The novel inhibitory receptor G6B is expressed on the surface of platelets and attenuates platelet function in vitro

The G6B cell-surface receptor, which contains a single Ig-like domain, has been shown to bind to SHP-1 and SHP-2 after phosphorylation of 2 immunoreceptor tyrosine-based inhibitory motifs (ITIMs) in its cytoplasmic tail, classifying this protein as a new member of the family of inhibitory receptors....

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Bibliographic Details
Published in:Blood 2007-06, Vol.109 (11), p.4806-4809
Main Authors: Newland, Stephen A., Macaulay, Iain C., Floto, Andres R., de Vet, Edwin C., Ouwehand, Willem H., Watkins, Nicholas A., Lyons, Paul A., Campbell, Duncan R.
Format: Article
Language:English
Subjects:
Adenosine Diphosphate - chemistry
Biological and medical sciences
Blood Platelets - metabolism
Blotting, Western
Carrier Proteins - chemistry
Cell Membrane - metabolism
Cross-Linking Reagents - pharmacology
Cytoplasm - metabolism
Gene Expression Regulation
Hematologic and hematopoietic diseases
Humans
Medical sciences
Membrane Proteins - metabolism
Peptides - chemistry
Phosphorylation
Protein Isoforms
Protein Structure, Tertiary
Receptors, Immunologic - biosynthesis
Receptors, Immunologic - physiology
Reverse Transcriptase Polymerase Chain Reaction
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Summary:The G6B cell-surface receptor, which contains a single Ig-like domain, has been shown to bind to SHP-1 and SHP-2 after phosphorylation of 2 immunoreceptor tyrosine-based inhibitory motifs (ITIMs) in its cytoplasmic tail, classifying this protein as a new member of the family of inhibitory receptors. In this study, we demonstrate by real-time polymerase chain reaction (PCR) and Western-blot analysis that G6B is expressed on platelets. Cross-linking of G6B with polyclonal antisera has a significant inhibitory effect on platelet aggregation and activation by agonists such as ADP and collagen-related peptide (CRP). This inhibitory function of G6B appears to operate in a calcium-independent manner. Our results suggest that G6B represents a novel inhibitory receptor found on the surface of platelets and that it could be an antithrombotic drug target.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood-2006-09-047449