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Submitted on June 3, 2005
Revised on October 31, 2005
Accepted on November 8, 2005

Organellar proteomics: Analysis of pancreatic zymogen granule membranes

Xuequn Chen, Angela K. Walker, John R. Strahler, Eric S. Simon, Sarah L. Tomanicek-Volk, Bradley B. Nelson, Mary C. Hurley, Stephen A. Ernst, John A. Williams, and Philip C. Andrews

The University of Michigan, Ann Arbor, MI 48109

Corresponding Author: xuequnc{at}umich.edu

The zymogen granule (ZG) is the specialized organelle in pancreatic acinar cells for digestive enzyme storage and regulated secretion, and has been a model for studying secretory granule functions. In an initial effort to comprehensively understand the functions of this organelle, we conducted a proteomic study to identify proteins from highly purified ZG membranes. By combining 2D gel electrophoresis and 2D LC with tandem mass spectrometry, 101 proteins were identified from purified ZG membranes including 28 known ZG proteins and 73 previously unknown proteins, including SNAP 29, Rab27B, Rab11A, Rab6, Rap1 and myosin Vc. Moreover, several hypothetical proteins were identified, representing potential novel proteins. The ZG localization of nine of these proteins was further confirmed by immunocytochemistry. To distinguish intrinsic membrane proteins from soluble and peripheral membrane proteins, a quantitative proteomics strategy was used to measure the enrichment of intrinsic membrane proteins through the purification process. The iTRAQ ratios correlated well with known or TMHMM-predicted soluble or membrane proteins. By combining subcellular fractionation with high-resolution separation and comprehensive identification of proteins, we have begun to elucidate zymogen granule functions through proteomic and subsequent functional analysis of its membrane components.


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