Di Felice V, David S, Cappello F, Farina F, Zummo G
Human Anatomy Section, Department of Experimental Medicine, University of Palermo, Via del vespro 129, 90127 Palermo, Italy.
Cell Mol Life Sci. 2005 Jan;62(1):4-9. doi: 10.1007/s00018-004-4367-6.
Heat shock protein 60 (HSP60) plays an important role in the protein folding of prokaryotic and eukaryotic cells. Most of the papers published on chlamydial HSP60 concern its role in immune response during infection. In the last decade, exposure to Chlamydia trachomatis has been consistently associated with the development of cervical and ovarian cancer. Moreover, it has been suggested that chlamydial HSP60 may have an anti-apoptotic effect during persistent infection. We hypothesize that the accumulation of exogenous chlamydial HSP60 in the cytoplasm of actively replicating eukaryotic cells may interfere with the regulation of the apoptotic pathway. The concomitant expression of viral oncoproteins and/or the presence of mutations may lead to the ability to survive apoptotic stimuli, loss of replicative senescence, uncontrolled proliferation and, finally neoplastic transformation.
热休克蛋白60（HSP60）在原核细胞和真核细胞的蛋白质折叠中起重要作用。大多数关于衣原体HSP60的论文都关注其在感染期间免疫反应中的作用。在过去十年中，沙眼衣原体感染一直与宫颈癌和卵巢癌的发生相关。此外，有人提出衣原体HSP60在持续感染期间可能具有抗凋亡作用。我们假设，在活跃复制的真核细胞细胞质中外源衣原体HSP60的积累可能会干扰凋亡途径的调节。病毒癌蛋白的同时表达和/或突变的存在可能导致细胞有能力在凋亡刺激下存活、丧失复制性衰老、不受控制地增殖，并最终发生肿瘤转化。
