Cysteine and Glutathione Secretion in Response to Protein Disulfide Bond Formation in the ER

• DOI: 10.1126/science.277.5332.1681
• Publication Date: 2002-07-27T09:44:47Z
• Authors: Stephana Carelli; Aldo Ceriotti; Andrea Cabibbo; Giorgio Fassina; Menotti Ruvo; Roberto Sitia
• Keywords: Secretory protein; Thiol; Dithiothreitol; Oxidizing agent

Protein folding in the endoplasmic reticulum (ER) often involves formation of disulfide bonds. The oxidizing conditions required within this organelle were shown to be maintained through release small thiols, mainly cysteine and glutathione. Thiol secretion was stimulated when proteins rich bonds translocated into ER, prevented by inhibition protein synthesis. Endogenously generated glutathione counteracted thiol-mediated retention ER altered extracellular redox. thiols might link bond intra- intercellular redox signaling.