Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052216 | FEBS Letters | 2006 | 6 Pages |
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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Authors
Christiane Habich, Karina Kempe, Francisco J. Gomez, Mark Lillicrap, Hill Gaston, Ruurd van der Zee, Hubert Kolb, Volker Burkart,