Macrophage–tumour cell interactions: identification of MUC1 on breast cancer cells as a potential counter-receptor for the macrophage-restricted receptor, sialoadhesin

Authors

  • Nath,

    1. *ICRF Laboratories, University of Oxford, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK, and ICRF Breast Cancer Biology Group, Guy’s Hospital, London, UK
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  • Hartnell*,

    1. *ICRF Laboratories, University of Oxford, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK, and ICRF Breast Cancer Biology Group, Guy’s Hospital, London, UK
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  • Happerfield,

    1. *ICRF Laboratories, University of Oxford, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK, and ICRF Breast Cancer Biology Group, Guy’s Hospital, London, UK
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  • Miles,

    1. *ICRF Laboratories, University of Oxford, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK, and ICRF Breast Cancer Biology Group, Guy’s Hospital, London, UK
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  • Burchell,

    1. *ICRF Laboratories, University of Oxford, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK, and ICRF Breast Cancer Biology Group, Guy’s Hospital, London, UK
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  • Taylor-Papadimitriou,

    1. *ICRF Laboratories, University of Oxford, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK, and ICRF Breast Cancer Biology Group, Guy’s Hospital, London, UK
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  • Crocker*§

    1. *ICRF Laboratories, University of Oxford, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK, and ICRF Breast Cancer Biology Group, Guy’s Hospital, London, UK
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Dr Crocker Department of Biochemistry MSI/WTB Complex, University of Dundee, Dow Street, Dundee, DD1 5EH, UK.

Abstract

In many carcinomas, infiltrating macrophages are commonly found closely associated with tumour cells but little is known concerning the nature or significance of adhesion molecules involved in these cellular interactions. Here we demonstrate in primary human breast cancers that sialoadhesin (Sn), a macrophage-restricted adhesion molecule, is frequently expressed on infiltrating cells that often make close contact with breast carcinoma cells. To determine whether Sn could act as a specific receptor for ligands on breast cancer cell lines, binding assays were performed with a recombinant form of the protein fused to the Fc portion of human immunoglobulin G1 (IgG1) (Sn-Fc). Sn-Fc was found to bind specifically and in a sialic acid-dependent manner to the breast cancer cell lines MCF-7, T47.D and BT-20 both in solid- and solution-phase binding assays. To investigate the nature of the sialoglycoproteins recognized by Sn on breast cancer cells, MCF-7 cells were labelled with [6-3H]glucosamine. Following precipitation with Sn-Fc, a major band of ≈240 000 MW was revealed, which was shown in reprecipitation and Western blotting experiments to be the epithelial mucin, MUC1.

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