Signal transduction pathways mediated by PECAM-1: new roles for an old molecule in platelet and vascular cell biology. Arterioscler Thromb Vasc Biol 2003 Jun 01;23(6):953-64
Date
04/12/2003Pubmed ID
12689916DOI
10.1161/01.ATV.0000071347.69358.D9Scopus ID
2-s2.0-0038120892 (requires institutional sign-in at Scopus site) 350 CitationsAbstract
Recent studies of platelet endothelial cell adhesion molecule-1 (PECAM-1 [CD31])-deficient mice have revealed that this molecule plays an important role in controlling the activation and survival of cells on which it is expressed. In this review, we focus on the complex cytoplasmic domain of PECAM-1 and describe what is presently known about its structure, posttranslational modifications, and binding partners. In addition, we summarize findings that implicate PECAM-1 as an inhibitor of cellular activation via protein tyrosine kinase-dependent signaling pathways, an activator of integrins, and a suppressor of cell death via pathways that depend on damage to the mitochondria. The challenge of future research will be to bridge our understanding of the functional and biochemical properties of PECAM-1 by establishing mechanistic links between signals transduced by the PECAM-1 cytoplasmic domain and discrete cellular responses.
Author List
Newman PJ, Newman DKAuthors
Debra K. Newman PhD Investigator in the Blood Research Institute department at BloodCenter of WisconsinDebra K. Newman PhD Professor in the Pharmacology and Toxicology department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Apoptosis
Endothelium, Vascular
Humans
Integrins
Mice
Mice, Knockout
Models, Molecular
Molecular Sequence Data
Phosphorylation
Platelet Activation
Platelet Endothelial Cell Adhesion Molecule-1
Protein Processing, Post-Translational
Protein Structure, Tertiary
Signal Transduction
Structure-Activity Relationship
