The unfolding tale of PECAM‐1

@article{Jackson2003TheUT,
  title={The unfolding tale of PECAM‐1},
  author={Denise E. Jackson},
  journal={FEBS Letters},
  year={2003},
  volume={540}
}
  • D. E. Jackson
  • Published 10 April 2003
  • Biology, Medicine
  • FEBS Letters
Platelet endothelial cell adhesion molecule‐1 (PECAM‐1/CD31) is a member of the immunoglobulin (Ig) superfamily that has distinctive features of an immunoreceptor based upon its genomic structure and the presence of intrinsic immunoreceptor tyrosine inhibitory motifs (ITIMs) in its ligand binding polypeptide. This has lead to its subclassification into the Ig‐ITIM superfamily. Its amino‐terminal Ig‐like domain of PECAM‐1 is necessary for its homophilic binding, which plays an important role in… Expand
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TLDR
Engagement of PECAM-1 causes up-regulation of integrin function on leukocytes, implicating PECam-1 as a trigger molecule that may regulate leukocyte trafficking through the vessel wall. Expand
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TLDR
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TLDR
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TLDR
PECAM-1, like certain integrins, appears to be capable of antibody-induced conformational changes that alter affinity for its ligand, and similar changes induced by physiologic stimuli could be important in regulating the function of PECam-1 in vascular cells. Expand
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TLDR
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TLDR
It is suggested that a dynamic equilibrium between PECAM-1 monomers, dimers, and oligomers may control cellular activation signals that influence the adhesive properties of vascular cells that express this novel member of the immunoreceptor tyrosine–based inhibitory motif family of regulatory receptors. Expand
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TLDR
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TLDR
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Platelet Endothelial Cell Adhesion Molecule-1 (PECAM-1) Homophilic Adhesion Is Mediated by Immunoglobulin-like Domains 1 and 2 and Depends on the Cytoplasmic Domain and the Level of Surface Expression*
TLDR
Analysis of the binding interactions of L-cells expressing full-length and selectively mutated forms of human, murine, and human/murine chimeric PECAM-1 molecules in an established aggregation assay suggests that PECam-1-ligand interactions can be regulated through multiple pathways including alterations of the cytoplasmic domain and the level of surface expression. Expand
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