Open AccessChaperone proteins identified from synthetic proteasome inhibitor‐induced inclusions in PC12 cells by proteomic analysis
Author(s) -
Li Xing'an,
Zhang Yingjiu,
Hu Yihong,
Chang Ming,
Liu Tao,
Wang Danping,
Zhang Yu,
Zhang Lei,
Hu Linsen
Publication year - 2008
Publication title -
acta biochimica et biophysica sinica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.771
H-Index - 57
eISSN - 1745-7270
pISSN - 1672-9145
DOI - 10.1111/j.1745-7270.2008.00416.x
Subject(s) - chaperone (clinical) , proteome , proteasome , proteomics , biochemistry , biology , chemistry , microbiology and biotechnology , pathology , medicine , gene
Chaperone proteins are significant in Lewy bodies, but the profile of chaperone proteins is incompletely unraveled. Proteomic analysis is used to determine protein candidates for further study. Here, to identify potential chaperone proteins from agent‐induced inclusions, we carried out proteomic analysis of artificially synthetic proteasome inhibitor (PSI)‐induced inclusions formed in PC12 cells exposed to 10 μM PSI for 48 h. Using biochemical fractionation, 2‐D electrophoresis, and identification through peptide mass fingerprints searched against multiple protein databases, we repeatedly identified eight reproducible chaperone proteins from the PSI‐induced inclusions. Of these, 58 kDa glucose regulated protein, 75 kDa glucose regulated protein, and calcium‐binding protein 1 were newly identified. The other five had been reported to be consistent components of Lewy bodies. These findings suggested that the three potential chaperone proteins might be recruited to PSI‐induced inclusions in PC12 cells under proteasome inhibition.