Platelet moesin interacts with PECAM-1 (CD31). Platelets 2003 Jun;14(4):211-7
Date
07/10/2003Pubmed ID
12850829DOI
10.1080/0953710031000118830Scopus ID
2-s2.0-0037711542 (requires institutional sign-in at Scopus site) 19 CitationsAbstract
Platelet activation results information 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.
Author List
Gamulescu MA, Seifert K, Tingart M, Falet H, Hoffmeister KMAuthors
Herve Falet PhD Associate Professor in the Cell Biology, Neurobiology and Anatomy department at Medical College of WisconsinKarin Hoffmeister MD Professor in the Biochemistry department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
ActinsBlood Platelets
Cytoskeleton
Humans
Microfilament Proteins
Platelet Endothelial Cell Adhesion Molecule-1
Precipitin Tests
Protein Binding
Pseudopodia
Thrombin