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Analysis of the membrane proteome of canine pancreatic rough microsomes identifies a novel Hsp40, termed ERj7
Author(s) -
Zahedi René P.,
Völzing Christian,
Schmitt Andreas,
Frien Michael,
Jung Martin,
Dudek Johanna,
Wortelkamp Stefanie,
Sickmann Albert,
Zimmermann Richard
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800722
Subject(s) - biogenesis , chaperone (clinical) , microbiology and biotechnology , proteome , proteomics , secretion , secretory protein , hsp70 , microsome , biology , membrane protein , chemistry , biochemistry , heat shock protein , membrane , in vitro , gene , medicine , pathology
The rough ER (rER) plays a central role in the biogenesis of most extracellular and many organellar proteins in eukaryotic cells. Cells that are specialized in protein secretion, such as pancreatic cells, are particularly rich in rER. In the process of cell homogenization, the rER is converted into ribosome‐studded vesicles, the so‐called rough microsomes. Here we report on a membrane proteomic analysis of canine pancreatic rough microsomes. Special emphasis was placed on components involved in the various aspects of protein biogenesis, such as protein transport, protein folding, protein modification, and protein degradation. Our results indicate that the Hsp70‐chaperone network that is present in the pancreatic ER is even more complex than previously thought, and suggest that the pancreatic rER has a significant capacity for protein degradation.