CEACAM2 positively regulates integrin αIIbβ3-mediated platelet functions. (16th November 2016)

• Record Type: Journal Article
• Authors: Alshahrani, Musaed M.; Kyriacou, Roula P.; O'Malley, Cindy J.; Heinrich, Garrett; Najjar, Sonia M.; Jackson, Denise E.
• Is Part Of: Platelets. Volume 27:Number 8(2016)
• Page Start: 743
• Page End: 750
• Publication Date: 2016-11-16
• Subjects: Blood platelets -- Periodicals; Blood Platelets -- Periodicals; 615.39
• DOI: 10.3109/09537104.2016.1171834
• Languages: English
• ISSNs: 0953-7104

Abstract

Abstract: Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) is an Ig-ITIM superfamily member that regulates integrin αIIbβ3 function. We hypothesized that its twin protein, CEACAM2, exerts a similar physiologic role in murine platelets. CEACAM2-deficient mice ( Cc2 −/− ) displayed prolonged tail bleeding times and increased volume of blood loss. Cc2 − / − platelets have moderate integrin αIIbβ3-mediated functional defects with impaired kinetics of platelet spreading on fibrinogen and type I collagen and delayed kinetics in the retraction of fibrin clots in vitro . This functional integrin αIIbβ3 defect could not be attributed to altered integrin αIIbβ3 expression. Cc2 − / − platelets displayed normal 'inside-out' signaling properties as demonstrated by normal agonist-induced binding of soluble fluorescein isothiocyanate (FITC)-fibrinogen and JON/A antibody binding. This data provides direct evidence that disruption of CEACAM2 induces a moderate integrin αIIbβ3-mediated platelet function defect, and that CEACAM2 is essential to maintain a normal integrin αIIbβ3-mediated platelet function.