Department of Immunology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil.
Scand J Immunol. 2011 May;73(5):436-48. doi: 10.1111/j.1365-3083.2010.02504.x.
Chaperone production is an essential step for proper folding of certain proteins. Accumulation of misfolded/unfolded proteins within the endoplasmic reticulum (ER) lumen triggers a signalling pathway named unfolded protein response (UPR). Upon activation, the UPR pathway augments transcription of ER chaperones increasing protein folding, decreases protein translation to ameliorate the ER overload, increases protein degradation, and activates the apoptotic programme if all previous measures fail. In this review, we will cover the chaperones involved in folding of proteins related to the immune response, followed by an overview of the UPR pathway. Lastly, we will discuss data from this last decade that demonstrate how the improper activation of the UPR pathway has been uncovered as a mechanism responsible for failure to mount a proper immune response, both innate and adaptive.
伴侣蛋白的产生是某些蛋白质正确折叠所必需的步骤。内质网（ER）腔中错误折叠/未折叠蛋白质的积累会触发一种称为未折叠蛋白反应（UPR）的信号通路。激活后，UPR 途径会增加 ER 伴侣蛋白的转录，从而增加蛋白质折叠，减少蛋白质翻译以减轻 ER 过载，增加蛋白质降解，如果所有先前的措施都失败，则激活凋亡程序。在这篇综述中，我们将介绍与免疫反应相关的蛋白质折叠所涉及的伴侣蛋白，然后概述 UPR 途径。最后，我们将讨论过去十年的数据，这些数据表明，UPR 途径的不当激活如何被揭示为导致无法产生适当免疫反应（先天和适应性）的机制。
