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In vitro ischemia decreases histone H4K16 acetylation in neural cells
Author(s) -
Dmitriev Ruslan I.,
Papkovsky Dmitri B.
Publication year - 2015
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.2014.11.038
Subject(s) - acetylation , histone , histone h4 , microbiology and biotechnology , trichostatin a , mitochondrion , biochemistry , chemistry , biology , cytosol , histone deacetylase , gene , enzyme
Inhibitors of histone deacetylases are frequently used against ischemia‐induced injury, but the specific mechanisms of their action are poorly understood. Here, we report that following a 5–7‐h oxygen–glucose deprivation (OGD) acetylation of histone H4 at residue K16 (H4K16Ac) decreases by 40–80% in both PC12 cells and primary neurons. This effect can be reverted by treatment with trichostatin A, or by supplementation with acetyl‐CoA. A decrease in H4K16Ac levels can affect the expression of mitochondrial uncoupling protein 2 (UCP2), huntingtin‐interacting protein 1 (HIP1) and Notch‐pathway genes in a cell‐specific manner. Thus, H4K16 acetylation is important for responses to ischemia and cell energy stress, and depends on both cytosolic and mitochondrial acetyl‐CoA.