Linked Life Data

9845526

Source:http://linkedlifedata.com/resource/pubmed/id/9845526

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1999-2-5
pubmed:abstractText
We have recently described Poliovirus Receptor Related 2 (PRR2), a new cell surface molecule homologous to the poliovirus receptor (PVR/CD155). Both molecules are transmembrane glycoproteins belonging to the Ig superfamily (IgSF). They contain 3 Ig domains of V, C2, and C2 types in their extracellular regions that share 51% aa identity. The PRR2 gene encodes two mRNA isoforms of 3.0 kb (hPRR2 [short form]) and 4.4 kb (hPRR2delta [long form]), both widely expressed in human tissues, including hematopoietic cells. To further characterize PRR2 expression during hematopoiesis and to analyze its function, we have developed a monoclonal antibody (MoAb) directed against its extracellular region (R2.477). PRR2 was expressed in 96% of the CD34(+), 88% of the CD33(+), and 95% of the CD14(+) hematopoietic lineages and faintly in the CD41 compartment. Ectopic expression of both PRR2 cDNAs induced marked cell aggregation. A soluble chimeric receptor construct with the Fc fragment of human IgG1 (PRR2-Fc) as well as a fab fragment of the anti-PRR2 MoAb (R2.477) inhibit aggregation. PRR2-Fc binds specifically to PRR2-expressing cells. These results suggest that PRR2 is a homophilic adhesion receptor. PRR2 was also expressed at the surface of endothelial cells at the intercellular junctions of adjacent cells but not at the free cellular edges. Homophilic interactions are associated with dimerization of isoforms of PRR2 and lead to the tyrosine phosphorylation of PRR2delta. Altogether, these results suggest that homophilic properties of PRR2 could participate to the regulation of hematopoietic/endothelial cell functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4602-11
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9845526-Animals, pubmed-meshheading:9845526-Bone Marrow Cells, pubmed-meshheading:9845526-Cell Adhesion, pubmed-meshheading:9845526-Cell Adhesion Molecules, pubmed-meshheading:9845526-Cells, Cultured, pubmed-meshheading:9845526-Cricetinae, pubmed-meshheading:9845526-Dimerization, pubmed-meshheading:9845526-Endothelium, Vascular, pubmed-meshheading:9845526-Flow Cytometry, pubmed-meshheading:9845526-Hematopoietic Stem Cells, pubmed-meshheading:9845526-Humans, pubmed-meshheading:9845526-Immunohistochemistry, pubmed-meshheading:9845526-Membrane Glycoproteins, pubmed-meshheading:9845526-Mice, pubmed-meshheading:9845526-Phosphorylation, pubmed-meshheading:9845526-Protein Isoforms, pubmed-meshheading:9845526-Receptors, Cell Surface, pubmed-meshheading:9845526-Receptors, Tumor Necrosis Factor, pubmed-meshheading:9845526-Receptors, Tumor Necrosis Factor, Member 14, pubmed-meshheading:9845526-Receptors, Virus
pubmed:year
1998
pubmed:articleTitle
The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule.
pubmed:affiliation
INSERM U.119, Unité de Cancérologie et Thérapeutique Expérimentales, Marseille, France. lopez@marseille.inserm.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't