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Characterization of the human homolog of the rat MRC OX-2 membrane glycoprotein

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Abstract

The MRC OX-2 antigen is a membrane glycoprotein present on rat thymocytes, neurons, follicular dendritic cells, endothelium, and some smooth muscle. The sequence of 248 amino acids has similarities to Ig domains organized with one V-like domain, one C-like domain, and transmembrane and cytoplasmic regions. Thus it resembles a T-cell receptor chain but shows no sequence divergence. We report the characterization of the human gene for this molecule. Its exon organization is similar to that found for immunoglobulins although the region with similarities to Ig J regions is found within the same exon as the V-like domain. Human MRC OX-2 is expressed at the mRNA level in brain and B-cell lines but not detected in liver or T-cell lines. It does not obviously correspond to any previously defined leukocyte antigen. The sequence homology for the human and rat MRC OX-2 molecules is higher for the Ig-related region (75 %) than for many other Ig-related molecules and very high in the transmembrane region (96 %), implying a functional role other than simply its anchoring into the membrane.

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Author notes

  1. Geoff W. McCaughan

    Present address: A. W. Morrow Gastroenterology and Liver Centre, Royal Prince Alfred Hospital, Missenden Road, Camperdown, Syndney, Australia

  2. Melanie J. Clark

    Present address: MRC Laboratory of Molecular Biology, University Postgraduate Medical School, Hills Road, CB2 2QH, Cambridge, UK

Authors and Affiliations

  1. MRC Cellular Immunology Research Unit Sir William Dunn School of Pathology, University of Oxford, South Parks Road, OX1 3RE, Oxford, UK

    Geoff W. McCaughan, Melanie J. Clark & A. Neil Barclay

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  1. Geoff W. McCaughan
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  2. Melanie J. Clark
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  3. A. Neil Barclay
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McCaughan, G.W., Clark, M.J. & Neil Barclay, A. Characterization of the human homolog of the rat MRC OX-2 membrane glycoprotein. Immunogenetics 25, 329–335 (1987). https://doi.org/10.1007/BF00404426

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  • DOI: https://doi.org/10.1007/BF00404426

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