Literature DB >> 2009910

The MRC OX-47 antigen is a member of the immunoglobulin superfamily with an unusual transmembrane sequence.

S Fossum1, S Mallett, A N Barclay.   

Abstract

The MRC OX-47 monoclonal antibody recognizes a membrane antigen present at low levels on many lymphocytes but whose expression is markedly increased on activation with mitogens. cDNA clones for the OX-47 antigen were isolated from an expression library and the protein sequence deduced. It contains a leader sequence giving a mature protein of 251 amino acids with a single putative transmembrane region, a cytoplasmic domain of 40 amino acids and an extracellular domain of 187 amino acids that contained two immunoglobulin-like domains. The putative transmembrane sequence includes a glutamic acid residue within the hydrophobic sequence. The presence of acidic residues within the hydrophobic sequence of transmembrane sequences usually indicates association with other polypeptides and this is predicted for the OX-47 antigen. A sequence of 37 amino acids that included all the transmembrane region was identical to that of the chicken HT7 antigen present on endothelium in brain and erythroblasts. The level of protein sequence identity in the Ig-like domains was lower but HT7 is almost certainly the chicken homologue of the rat OX-47 antigen. The ligand and function of the molecule are unknown. In addition to lymphoblasts the OX-47 antigen was localized on a variety of other cell types including various immature cells, endothelia and cells with excitable membranes.

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Year:  1991        PMID: 2009910     DOI: 10.1002/eji.1830210320

Source DB:  PubMed          Journal:  Eur J Immunol        ISSN: 0014-2980            Impact factor:   5.532


  46 in total

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Authors:  C Juel; A P Halestrap
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9.  Membrane-anchored carbonic anhydrase IV interacts with monocarboxylate transporters via their chaperones CD147 and GP70.

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10.  The interaction of HAb18G/CD147 with integrin alpha6beta1 and its implications for the invasion potential of human hepatoma cells.

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