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• W1974703721 abstract "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 GPIbβ 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 GPIbβ. The novel interaction of GPVI and calmodulin may regulate aspects of GPVI function." @default.
• W1974703721 created "2016-06-24" @default.
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• W1974703721 date "2002-06-01" @default.
• W1974703721 modified "2023-10-07" @default.
• W1974703721 title "Interaction of calmodulin with the cytoplasmic domain of platelet glycoprotein VI" @default.
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• W1974703721 doi "https://doi.org/10.1182/blood-2001-11-0008" @default.
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