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Science 12 September 1997:
Vol. 277. no. 5332, pp. 1681 - 1684
DOI: 10.1126/science.277.5332.1681
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Reports

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

Stephana Carelli, Aldo Ceriotti, Andrea Cabibbo, Giorgio Fassina, Menotti Ruvo, Roberto Sitia *

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.

S. Carelli, A. Cabibbo, R. Sitia, DIBIT, Istituto Scientifico San Raffaele, Milano, Italy.
A. Ceriotti, Istituto Biosintesi Vegetali, Consiglio Nazionale delle Ricerche, Milano, Italy.
G. Fassina and M. Ruvo, Tecnogen, Piana di Monte Verna (CE), Italy.
*   To whom correspondence should be addressed. E-mail: sitiar{at}dibit.hsr.it

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Science. ISSN 0036-8075 (print), 1095-9203 (online)