[HTML][HTML] Regulation of glycoprotein Ib-IX-von Willebrand factor interaction by cAMP-dependent protein kinase-mediated phosphorylation at Ser 166 of glycoprotein Ibβ
The platelet receptor for von Willebrand factor (VWF), glycoprotein (GP) Ib-IX, mediates
initial platelet adhesion and activation. It is known that the cytoplasmic domain of GPIbβ is
phosphorylated at Ser 166 by cAMP-dependent protein kinase (PKA). To understand the
physiological role of GPIbβ phosphorylation, a GPIb-IX mutant replacing Ser 166 of GPIbβ
with alanine (S166A) and a deletion mutant lacking residues 166–181 of GPIbβ (Δ165) were
constructed. These mutants, expressed in Chinese hamster ovary (CHO) cells, showed an …
initial platelet adhesion and activation. It is known that the cytoplasmic domain of GPIbβ is
phosphorylated at Ser 166 by cAMP-dependent protein kinase (PKA). To understand the
physiological role of GPIbβ phosphorylation, a GPIb-IX mutant replacing Ser 166 of GPIbβ
with alanine (S166A) and a deletion mutant lacking residues 166–181 of GPIbβ (Δ165) were
constructed. These mutants, expressed in Chinese hamster ovary (CHO) cells, showed an …