Carbohydrate-independent recognition of collagens by the macrophage mannose receptor. European Journal of Immunology.

L. Martinez-Pomares, D. Wienke, R. Stillion, Emma Jane McKenzie, J. N. Arnold, J. Harris, E. McGreal, R. B. Sim, C. M. Isacke, S. Gordon

    Research output: Contribution to journalArticle

    81 Citations (Scopus)

    Abstract

    Mannose receptor (MR) is the best characterised member of a family of four endocytic molecules that share a common domain structure; a cysteine-rich (CR) domain, a fibronectin-type II (FNII) domain and tandemly arranged C-type lectin-like domains (CTLD, eight in the case of MR). Two distinct lectin activities have been described for MR. The CR domain recognises sulphated carbohydrates while the CTLD mediate binding to mannose, fucose or N-acetylglucosamine. FNII domains are known to be important for collagen binding and this has been studied in the context of two members of the MR family, Endo180 and the phospholipase A(2) receptor. Here, we have investigated whether the broad and effective lectin activity mediated by the CR domain and CTLD of MR is favoured to the detriment of FNII-mediated interaction(s). We show that MR is able to bind and internalise collagen in a carbohydrate-independent manner and that MR deficient macrophages have a marked defect in collagen IV and gelatin internalisation. These data have major implications at the molecular level as there are now three distinct ligand-binding sites described for MR. Furthermore our findings extend the range of endogenous ligands recognised by MR, a molecule firmly placed at. the interface between homeostasis and immunity.

    Original languageEnglish
    Pages (from-to)1074-1082
    Number of pages9
    JournalEuropean Journal of Immunology
    Volume36
    Issue number5
    DOIs
    Publication statusPublished - 2006

    Keywords

    • CD206/208
    • Endo180
    • extracellular matrix
    • macrophages
    • mannose receptor
    • CYSTEINE-RICH DOMAIN
    • MURINE MACROPHAGES
    • ENDOTHELIAL-CELLS
    • INTERFERON-GAMMA
    • BINDING
    • ACTIVATION
    • PROTEIN
    • MICE
    • AUTOANTIGENS
    • HOMEOSTASIS

    Cite this

    Martinez-Pomares, L., Wienke, D., Stillion, R., McKenzie, E. J., Arnold, J. N., Harris, J., ... Gordon, S. (2006). Carbohydrate-independent recognition of collagens by the macrophage mannose receptor. European Journal of Immunology. European Journal of Immunology, 36(5), 1074-1082. https://doi.org/10.1002/eji.200535685

    Carbohydrate-independent recognition of collagens by the macrophage mannose receptor. European Journal of Immunology. / Martinez-Pomares, L.; Wienke, D.; Stillion, R.; McKenzie, Emma Jane; Arnold, J. N.; Harris, J.; McGreal, E.; Sim, R. B.; Isacke, C. M.; Gordon, S.

    In: European Journal of Immunology, Vol. 36, No. 5, 2006, p. 1074-1082.

    Research output: Contribution to journalArticle

    Martinez-Pomares, L, Wienke, D, Stillion, R, McKenzie, EJ, Arnold, JN, Harris, J, McGreal, E, Sim, RB, Isacke, CM & Gordon, S 2006, 'Carbohydrate-independent recognition of collagens by the macrophage mannose receptor. European Journal of Immunology.', European Journal of Immunology, vol. 36, no. 5, pp. 1074-1082. https://doi.org/10.1002/eji.200535685
    Martinez-Pomares, L. ; Wienke, D. ; Stillion, R. ; McKenzie, Emma Jane ; Arnold, J. N. ; Harris, J. ; McGreal, E. ; Sim, R. B. ; Isacke, C. M. ; Gordon, S. / Carbohydrate-independent recognition of collagens by the macrophage mannose receptor. European Journal of Immunology. In: European Journal of Immunology. 2006 ; Vol. 36, No. 5. pp. 1074-1082.
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    AU - Martinez-Pomares, L.

    AU - Wienke, D.

    AU - Stillion, R.

    AU - McKenzie, Emma Jane

    AU - Arnold, J. N.

    AU - Harris, J.

    AU - McGreal, E.

    AU - Sim, R. B.

    AU - Isacke, C. M.

    AU - Gordon, S.

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    AB - Mannose receptor (MR) is the best characterised member of a family of four endocytic molecules that share a common domain structure; a cysteine-rich (CR) domain, a fibronectin-type II (FNII) domain and tandemly arranged C-type lectin-like domains (CTLD, eight in the case of MR). Two distinct lectin activities have been described for MR. The CR domain recognises sulphated carbohydrates while the CTLD mediate binding to mannose, fucose or N-acetylglucosamine. FNII domains are known to be important for collagen binding and this has been studied in the context of two members of the MR family, Endo180 and the phospholipase A(2) receptor. Here, we have investigated whether the broad and effective lectin activity mediated by the CR domain and CTLD of MR is favoured to the detriment of FNII-mediated interaction(s). We show that MR is able to bind and internalise collagen in a carbohydrate-independent manner and that MR deficient macrophages have a marked defect in collagen IV and gelatin internalisation. These data have major implications at the molecular level as there are now three distinct ligand-binding sites described for MR. Furthermore our findings extend the range of endogenous ligands recognised by MR, a molecule firmly placed at. the interface between homeostasis and immunity.

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