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Blood, Vol. 95 No. 3 (February 1), 2000:
pp. 886-893
Structural and functional characterization of the mouse von
Willebrand factor receptor GPIb-IX with novel monoclonal antibodies
Wolfgang Bergmeier,
Kirsten Rackebrandt,
Werner Schröder,
Hubert Zirngibl, and
Bernhard Nieswandt
From the Department of Molecular Oncology, General Surgery,
University of Witten-Herdecke, and the BAYER Pharma Research Center,
Wuppertal, Germany.
Five novel monoclonal antibodies (mAbs; p0p 1-5) were used to
characterize the structural and functional properties and the in vivo
expression of the murine GPIb-IX complex (von Willebrand factor
receptor). The molecular weights of the subunits are similar to
the human homologs: GPIb (150 kd), GPIb (25 kd), and GPIX (25 kd). Activation of platelets with thrombin or PMA predominantly induced
shedding of glycocalicin (GC; 130 kd) but only low levels of receptor
internalization. The GC concentration in normal mouse plasma was found
to be at least 10 times higher than that described for human plasma
(approximately 25 µg/mL versus 1-2 µg/mL). Two additional cleavage
sites for unidentified platelet-derived proteases were found on
GPIb, as demonstrated by the generation of 3 N-terminal fragments
during in vitro incubation of washed platelets (GC, 60 kd, 45 kd).
Occupancy of GPIb with p0p mAbs or F(ab)2-fragments resulted in aggregate formation in vitro and rapid irreversible thrombocytopenia in vivo, irrespective of the exact binding
epitopes of the individual antibodies. GPIb-IX was not detectable
immunohistochemically on endothelial cells in the major organs under
normal or inflammatory conditions. The authors conclude that the mouse
system might become an interesting model for studies on GPIb-IX
function and regulation.
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