Chaperone proteins identified from synthetic proteasome inhibitor-induced inclusions in PC12 cells by proteomic analysis.
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 microM 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.
Li
Xing'an
X
Laboratory for Proteomics, Department of Neurology, The First Affiliated Hospital of Jilin University, Changchun 130021, China.
Zhang
Yingjiu
Y
Hu
Yihong
Y
Chang
Ming
M
Liu
Tao
T
Wang
Danping
D
Zhang
Yu
Y
Zhang
Lei
L
Hu
Linsen
L
D000818:Animals; D002479:Inclusion Bodies / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D016716:PC12 Cells; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D061988:Proteasome Inhibitors; D020543:Proteome / Q000378:metabolism*; D051381:Rats
D018832:Molecular Chaperones; D061988:Proteasome Inhibitors; D020543:Proteome; D046988:Proteasome Endopeptidase Complex