Papp Eszter, Nardai Gábor, Söti Csaba, Csermely Péter
Department of Medical Chemistry, Semmelweis University, P.O. Box 260, H-1444 Budapest 8, Hungary.
Biofactors. 2003;17(1-4):249-57. doi: 10.1002/biof.5520170124.
Protection against oxidative stress is highly interrelated with the function of the most ancient cellular defense system, the network of molecular chaperones, heat shock, or stress-proteins. These ubiquitous, conserved proteins help other proteins and macromolecules to fold or re-fold and reach their final, native conformation. Redox regulation of protein folding becomes especially important during the preparation of extracellular proteins to the outside oxidative milieu, which should take place in a gradual and step-by-step controlled manner in the endoplasmic reticulum or in the periplasm. Several chaperones, such as members of the Hsp33 family in yeast and the plethora of small heat shock proteins as well as one of the major chaperones, Hsp70 are able to act against cytoplasmic oxidative damage. Abrupt changes of cellular redox status lead to chaperone induction. The function of several chaperones is tightly regulated by the surrounding redox conditions. Moreover, our recent data suggest that chaperones may act as a central switchboard for the transmission of redox changes in the life of the cell.
抗氧化应激与最古老的细胞防御系统——分子伴侣、热休克或应激蛋白网络的功能高度相关。这些普遍存在且保守的蛋白质帮助其他蛋白质和大分子折叠或重新折叠，以达到其最终的天然构象。在将细胞外蛋白质准备好释放到外部氧化环境的过程中，蛋白质折叠的氧化还原调节变得尤为重要，这一过程应该在内质网或周质中以逐步控制的方式进行。几种伴侣蛋白，如酵母中Hsp33家族的成员、大量的小热休克蛋白以及主要伴侣蛋白之一Hsp70，能够对抗细胞质氧化损伤。细胞氧化还原状态的突然变化会导致伴侣蛋白的诱导。几种伴侣蛋白的功能受到周围氧化还原条件的严格调控。此外，我们最近的数据表明，伴侣蛋白可能作为细胞生命中氧化还原变化传递的中央总机。
