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Loss of the zymogen granule protein syncollin affects pancreatic protein synthesis and transport but not secretion

MPS-Authors
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Antonin,  W.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Wagner,  M.
Department of Molecular Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Antonin, W., Wagner, M., Riedel, D., Brose, N., & Jahn, R. (2002). Loss of the zymogen granule protein syncollin affects pancreatic protein synthesis and transport but not secretion. Molecular and Cellular Biology, 22(5), 1545-1554. Retrieved from http://mcb.asm.org/cgi/reprint/22/5/1545.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F42C-6
Abstract
Syncollin is a small protein that is abundantly expressed in pancreatic acinar cells and that is tightly associated with the lumenal side of the zymogen granule membrane. To shed light on the hitherto unknown function of syncollin, we have generated syncollin-deficient mice. The mice are viable and show a normal pancreatic morphology as well as normal release kinetics in response to secretagogue stimulation. Although syncollin is highly enriched in zymogen granules, no change was found in the overall protein content and in the levels of chymotrypsin, trypsin, and amylase. However, syncollin-deficient mice reacted to caerulein hyper-stimulation with a more severe pancreatitis. Furthermore, the rates of both protein synthesis and intracellular transport of secretory proteins were reduced. We conclude that syncollin plays a role in maturation and/or concentration of zymogens in zymogen granules.