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Prepublished online as a Blood First Edition Paper on April 17, 2002; DOI 10.1182/blood-2001-11-0008.
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Blood, 1 June 2002, Vol. 99, No. 11, pp. 4219-4221
BRIEF REPORT
Interaction of calmodulin with the cytoplasmic domain of platelet
glycoprotein VI
Robert K. Andrews,
Katsue Suzuki-Inoue,
Yang Shen,
David Tulasne,
Stephen P. Watson, and
Michael C. Berndt
From the Hazel and Pip Appel Vascular Biology
Laboratory, Baker Medical Research Institute, Melbourne; the Department
of Biochemistry and Molecular Biology, Monash University, Clayton,
Victoria, Australia; and the Department of Pharmacology, University of
Oxford, United Kingdom.
The platelet collagen receptor, glycoprotein VI (GPVI), and
GPIb-IX-V, which binds von Willebrand factor, initiate platelet aggregation at low or high shear stress, respectively. We recently reported that positively charged, membrane-proximal sequences within
cytoplasmic domains of GPIb and GPV of GPIb-IX-V bind calmodulin. We
now show that GPVI also binds calmodulin as follows (1) calmodulin
coimmunoprecipitated with GPVI from resting platelet lysates using an
anti-GPVI IgG, but partially dissociated in platelets activated by
collagen or collagen-related peptide; (2) calmodulin coprecipitated
from platelet lysates with maltose-binding protein (MBP)-GPVI
cytoplasmic domain fusion protein, but not MBP alone; (3) GPVI-related
synthetic peptide based on the membrane-proximal sequence,
His269-Pro287, induced a shift in calmodulin migration on nondenaturing
gels, an assay that identifies calmodulin-binding peptides.
His269-Pro287 is analogous to the calmodulin-binding sequence in
GPIb. The novel interaction of GPVI and calmodulin may regulate
aspects of GPVI function.
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