Clark P R, Ménoret A
Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington 06030, USA.
Cell Stress Chaperones. 2001 Apr;6(2):121-5. doi: 10.1379/1466-1268(2001)006<0121:tihaam>2.0.co;2.
Growing evidence indicates that the stress response in general and heat shock proteins (Hsps) in particular have a profound impact on tumor immunogenicity. In this study, we show that tumor cells subjected to a nonlethal heat shock stress are unable to form tumors in syngenic mice, whereas they do so in athymic nude mice. Moreover, heat-shocked MethA immunity is tumor specific. Enhancement of T-cell-mediated immunogenicity correlates with the expression of the inducible Hsp70 but not the constitutive Hsc70. These observations have a bearing on the proposed functional role of Hsp-peptide association in antigen processing and presentation by major histocompatibility complex I molecules under normal and stressful conditions.
越来越多的证据表明，一般的应激反应，尤其是热休克蛋白（Hsps），对肿瘤免疫原性有深远影响。在本研究中，我们发现，经受非致死性热休克应激的肿瘤细胞无法在同基因小鼠体内形成肿瘤，而在无胸腺裸鼠体内则可以。此外，热休克处理后的MethA免疫具有肿瘤特异性。T细胞介导的免疫原性增强与诱导型Hsp70的表达相关，而与组成型Hsc70的表达无关。这些观察结果与热休克蛋白-肽结合在正常和应激条件下通过主要组织相容性复合体I分子进行抗原加工和呈递中所提出的功能作用有关。
