Carelli S, Ceriotti A, Cabibbo A, Fassina G, Ruvo M, Sitia R
DIBIT, Istituto Scientifico San Raffaele, Milano, Italy.
Science. 1997 Sep 12;277(5332):1681-4. doi: 10.1126/science.277.5332.1681.
Protein folding in the endoplasmic reticulum (ER) often involves the formation of disulfide bonds. The oxidizing conditions required within this organelle were shown to be maintained through the release of small thiols, mainly cysteine and glutathione. Thiol secretion was stimulated when proteins rich in disulfide bonds were translocated into the ER, and secretion was prevented by the inhibition of protein synthesis. Endogenously generated cysteine and glutathione counteracted thiol-mediated retention in the ER and altered the extracellular redox. The secretion of thiols might link disulfide bond formation in the ER to intra- and intercellular redox signaling.
内质网（ER）中的蛋白质折叠通常涉及二硫键的形成。已表明，该细胞器内所需的氧化条件是通过释放小分子硫醇（主要是半胱氨酸和谷胱甘肽）来维持的。当富含二硫键的蛋白质转运到内质网时，硫醇分泌受到刺激，而蛋白质合成的抑制则可阻止硫醇分泌。内源性生成的半胱氨酸和谷胱甘肽可抵消硫醇介导的内质网滞留作用，并改变细胞外氧化还原状态。硫醇的分泌可能将内质网中二硫键的形成与细胞内和细胞间的氧化还原信号传导联系起来。
