title: Modified C-reactive protein interacts with platelet glycoprotein Ibα.
abstract: Herein, we investigated the possible mechanisms by which recombinant modified CRP(m(r)CRP) modulates blood platelet function. Modified CRP could activate blood platelets and stimulate their adhesion and aggregation in the absence of any other physiological stimuli. Preincubation of isolated blood platelets with m(r)CRP at a concentration as low as 2 μg/ml resulted in significant platelet degranulation (fraction of CD62-positive platelets increased 2-fold, p < 0.0002), and at concentrations of 20 μg/ml and 100 μg/ml, increased exposure of the platelet procoagulant surface was observed (expression of annexin V-positive platelets increased to 5.7 ± 1.0% and 10.4 ± 2.2%, respectively, p < 0.03, vs. 2.9 ± 0.2% in control). Furthermore, m(r)CRP (100 μg/ml) strongly augmented spontaneous and ADP-induced fibrinogen binding to platelets (p < 0.05), platelet adhesion to fibrinogen and platelet aggregation. Using the Biacore™ surface plasmon resonance technique and glycoprotein Ibα (GPIbα) immobilized on the sensor surface, we demonstrated direct binding between platelet GPIbα and m(r)CRP. Binding of m(r)CRP to GPIbα and C1q was also observed by ELISA, irrespective of the immobilized ligand. These outcomes strongly support a role of the GPIb-IX-V complex in the interactions of m(r)CRP with blood platelets.
authors: Department of Haemostasis and Haemostatic Disorders, Medical University of Lodz, Żeromskiego 113, PL 90-549 Łódź, Poland. mboncler@csk.umed.lodz.pl
authors: Magdalena
authors: M
authors: Boncler
authors: Joanna
authors: J
authors: Rywaniak
authors: Jacek
authors: J
authors: Szymański
authors: Lawrence A
authors: LA
authors: Potempa
authors: Błażej
authors: B
authors: Rychlik
authors: Cezary
authors: C
authors: Watała