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Variability of integrin alpha 2 beta 1 activity on human platelets
TJ Kunicki, R Orchekowski, D Annis and Y Honda
Blood Research Institute, Blood Center of Southeastern Wisconsin,
Milwaukee.
The activity and surface antigenicity of alpha 2 beta 1 on platelets from
27 normal subjects were found to vary significantly. A fourfold range of
surface antigen correlates with a 20-fold variation in the ability of
nonactivated, washed platelets to adhere to type I collagen and a fivefold
variation in the adhesion of platelets to type III collagen. These
differences in surface receptor are reflected in significant variation in
the lag time required for type I collagen- induced platelet aggregation in
platelet-rich plasma. Among the same individuals, no difference was
observed in surface levels or activities of two other platelet integrins,
the fibronectin receptor alpha 5 beta 1 and the fibrinogen receptor alpha
IIb beta 3. In all cases studied, we observed complimentary differences in
the incorporation of 125I into surface alpha 2 beta 1, in quantity of
surface alpha 2 beta 1 antigens, and in alpha 2 beta 1 collagen receptor
activity. Despite variations in these parameters, there was no difference
in the electrophoretic mobility or isoelectric point of either integrin
subunit among the individuals studied. The wide range of activity and
antigenicity of this platelet collagen receptor may result from
polymorphism(s) in the alpha 2 beta 1 genes, or the activity of alpha 2
beta 1 may be variably regulated by another gene product. The heterogeneity
of platelet alpha 2 beta 1 that we describe in this report certainly
explains previous discrepancies concerning the contributions of this
integrin to platelet adhesion to collagens. Most importantly, differences
in surface collagen receptor activity may correlate with a long-term risk
toward thrombosis, impaired hemostasis, and/or cardiovascular disease.
Volume 82,
Issue 9,
pp. 2693-2703,
11/01/1993
Copyright © 1993 by The American Society of Hematology
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