Linked Life Data

11171323

Source:http://linkedlifedata.com/resource/pubmed/id/11171323

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
2001-2-22
pubmed:abstractText
We have previously reported the purification and characterization of a 32 kDa platelet surface glycoprotein that is recognized by the stimulatory monoclonal antibody, F11. The cDNA has been cloned and found to encode the human homolog of the murine junctional adhesion molecule, JAM; we therefore named this human homolog JAM-1. Northern blot analysis indicated that JAM-1 mRNA is expressed as multiple species, the predominant transcript being approximately 4.0 kb in size. Genetic mapping analysis using fluorescence in situ hybridization (FISH) showed that it is localized to chromosome 1q21.1-21.3. Recombinant JAM-1, when expressed in Chinese hamster ovary (CHO) cells, localized to the cell membrane with intense staining where two adjacent cells actually made contact with each other, suggesting that, similar to murine JAM, human JAM-1 may also localize at the cell-cell junction. In well-spread cells, JAM-1 co-localized with F-actin at the cell-cell contacts and at the membrane ruffles, but not at the stress fibers. Interestingly, JAM-1 localizes only to the cell-cell junctions formed by two transfected cells and not to the cell-cell junctions formed by a transfected cell with an untransfected cell, suggesting that JAM-1 may facilitate cell adhesion through homophilic binding. In addition, human platelets specifically bind to a monolayer of CHO cells expressing human JAM-1, further supporting homophilic interactions. The results presented here indicate that JAM-1, a receptor for a platelet-activating antibody, is the human homolog of the junctional adhesion molecule. JAM-1 is a single copy gene, which is constitutively expressed on various tissues and cells, and may be involved in cell to cell adhesion through homophilic interaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
539-47
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11171323-Amino Acid Sequence, pubmed-meshheading:11171323-Animals, pubmed-meshheading:11171323-Base Sequence, pubmed-meshheading:11171323-Blood Platelets, pubmed-meshheading:11171323-CHO Cells, pubmed-meshheading:11171323-Cell Adhesion, pubmed-meshheading:11171323-Cell Adhesion Molecules, pubmed-meshheading:11171323-Chromosome Mapping, pubmed-meshheading:11171323-Chromosomes, Human, Pair 1, pubmed-meshheading:11171323-Cricetinae, pubmed-meshheading:11171323-DNA, Complementary, pubmed-meshheading:11171323-Humans, pubmed-meshheading:11171323-Membrane Proteins, pubmed-meshheading:11171323-Molecular Sequence Data, pubmed-meshheading:11171323-RNA, Messenger, pubmed-meshheading:11171323-Receptors, Cell Surface, pubmed-meshheading:11171323-Receptors, Virus, pubmed-meshheading:11171323-Recombinant Proteins, pubmed-meshheading:11171323-Sequence Homology, Amino Acid, pubmed-meshheading:11171323-Subcellular Fractions, pubmed-meshheading:11171323-Tumor Cells, Cultured
pubmed:year
2001
pubmed:articleTitle
Characterization and chromosomal localization of JAM-1, a platelet receptor for a stimulatory monoclonal antibody.
pubmed:affiliation
Department of Biological Sciences, University of Delaware, Newark, DE 19716, USA. unaik@udel.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't