Linked Life Data

8765026

Source:http://linkedlifedata.com/resource/pubmed/id/8765026

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1996-10-24
pubmed:databankReference
pubmed:abstractText
Human natural killer (NK) cells express inhibitory (p58) or activatory (p50) receptors for HLA-C alleles. Here, we describe a novel member of the p58/p50 family that is expressed by a subset of NK cells in about one third of donors. This molecule, termed p50.3, mediates NK cell triggering as revealed by the induction of intracellular free calcium mobilization, cytokine release and cytotoxicity. In addition, anti-p50.3 monoclonal antibody (mAb) induced a selective, strong proliferation of p50.3+ NK cells in peripheral blood lymphocytes. Although p50.3 molecules do not appear to display an obvious HLA class I specificity, they are usually coexpressed with known inhibitory receptors for HLA class I alleles, mAb-mediated cross-linking of these receptors leads to inhibition of the anti-p50.3 mAb-induced NK cell activation and proliferation. Surface p50.3 molecules are glycoproteins of approximately 55-58 kDa which, upon deglycosylation, display a relative molecular mass of 36 kDa, similar to that of deglycosylated (activatory) p50 receptors. Analysis of the two-dimensional peptide maps of the 50.3 molecules revealed a high homology with the other HLA-C-specific p58/p50 receptors. The use of a set of oligodeoxynucleotide primers, previously shown to amplify the activatory (p50) forms of HLA-C-specific receptors, consistently amplified in p50.3+ clones a cDNA sequence termed KKA3. This sequence belongs to the p58/p50 multigene family, that encodes for a transmembrane protein specifically stained by anti-p50.3 mAb in cell transfectants. Similar to p50 molecules, the KKA3-encoded molecules are characterized by two extracellular immunoglobulin-like domains, by the presence of a lysine in the transmembrane region and a short (39 amino acids) cytoplasmic tail which does not contain immune receptor tyrosine-based activation motifs (ITAM)-like sequences.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1816-24
pubmed:dateRevised
2008-3-6
pubmed:meshHeading
pubmed-meshheading:8765026-Amino Acid Sequence, pubmed-meshheading:8765026-Animals, pubmed-meshheading:8765026-Antibodies, Monoclonal, pubmed-meshheading:8765026-Base Sequence, pubmed-meshheading:8765026-Cloning, Molecular, pubmed-meshheading:8765026-Cytotoxicity, Immunologic, pubmed-meshheading:8765026-Epitopes, pubmed-meshheading:8765026-Humans, pubmed-meshheading:8765026-Killer Cells, Natural, pubmed-meshheading:8765026-Lymphocyte Activation, pubmed-meshheading:8765026-Male, pubmed-meshheading:8765026-Mice, pubmed-meshheading:8765026-Mice, Inbred BALB C, pubmed-meshheading:8765026-Molecular Sequence Data, pubmed-meshheading:8765026-Receptors, Immunologic, pubmed-meshheading:8765026-Receptors, KIR, pubmed-meshheading:8765026-Receptors, KIR2DL3, pubmed-meshheading:8765026-Sequence Homology, Amino Acid, pubmed-meshheading:8765026-Transcription, Genetic
pubmed:year
1996
pubmed:articleTitle
A novel surface molecule homologous to the p58/p50 family of receptors is selectively expressed on a subset of human natural killer cells and induces both triggering of cell functions and proliferation.
pubmed:affiliation
Istituto Scientifico Tumori, Genova, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't