Heat shock proteins (HSPs) are developmentally conserved families of protein found in both prokaryotic and eukaryotic organisms. HSPs are engaged in a diverse range of physiological processes, including molecular chaperone activity to assist the initial protein folding or promote the unfolding and refolding of misfolded intermediates to acquire the normal or native conformation and its translocation and prevent protein aggregation as well as in immunity, apoptosis, and autophagy. These molecular chaperonins are classified into various families according to their molecular size or weight, encompassing small HSPs (e.g., HSP10 and HSP27), HSP40, HSP60, HSP70, HSP90, and the category of large HSPs that include HSP100 and ClpB proteins. The overexpression of HSPs is induced to counteract cell stress at elevated levels in a variety of solid tumors, including anticancer chemotherapy, and is closely related to a worse prognosis and therapeutic resistance to cancer cells. HSPs are also involved in anti-apoptotic properties and are associated with processes of cancer progression and development, such as metastasis, invasion, and cell proliferation. This review outlines the previously mentioned HSPs and their significant involvement in diverse mechanisms of tumor advancement and metastasis, as well as their contribution to identifying potential targets for therapeutic interventions.
热休克蛋白（HSPs）是一类在进化上高度保守的蛋白质家族，广泛存在于原核生物与真核生物中。它们参与多种生理过程，包括通过分子伴侣活性协助蛋白质初始折叠、促进错误折叠中间体的解折叠与重折叠以获取正常构象、介导蛋白质转运、防止蛋白质聚集，并在免疫应答、细胞凋亡及自噬等过程中发挥重要作用。根据分子量大小，这些分子伴侣蛋白可分为多个家族，包括小分子热休克蛋白（如HSP10和HSP27）、HSP40、HSP60、HSP70、HSP90以及大分子热休克蛋白类别（如HSP100和ClpB蛋白）。在多种实体肿瘤中，热休克蛋白的过度表达被诱导以应对细胞应激（包括抗癌化疗），其高表达与患者不良预后及肿瘤细胞治疗抵抗密切相关。此外，热休克蛋白具有抗凋亡特性，参与癌症进展与发展的关键过程，如转移、侵袭和细胞增殖。本文综述了上述热休克蛋白家族及其在肿瘤进展与转移机制中的重要作用，并探讨其作为潜在治疗靶点的价值。
肿瘤(癌症)患者之家