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          Institute: MPI für experimentelle Medizin     Collection: Molecular Neurobiology     Display Documents

ID: 18272.0, MPI für experimentelle Medizin / Molecular Neurobiology
Loss of the zymogen granule protein syncollin affects pancreatic protein synthesis and transport but not secretion
Authors:Antonin, W.; Wagner, M.; Riedel, D.; Brose, Nils; Jahn, Reinhard
Date of Publication (YYYY-MM-DD):2002-03
Title of Journal:Molecular and Cellular Biology
Journal Abbrev.:Mol. Cell. Biol.
Issue / Number:5
Start Page:1545
End Page:1554
Review Status:Peer-review
Audience:Experts Only
Abstract / Description: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.
Comment of the Author/Creator:Date: 2002, MAR
External Publication Status:published
Document Type:Article
Communicated by:Nils Brose
Affiliations:MPI für experimentelle Medizin/Molecular neurobiology
External Affiliations:Max Planck Inst Biophys Chem, Dept Neurobiol, Fassberg 11, D-; 37077 Gottingen, Germany; Max Planck Inst Biophys Chem, Dept Neurobiol, D-37077 Gottingen, Germany; Max Planck Inst Biophys Chem, Dept Mol Cell Biol, D-37077 Gottingen, Germany;
Identifiers:ISI:000173837000026 [ID No:1]
ISSN:0270-7306 [ID No:2]
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