Heat shock protein 60: Identification of specific epitopes for binding to primary macrophages
Heat shock protein 60: Identification of specific epitopes for binding to primary macrophages
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DOI：
10.1016/j.febslet.2005.11.060
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发表时间：
2006-01-09
期刊：
影响因子：
3.5
通讯作者：
Burkart, V
中科院分区：
文献类型：
--
作者：
Habich, C;Kempe, K;Burkart, V
在本研究中，我们描述了负责与初级巨噬细胞结合的人热休克蛋白 (HSP) 60 的区域。使用 HSP60 序列的 20 聚体肽与来自 C57BL/6J 小鼠的 HSP60 竞争结合巨噬细胞的研究表明，区域 aa241-260、aa391-410 和 aa461-480 参与表面结合。缺少 N 端 137、243 或 359 个氨基酸的 HSP60 突变体不同程度地抑制了 HSP60 与初级巨噬细胞的结合，表明所有三个区域都是最佳结合所必需的。对不同原核和真核 HSP60 物种的分析表明，系统发育上分离的 HSP60 物种在初级巨噬细胞上使用不同的结合位点。 (c) 2005 年欧洲生化学会联合会。由 Elsevier B.V. 出版。保留所有权利。
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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.