PECAM-1: regulator of endothelial junctional integrity. Cell Tissue Res 2014 Mar;355(3):607-19
Date
01/18/2014Pubmed ID
24435645Pubmed Central ID
PMC3975704DOI
10.1007/s00441-013-1779-3Scopus ID
2-s2.0-84899440750 (requires institutional sign-in at Scopus site) 234 CitationsAbstract
PECAM-1 (also known as CD31) is a cellular adhesion and signaling receptor comprising six extracellular immunoglobulin (Ig)-like homology domains, a short transmembrane domain and a 118 amino acid cytoplasmic domain that becomes serine and tyrosine phosphorylated upon cellular activation. PECAM-1 expression is restricted to blood and vascular cells. In circulating platelets and leukocytes, PECAM-1 functions largely as an inhibitory receptor that, via regulated sequential phosphorylation of its cytoplasmic domain, limits cellular activation responses. PECAM-1 is also highly expressed at endothelial cell intercellular junctions, where it functions as a mechanosensor, as a regulator of leukocyte trafficking and in the maintenance of endothelial cell junctional integrity. In this review, we will describe (1) the functional domains of PECAM-1 and how they contribute to its barrier-enhancing properties, (2) how the physical properties of PECAM-1 influence its subcellular localization and its ability to influence endothelial cell barrier function, (3) various stimuli that initiate PECAM-1 signaling and/or function at the endothelial junction and (4) cross-talk of PECAM-1 with other junctional molecules, which can influence endothelial cell function.
Author List
Privratsky JR, Newman PJAuthor
Peter J. Newman PhD Professor in the Pharmacology and Toxicology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsCell Adhesion
Endothelial Cells
Humans
Intercellular Junctions
Platelet Endothelial Cell Adhesion Molecule-1
