The ubiquitin-proteasome pathway is critical for the degradation of short-lived proteins in eukaryotic cells, and inhibition of this pathway could induce apoptosis in human leukaemic Mo7e cells. We analyzed the proteo...The ubiquitin-proteasome pathway is critical for the degradation of short-lived proteins in eukaryotic cells, and inhibition of this pathway could induce apoptosis in human leukaemic Mo7e cells. We analyzed the proteomic response of Mo7e cells by inhibiting the ubiquitin-proteasome pathway with . Among 72 protein spots showing significant changes in expression on 2-D protein gels, 4 of them were strongly increased. They are identified as Rho GDP dissociation inhibitor (GDI) βprotein, profilin 1, adenylate kinase isoenzyme 2, and eIF-5A as determined by peptide mass fingerprinting(PMF) using MALDI-TOF-MS a nd展开更多
基金This work was supported by grants from National Natural Science fOundation of China (No.30070377),and National High Technology Research and Development Program of China (No. 2001AA233041).
文摘The ubiquitin-proteasome pathway is critical for the degradation of short-lived proteins in eukaryotic cells, and inhibition of this pathway could induce apoptosis in human leukaemic Mo7e cells. We analyzed the proteomic response of Mo7e cells by inhibiting the ubiquitin-proteasome pathway with . Among 72 protein spots showing significant changes in expression on 2-D protein gels, 4 of them were strongly increased. They are identified as Rho GDP dissociation inhibitor (GDI) βprotein, profilin 1, adenylate kinase isoenzyme 2, and eIF-5A as determined by peptide mass fingerprinting(PMF) using MALDI-TOF-MS a nd
