Disruption of disulfide bonds exhibits differential effects on trafficking of regulated secretory proteins.

@article{Gorr1999DisruptionOD,
  title={Disruption of disulfide bonds exhibits differential effects on trafficking of regulated secretory proteins.},
  author={Sven-Ulrik Gorr and Xue Fen Huang and Darrin J. Cowley and Regina Kuliawat and Peter Arvan},
  journal={The American journal of physiology},
  year={1999},
  volume={277 1 Pt 1},
  pages={C121-31}
}
For several secretory proteins, it has been hypothesized that disulfide-bonded loop structures are required for sorting to secretory granules. To explore this hypothesis, we employed dithiothreitol (DTT) treatment in live pancreatic islets, as well as in PC-12 and GH(4)C(1) cells. In islets, disulfide reduction in the distal secretory pathway did not increase constitutive or constitutive-like secretion of proinsulin (or insulin). In PC-12 cells, DTT treatment caused a dramatic increase in… CONTINUE READING
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