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Glycoprotein V is not the thrombin activation receptor on human blood
platelets
D Bienz, W Schnippering and KJ Clemetson
Thrombin activation of platelets involves two receptors: glycoprotein Ib
(GPIb), which affects the kinetics of the response; and, as a strong
candidate for the second, essential receptor, GPV, a hydrophobic, 82-kd
glycoprotein with an isoelectric point (pI) of pH 5.85 to 6.55. Whole
platelets were treated with endogenous platelets calcium-activated
proteases, yielding a major fragment, GPV8, with molecular weight (mol wt)
of 79 kilodaltons (kd). The fragment was purified by affinity
chromatography on wheat germ agglutinin followed by ion exchange
chromatography on DEAE-Sephacel using first a 0 to 0.7-mol/L and then a 0
to 0.3-mol/L NaCl gradient. A rabbit was immunized with the purified GPV8
for preparation of polyclonal antibodies. Crossed immunoelectrophoresis and
two-dimensional polyacrylamide gel electrophoresis (PAGE) electrophoretic
blotting with the separate phases of a Triton X-114 phase partition of
human platelets showed the characteristic pattern of GPV in the hydrophobic
phase. During thrombin- induced platelet aggregation GPV is hydrolysed,
releasing a fragment, GPVf1, to the supernatant. The fragment GPVf1 still
contains a thrombin- binding site. Anti-GPV antibodies blocked GPV
proteolysis, but did not inhibit platelet activation induced by thrombin.
We conclude that proteolysis of GPV by thrombin is not essential for
platelet activation.
Volume 68,
Issue 3,
pp. 720-725,
09/01/1986
Copyright © 1986 by The American Society of Hematology
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