Interaction of calmodulin with the cytoplasmic domain of platelet glycoprotein VI.

نویسندگان

  • Robert K Andrews
  • Katsue Suzuki-Inoue
  • Yang Shen
  • David Tulasne
  • Stephen P Watson
  • Michael C Berndt
چکیده

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 GPIbbeta 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 GPIbbeta. The novel interaction of GPVI and calmodulin may regulate aspects of GPVI function.

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Brief report Interaction of calmodulin with the cytoplasmic domain of platelet glycoprotein VI

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 GPIbIX-V bind calmodulin. We now show that GPVI also binds calmodulin as follows—(1) calmodulincoi...

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عنوان ژورنال:
  • Blood

دوره 99 11  شماره 

صفحات  -

تاریخ انتشار 2002