Analysis of mannose receptor regulation by IL-4, IL-10, and proteolytic processing using novel monoclonal antibodies

L. Martinez-Pomares, D. M. Reid, G. D. Brown, P. R. Taylor, R. J. Stillion, S. A. Linehan, S. Zamze, S. Gordon, Simon Yuk Chun Wong

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107 Citations (Scopus)

Abstract

The study of the murine macrophage mannose receptor (MR) has been hampered by the lack of specific reagents. We have generated and characterized novel anti-MR monoclonal antibodies and used them to analyze MR expression in primary mouse macrophages (MO). In BioGel- and thioglycollate-elicited MO, interleukin (IL)-4 up-regulated total cell-associated MR (cMR), correlating with enhanced surface expression. We investigated the influence of IL-10, a well-characterized deactivator of MO function, on MR levels and observed that it had a similar effect to IL-4. In both cases, enhanced cMR levels translated into increased production of the soluble form of the receptor (sMR). We have demonstrated the presence of sMR in cultures of stable non-MO transductants expressing full-length MR, indicating that the proteolytic activity responsible for cMR cleavage is not MO-restricted. These data support a role for the MR in T helper cell type 2 cytokine-driven, immune responses and suggest a non-MO contribution to sMR production in vivo.

Original languageEnglish
Pages (from-to)604-613
Number of pages9
JournalJournal of Leukocyte Biology
Volume73
DOIs
Publication statusPublished - 2003

Keywords

  • macrophage
  • shedding
  • CYSTEINE-RICH DOMAIN
  • CARBOHYDRATE-RECOGNITION DOMAINS
  • MACROPHAGES IN-VITRO
  • BETA 1,4GLCNAC BETA
  • B-CELL FOLLICLES
  • DENDRITIC CELLS
  • MURINE MACROPHAGES
  • INTERFERON-GAMMA
  • HOST-DEFENSE
  • ENDOTHELIAL-CELLS

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