Habich Christiane, Kempe Karina, Gomez Francisco J, Lillicrap Mark, Gaston Hill, van der Zee Ruurd, Kolb Hubert, Burkart Volker
German Diabetes Clinic, German Diabetes Center, Leibniz Institute, Heinrich-Heine-University of Düsseldorf, D-40225 Düsseldorf, Germany.
FEBS Lett. 2006 Jan 9;580(1):115-20. doi: 10.1016/j.febslet.2005.11.060. Epub 2005 Dec 6.
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.
在本研究中，我们对人类热休克蛋白（HSP）60与原代巨噬细胞结合的区域进行了表征。使用HSP60序列的20肽来竞争HSP60与C57BL/6J小鼠巨噬细胞结合的研究表明，aa241 - 260、aa391 - 410和aa461 - 480区域参与表面结合。缺少N端137、243或359个氨基酸的HSP60突变体对HSP60与原代巨噬细胞的结合有不同程度的抑制作用，表明这三个区域对于最佳结合都是必需的。对不同原核和真核HSP60物种的分析表明，系统发育上不同的HSP60物种在原代巨噬细胞上使用不同的结合位点。
