The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome
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- 作者：Sandra Reega ; Tobias Junga ; b ; José ; P. Castroa ; b ; Kelvin J.A. Daviesc ; Andrea Henzed ; Tilman Grunea ; b ; Scientific.director@dife.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：AMC ; 7-amino-4-methylcoumarin ; CL ; Cross-linker ; DNP ; Dinitrophenyl ; FRAP ; Fluorescence recovery after photobleaching ; GFP ; Green fluorescent protein ; Hsc70 ; Heat shock cognate protein 70 (also referred to as Hsp73) ; Hsp70 ; Heat shock protein 70 (also referred to as Hsp72 or Hsp70-1) ; IP ; Immunoprecipitate ; LC ; Lactacystin ; oxActin ; Oxidized actin ; PC ; Protein carbonyl ; Scr. ; Scrambled ; UF ; Unbound Fraction
- 刊名：Free Radical Biology and Medicine
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：99
- 期：Complete
- 页码：153-166
- 全文大小：1736 K
文摘
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Expression of Hsp70 is induced following oxidative stress.
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Hsp70 promotes overall proteolysis after oxidative stress and enhances proteasomal degradation of oxidized proteins.
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Hsp70 binds to oxidized proteins and possibly mediates their interaction with the 20 S proteasome.