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Blood, Vol. 95 No. 8 (April 15), 2000:
pp. 2600-2609
Cloning of the human platelet F11 receptor: a cell adhesion
molecule member of the immunoglobulin superfamily involved in
platelet aggregation
Malgorzata B. Sobocka,
Tomasz Sobocki,
Probal Banerjee,
Cipora Weiss,
Julie I. Rushbrook,
Allen J. Norin,
John Hartwig,
Moro O. Salifu,
Mariana S. Markell,
Anna Babinska,
Yigal H. Ehrlich, and
Elizabeth Kornecki
From the Departments of Anatomy/Cell Biology, Biochemistry and
Medicine/Renal Division, SUNY Downstate Medical Center, Brooklyn, NY;
Program in Neuroscience and the Departments of Chemistry and Biology,
CUNY/CSI, Staten Island, NY; and the Department of
Medicine/Division of Experimental Medicine and Hematology, Brigham and
Women's Hospital, Harvard Medical School, Boston, MA.
This study demonstrates that the human platelet F11 receptor (F11R)
functions as an adhesion molecule, and this finding is confirmed by the
structure of the protein as revealed by molecular cloning. The F11R is
a 32-/35-kd protein duplex that serves as the binding site through
which a stimulatory monoclonal antibody causes platelet aggregation and
granule secretion. A physiological role for the F11R protein was
demonstrated by its phosphorylation after the stimulation of platelets
by thrombin and collagen. A pathophysiological role for the F11R was
revealed by demonstrating the presence of F11R-antibodies in patients
with thrombocytopenia. Adhesion of platelets through the F11R resulted
in events characteristic of the action of cell adhesion molecules
(CAMs). To determine the structure of this protein, we cloned the F11R
cDNA from human platelets. The predicted amino acid sequence
demonstrated that it is an integral membrane protein and an
immunoglobulin superfamily member containing 2 extracellular C2-type
domains. The structure of the F11R as a member of a CAM family of
proteins and its activity in mediating adhesion confirm each another.
We conclude that the F11R is a platelet-membrane protein involved in 2 distinct processes initiated on the platelet surface. The first is
antibody-induced platelet aggregation and secretion that are dependent
on both the Fc RII and the GPIIb/IIIa integrin and that may be
involved in pathophysiological processes associated with certain
thrombocytopenias. The second is an F11R-mediated platelet adhesion
that is not dependent on either the FcRII or the fibrinogen receptor
and that appears to play a role in physiological processes associated
with platelet adhesion and aggregation.
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