ArticleThe Journal of cell biology1992
Activation-dependent changes in human platelet PECAM-1: phosphorylation, cytoskeletal association, and surface membrane redistribution.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 137 citations in OpenAlex.
- Thymic function as a central determinant of immune competence and clinical outcomes.Seminars in immunopathology · 2026Review
- Increased Cell Adhesion Molecules, PECAM-1, ICAM-3, or VCAM-1, Predict Increased Risk for Flare in Patients With Quiescent Inflammatory Bowel Disease.Journal of clinical gastroenterology · 2017Article
- S-adenosylhomocysteine induces inflammation through NFkB: A possible role for EZH2 in endothelial cell activation.Biochimica et biophysica acta · 2016Article
- PECAM-1 isoforms, eNOS and endoglin axis in regulation of angiogenesis.Clinical science (London, England : 1979) · 2015Review
- PECAM-1: regulator of endothelial junctional integrity.Cell and tissue research · 2014Review
- Article
- Human peripheral blood-derived CD31+ cells have robust angiogenic and vasculogenic properties and are effective for treating ischemic vascular disease.Journal of the American College of Cardiology · 2010Article
- Basal and angiopoietin-1-mediated endothelial permeability is regulated by sphingosine kinase-1.Blood · 2008Article
- Article
- PECAM-1 affects GSK-3beta-mediated beta-catenin phosphorylation and degradation.The American journal of pathology · 2006Article
- Platelet endothelial cell adhesion molecule in cell signaling and thrombosis.Molecular and cellular biochemistry · 2003Review
- Altered vascular permeability and early onset of experimental autoimmune encephalomyelitis in PECAM-1-deficient mice.The Journal of clinical investigation · 2002Article
- Novel cytokine-independent induction of endothelial adhesion molecules regulated by platelet/endothelial cell adhesion molecule (CD31).The Journal of cell biology · 1997Article
- Tyrosine residue in exon 14 of the cytoplasmic domain of platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) regulates ligand binding specificity.The Journal of cell biology · 1997Article
- Thrombospondin-1, a natural inhibitor of angiogenesis, regulates platelet-endothelial cell adhesion molecule-1 expression and endothelial cell morphogenesis.Molecular biology of the cell · 1997Article
- Platelet-endothelial cell adhesion molecule-1 (PECAM-1/CD31) tyrosine phosphorylation state changes during vasculogenesis in the murine conceptus.The American journal of pathology · 1997Article
- Immunohistochemical studies of vascular volume and proliferative activity in squamous cell carcinoma of the esophagus.Surgery today · 1997Article
- Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Modulation by high glucose of adhesion molecule expression in cultured endothelial cells.Diabetologia · 1995Article
- Mapping the homotypic binding sites in CD31 and the role of CD31 adhesion in the formation of interendothelial cell contacts.The Journal of cell biology · 1995Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
PECAM-1 is a recently described member of the immunoglobulin gene (Ig) superfamily that is expressed on the surface on platelets, several leukocyte subsets, and at the endothelial cell intracellular junction. Recent studies have shown that the extracellular domain of PECAM-1, which is comprised of 6 Ig-like homology units, participates in mediating cell-cell adhesion, plays a role in initiating endothelial cell contact, and may later serve to stabilize the endothelial cell monolayer. PECAM-1 also has a relatively large 108 amino acid cytoplasmic domain, with potential sites for phosphorylation, lipid modification, and other posttranslational events that could potentially modulate its adhesive function or regulate its subcellular distribution. Virtually nothing is known about the contribution of the intracellular region of the PECAM-1 molecule to either of these cellular processes. Using human platelets as a model, we now demonstrate that PECAM-1 becomes highly phosphorylated in response to cellular activation, and coincident with phosphorylation associates with the cytoskeleton of activated, but not resting, platelets. The engagement of PECAM-1 with the platelet cytoskeleton enables it to move large distances within the plane of the membrane of fully-spread, adherent platelets. This redistribution may similarly account for the ability of PECAM-1 to localize to the intracellular borders of endothelial cells once cell-cell contact has been achieved.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.