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. 2003 Aug;23(16):5790–5802. doi: 10.1128/MCB.23.16.5790-5802.2003

FIG. 2.

FIG. 2.

HSP27 enhances the degradation of ubiquitinated proteins in stressed cells. (A) Control-transfected (Co) and HSP27-transfected U937 cells either were left untreated or were treated with 100 μM etoposide (VP16) for 4 h in the absence or presence of 25 μM MG132. Protein ubiquitination (Ub-proteins) was monitored by Western blotting with an antiubiquitin antibody. α-actin served as the loading control. (B) Densitometry analysis of Ub-proteins in three independent experiments (mean and standard deviation) similar to that shown in panel A. AU, arbitrary units. (C) U937 cells either were left untreated (NT) or were exposed for 1 h to 42°C (HS) and then were incubated at 37°C for the indicated times. The indicated proteins were studied by Western blotting. α-Actin served as the loading control. (D) Densitometry analysis of Ub-proteins shown in panel C.