Quantitative Proteomics Analysis of Pancreatic Zymogen Granule Membrane Proteins View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2009

AUTHORS

Xuequn Chen , Philip C. Andrews

ABSTRACT

Pancreatic zymogen granules (ZG) are specialized for digestive enzyme storage and regulated secretion in the exocrine pancreas and are a classical model for studying secretory granule function. To understand the function of this organelle, we have conducted a proteomic study to identify the ZG membrane proteins from ZGs purified by Percoll gradient centrifugation. By combining multiple separation strategies including two-dimensional gel electrophoresis and two-dimensional liquid chromatography with tandem mass spectrometry (TMS), we identified 101 proteins from purified ZG membranes including a large number of proteins previously unknown on ZG membranes. To distinguish intrinsic membrane proteins from soluble and peripheral membrane proteins, a quantitative proteomics strategy was developed to measure the enrichment of intrinsic membrane proteins through the purification steps by labeling crude, KBr-, and Na(2)CO(3)-washed ZG membranes with multiplexed isobaric tags (iTRAQ), 114, 116 and 117, respectively. The proteins with 117:114 ratios greater than one correlated well with known or predicted intrinsic membrane proteins. More... »

PAGES

327-338

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-60327-310-7_23

DOI

http://dx.doi.org/10.1007/978-1-60327-310-7_23

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014574380

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19153703


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