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Heat shock protein 70 inhibits the nuclear import of apoptosis‐inducing factor to avoid DNA fragmentation in TF‐1 cells during erythropoiesis
Author(s) -
Lui Julian Chun-Kin,
Kong Siu-Kai
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.11.082
Subject(s) - dna fragmentation , erythropoiesis , depolarization , microbiology and biotechnology , apoptosis , fragmentation (computing) , apoptosis inducing factor , hsp70 , dna damage , chemistry , cytosol , heat shock protein , mitochondrion , biology , caspase , programmed cell death , dna , biophysics , biochemistry , medicine , ecology , gene , anemia , enzyme
Loss of mitochondrial membrane potential (ΔΨ m ) and release of AIF (apoptosis‐inducing factor) from mitochondria are key steps in apoptosis. In TF‐1 model, ΔΨ m was depolarized with AIF release during erythroid development. Yet, no DNA fragmentation was observed. When ΔΨ m depolarization had been blocked, erythropoiesis was suppressed. Interestingly, heat shock protein 70 (Hsp70) was found transiently upregulated during depolarization and it retained AIF in the cytosol to avoid DNA damages. When Hsp inhibitor was added, DNA fragmentation occurred. We show this mechanism for the first time in erythropoiesis how cells with ΔΨ m depolarization and AIF release escape apoptosis.