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Tyrosine phosphorylation and p72syk activation by an anti-glycoprotein Ib
monoclonal antibody
M Yanabu, Y Ozaki, S Nomura, T Miyake, Y Miyazaki, H Kagawa, Y Yamanaka, N Asazuma, K Satoh, S Kume, Y Komiyama and S Fukuhara
First Department of Internal Medicine, Kansai Medical University, Osaka,
Japan.
NNKY5-5, an IgG monoclonal antibody directed against the von Willebrand
factor-binding domain of glycoprotein (GP) Ib alpha, induced weak but
irreversible aggregation (or association) of platelets in citrate-
anticoagulated platelet-rich plasma. This phenomenon was defined as small
aggregate formation (SAF). Platelets in hirudin-anticoagulated plasma or
washed platelets showed little response to NNKY5-5 alone, but the antibody
potentiated aggregation induced by low concentrations of adenosine
diphosphate or platelet-activating factor. NNKY5-5 did not induce granule
release or intracellular Ca2+ mobilization. However, NNKY5-5 caused
tyrosine phosphorylation of a 64-kD protein and activation of a tyrosine
kinase, p72syk. An anti-Fc gamma II receptor antibody had no effect on SAF,
suggesting that NNKY5-5 activated platelets by interacting with
glycoprotein Ib. Fab' fragments of NNKY5- 5 did not induce SAF, but
potentiated aggregation induced by other agonists. The Fab' fragment of
NNKY5-5 induced the activation of p72syk, suggesting that such activation
was independent of the Fc gamma II receptor. Cross-linking of the
receptor-bound Fab' fragment of NNKY5- 5 with a secondary antibody induced
SAF. GRGDS peptide, chelation of extracellular Ca2+, and an anti-GPIIb/IIIa
antibody inhibited NNKY5-5- induced SAF, but had no effect on 64-kD protein
tyrosine phosphorylation or p72syk activations. Various inhibitors,
including aspirin and protein kinase C, had no effect on SAF, protein
tyrosine phosphorylation, or p72syk activation. In contrast, tyrphostin 47,
a potent tyrosine kinase inhibitor, inhibited NNKY5-5-induced SAF as well
as tyrosine phosphorylation and p72syk activation. Our findings suggest
that binding of NNKY5-5 to GPIb potentiates platelet aggregation by
facilitating the interaction between fibrinogen and GPIIb/IIIa through a
mechanism associated with p72syk activation and tyrosine phosphorylation of
a 64-kD protein.
Volume 89,
Issue 5,
pp. 1590-1598,
03/01/1997
Copyright © 1997 by The American Society of Hematology
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