Cell and Tissue Research

, Volume 355, Issue 3, pp 607–619

PECAM-1: regulator of endothelial junctional integrity


DOI: 10.1007/s00441-013-1779-3

Cite this article as:
Privratsky, J.R. & Newman, P.J. Cell Tissue Res (2014) 355: 607. doi:10.1007/s00441-013-1779-3


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.


PECAM-1 CD31 Vascular permeability Adhesion molecules 

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Blood Research InstituteBloodCenter of WisconsinMilwaukeeUSA
  2. 2.Department of PharmacologyMedical College of WisconsinMilwaukeeUSA
  3. 3.Department of Cellular Biology and AnatomyMedical College of WisconsinMilwaukeeUSA
  4. 4.The Cardiovascular Research CenterMedical College of WisconsinMilwaukeeUSA

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