Digestive end products mobilize secretory proteins from subcellular stores in the pancreas.

@article{Grendell1981DigestiveEP,
  title={Digestive end products mobilize secretory proteins from subcellular stores in the pancreas.},
  author={James H. Grendell and S. S. Rothman},
  journal={The American journal of physiology},
  year={1981},
  volume={241 1},
  pages={G67-73}
}
Two digestive end products, D-glucose and L-lysine, produced substantial concentration-dependent release of amylase and trypsinogen, respectively, from subcellular storage pools into a postmicrosomal supernatant fraction of rat pancreatic tissue homogenate. This process was selective in that D-glucose did not lead to trypsinogen release, while L-lysine did not effect amylase. An analogue of D-glucose, 2-deoxy-D-glucose, was much less potent than D-glucose on an equimolar basis. Half-maximal… CONTINUE READING