Melikov Aleksandr, Novák Petr
BIOCEV, Faculty of Science, Charles University, Prague, Czech Republic.
BIOCEV, Institute of Microbiology, Czech Academy of Sciences, Prague, Czech Republic.
Folia Biol (Praha). 2024;70(3):152-165. doi: 10.14712/fb2024070030152.
Protein folding is an extremely complicated process, which has been extensively tackled during the last decades. In vivo, a certain molecular machinery is responsible for assisting the correct folding of proteins and maintaining protein homeostasis: the members of this machinery are the heat shock proteins (HSPs), which belong among molecular chaperones. Mutations in HSPs are associated with several inherited diseases, and members of this group were also proved to be involved in neurodegenerative pathologies (e.g., Alzheimer and Parkinson diseases), cancer, viral infections, and antibiotic resistance of bacteria. Therefore, it is critical to understand the principles of HSP functioning and their exact role in human physiology and pathology. This review attempts to briefly describe the main chaperone families and the interplay between individual chaperones, as well as their general and specific functions in the context of cell physiology and human diseases.
蛋白质折叠是一个极其复杂的过程，在过去几十年中已得到广泛研究。在体内，特定的分子机制负责协助蛋白质正确折叠并维持蛋白质稳态：该机制的成员是热休克蛋白（HSPs），属于分子伴侣。HSPs中的突变与多种遗传性疾病相关，并且该组中的成员也被证明与神经退行性疾病（如阿尔茨海默病和帕金森病）、癌症、病毒感染以及细菌的抗生素耐药性有关。因此，了解HSPs的功能原理及其在人类生理和病理中的确切作用至关重要。本综述试图简要描述主要的伴侣蛋白家族、各个伴侣蛋白之间的相互作用，以及它们在细胞生理学和人类疾病背景下的一般和特定功能。
