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Analysis of mannose receptor regulation by IL‐4, IL‐10, and proteolytic processing using novel monoclonal antibodies
Author(s) -
MartinezPomares Luisa,
Reid Delyth M.,
Brown Gordon D.,
Taylor Philip R.,
Stillion Richard J.,
Linehan Sheena A.,
Zamze Susanne,
Gordon Siamon,
Wong Simon Y. C.
Publication year - 2003
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.0902450
Subject(s) - mannose receptor , biology , monoclonal antibody , microbiology and biotechnology , mannose , receptor , cytokine , immune system , antibody , macrophage , in vitro , immunology , biochemistry
The study of the murinemacrophage 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 (MØ). In BioGel‐ and thioglycollate‐elicited MØ, 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 MØ 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‐MØ transductants expressing full‐length MR, indicating that the proteolytic activity responsible for cMR cleavage is not MØ‐restricted. These data support a role for the MR in T helper cell type 2 cytokine‐driven, immune responses and suggest a non‐MØ contribution to sMR production in vivo.