| Kim I |
------>authors3_c=None ------>paper_class1=1 ------>Impact_Factor=None ------>paper_class3=2 ------>paper_class2=1 ------>vol=298 ------>confirm_bywho=ryyuan ------>insert_bywho=hsuc ------>Jurnal_Rank=None ------>authors4_c=None ------>comm_author= ------>patent_EDate=None ------>authors5_c=None ------>publish_day=None ------>paper_class2Letter=None ------>page2=238 ------>medlineContent= ------>unit=E0100 ------>insert_date=20050701 ------>iam=7 ------>update_date=None ------>author=??? ------>change_event=4 ------>ISSN=None ------>authors_c=None ------>score=400 ------>journal_name=Exp Cell Res ------>paper_name=Ahn YS. Pyrrolidine dithiocarbamate and zinc inhibit proteasome-dependent proteolysis. ------>confirm_date=20050711 ------>tch_id=091141 ------>pmid=15242777 ------>page1=229 ------>fullAbstract=Proteasomes play important roles in a variety of cellular processes such as cell cycle progression, signal transduction and immune responses. Proteasome activity is important in maintaining rapid turnover of short-lived proteins, as well as preventing accumulation of misfolded or damaged proteins. Alteration in ubiquitin-proteasome function may be detrimental to its crucial role in maintaining cellular homeostasis. Here, we have found that treatment of pyrrolidine dithiocarbamate (PDTC), a zinc ionophore, resulted in the accumulation of several proteasome substrates including p53 and p21 in HeLa cells. The PDTC effect was due to an extended half-life of these proteins through the mobilization of zinc. PDTC and/or zinc also increased fluorescence intensity of Ub(G76V)-GFP fusion protein that is degraded rapidly by the ubiquitin-proteasome system. Treatment of cells with zinc induced formation of ubiquitinated inclusions in the centrosome, a histological marker of proteasome inhibition. Western blotting showed zinc-induced increase in laddering bands of polyubiquitin-conjugated proteins. In vitro study, zinc inhibited the ubiquitin-independent proteasomal degradations of p21 and alpha-synuclein. These results suggest that zinc may modulate cell functions through its action on the turnover of proteins that are susceptible to proteasome-dependent proteolysis. ------>tmu_sno=None ------>sno=11510 ------>authors2=Kim CH ------>authors3=Kim JH ------>authors4=Lee J ------>authors5=Choi JJ ------>authors6=Chen ZA, Lee MG, Chung KC, Hsu CY, ------>authors6_c=None ------>authors=Kim I ------>delete_flag=0 ------>SCI_JNo=None ------>authors2_c=None ------>publish_area=None ------>updateTitle=Pyrrolidine dithiocarbamate and zinc inhibit proteasome-dependent proteolysis. ------>language=2 ------>check_flag=None ------>submit_date=None ------>country=None ------>no=1 ------>patent_SDate=None ------>update_bywho=None ------>publish_year=2004 ------>submit_flag=None ------>publish_month=None |