Heat shock protein 60: identification of specific epitopes for binding to primary macrophages |
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Authors: | Habich Christiane Kempe Karina Gomez Francisco J Lillicrap Mark Gaston Hill van der Zee Ruurd Kolb Hubert Burkart Volker |
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Affiliation: | German Diabetes Clinic, German Diabetes Center, Leibniz Institute, Heinrich-Heine-University of Düsseldorf, D-40225 Düsseldorf, Germany. christiane.habich@ddz.uni-duesseldorf.de |
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Abstract: | In the present study, we characterized regions of human heat shock protein (HSP) 60 responsible for binding to primary macrophages. Studies using 20-mer peptides of the HSP60 sequence to compete with HSP60-binding to macrophages from C57BL/6J mice showed that regions aa241-260, aa391-410 and aa461-480 are involved in surface-binding. HSP60 mutants, lacking the N-terminal 137, 243 or 359 amino acids, inhibited HSP60-binding to primary macrophages to different degrees, demonstrating that all three regions are required for optimal binding. Analysis of different pro- and eukaryotic HSP60 species indicated that phylogenetically separate HSP60 species use different binding sites on primary macrophages. |
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Keywords: | HSP, heat shock protein IL, interleukin TLR, Toll-like receptor BMM, bone marrow-derived macrophages |
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