyzed by polyacrylamide
gel electrophoresis. Binding of HDL and LDL was found to be independent of
the state of platelet activation and did not require divalent ions. Binding
of HDL to the platelet was saturable, and a class of sites that maximally
bound 1,585 +/- 390 HDL particles, with a dissociation constant of 3.1 X
10(-8) mol/L, was identified. Binding of LDL to the platelet was more
complex, but evidence for a class of sites that bound 7,075 +/- 4,800 LDL
particles, with a dissociation constant of 4 X 10(- 8) mol/L, was found.
LDL was a poor inhibitor of 125I-HDL binding to the platelet, whereas HDL
was an effective inhibitor of 125I-LDL binding. The capacity of HDL to bind
or inhibit LDL binding was not dependent on its apoprotein E content. These
results are most readily interpreted in terms of two types of lipoprotein
interaction sites on platelets: (1) an HDL binding site that does not bind
or interacts poorly with LDL, and (2) an LDL binding site that recognizes
or is otherwise altered by HDL. The HDL site may be similar to the HDL
receptor expressed by steroidogenic tissues in terms of apoprotein
specificity. The LDL site is not the same as the LDL receptor of most
extrahepatic cells.
Volume 64,
Issue 2,
pp. 365-374,
08/01/1984
Copyright © 1984 by The American Society of Hematology
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