Platelet moesin interacts with PECAM-1 (CD31)

Author: Gamulescu Maria-Andreea   Seifert Kerstin   Tingart Markus   Falet Hervé   Hoffmeister Karin M.  

Publisher: Informa Healthcare

ISSN: 1369-1635

Source: Platelets, Vol.14, Iss.4, 2003-06, pp. : 211-217

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Platelet activation results in formation of filopodia and cell spreading by extension of lamellae. Moesin is a member of the ezrin/radixin/moesin (ERM) family of proteins, which localize in cell extensions like filopodia and function as cross-linkers between the actin cytoskeleton and the plasma membrane. Here we investigated whether the adhesion molecule PECAM-1 (CD31) is a membrane-binding partner for moesin in platelets. Our data show that moesin co-immunoprecipitated with PECAM-1 in lysates from thrombin-stimulated, but not resting platelets. Furthermore, PECAM-1 co-localized with moesin at the cell periphery and in filopodia of glass-activated platelets. Our observations suggest that moesin may play a role in platelet adhesion, linking PECAM-1 with the actin cytoskeleton.

Related content