摘要
热休克蛋白（HSP）是一类在生物进化中高度保守、广泛存在于原核和真核生物中的蛋白质。大量资料表明，HSP作为分子伴侣，参与其它蛋白质的折叠、转运、合成等过程，并可与细胞内的其它蛋白质结合，参与细胞的抗损伤、修复和热耐受过程，某些热休克蛋白还具有佐剂效应，能够激活免疫应答反应，以往对于HSP70及其免疫治疗的研究较为广泛。近年来随着对热休克蛋白研究的不断深入，人们发现高分子量的HSP110因其强大的分子伴侣功能而具备独特的佐剂效应，因而被认为在瘤苗制备及抗肿瘤免疫中具有很大的应用前景。
Heat shock proteins （HSPs） are most highly conserved proteins in prokaryotes and eukarytes. A vgreat of data showed that HSPs act as molecular chaperones to regulate protein folding,transloeation, and assembly,it can combine with other proteins existing in cells and participate in the process of anti-damage, repair and thermotoleranee of cells, some HSPs can work as adjuvant and activate immune response. In the past, many researches focused on HSP70 and its role of immune therapy. Recent years,large molecular, HSP 110 was found to has the unique adjuvant effect since its powerful moleeular chaperoning function, thus was thought to has wide application perspective in the preparation of tumor racine and anti-tumor immunity.
出处
《国际免疫学杂志》
CAS
2007年第4期213-216,共4页
International Journal of Immunology
基金
国家重大基础研究计划“973”免疫学项目（2001CB510002）
