University of Maryland Biotechnology Institute, Center of Marine Biotechnology, Columbus Center, Baltimore, Maryland, USA.
Ann N Y Acad Sci. 2010 Jun;1197:85-93. doi: 10.1111/j.1749-6632.2010.05187.x.
Aging entails progressive deterioration of molecules and supramolecular structures, including Hsp chaperones and their complexes, paralleled by functional decline. Recent research has changed our views on Hsp chaperones. They work inside and outside cells in many locations, alone or forming teams, interacting with cells, receptors, and molecules that are not chaperones, in roles that are not typically attributed to chaperones, such as protein folding. Hsp chaperones form a physiological system with a variety of functions and interactions with other systems, for example, the immune system. We propose that chaperone malfunctioning due to structural damage or gene dysregulation during aging has an impact on the immune system, creating the conditions for an overall malfunction of both systems. Pathological chaperones cannot interact with the immune system as normal ones do, and this leads to an overall readjustment of the interactions that is apparent during senescence and is likely to cause many of its manifestations.
衰老是分子和超分子结构逐渐恶化的过程，包括热休克蛋白伴侣及其复合物，伴随着功能下降。最近的研究改变了我们对热休克蛋白伴侣的看法。它们在细胞内外的许多位置单独或形成团队工作，与细胞、受体和非伴侣分子相互作用，发挥通常不归因于伴侣分子的作用，例如蛋白质折叠。热休克蛋白伴侣形成了一个具有多种功能的生理系统，并与其他系统（例如免疫系统）相互作用。我们提出，由于衰老过程中结构损伤或基因失调导致伴侣蛋白功能失常，会对免疫系统产生影响，为两个系统的整体功能失常创造条件。病理伴侣蛋白不能像正常伴侣蛋白那样与免疫系统相互作用，这导致在衰老过程中明显的相互作用的全面调整，并且可能导致其许多表现。
