PMID- 22036635
OWN - NLM
STAT- MEDLINE
DCOM- 20120216
LR  - 20211020
IS  - 1873-5835 (Electronic)
IS  - 0145-2126 (Print)
IS  - 0145-2126 (Linking)
VI  - 36
IP  - 2
DP  - 2012 Feb
TI  - BCR-ABL1 kinase facilitates localization of acetylated histones 3 and 4 on DNA 
      double-strand breaks.
PG  - 241-4
LID - 10.1016/j.leukres.2011.10.007 [doi]
AB  - BCR-ABL1 kinase-positive leukemia cells accumulate high numbers of DNA 
      double-strand breaks (DSBs) induced by the reactive oxygen species (ROS) or 
      cytotoxic agents. To repair these lesions and prevent apoptosis BCR-ABL1 kinase 
      stimulates the efficiency of DSB repair in leukemia cells. Histone 
      acetylation-dependent chromatin re-modeling plays a crucial role in this process. 
      Here we report that leukemia cells expressing BCR-ABL1 kinase displayed an 
      enhanced histone acetylase activity (HAT) and reduced histone deacetylase 
      activity (HDAC), which was associated with abundant expression of acetylated 
      histones 3 and 4 (Ac-H3 and Ac-H4, respectively). Moreover, Ac-H3 and Ac-H4 
      readily co-localized with the spontaneous and mitomycin C-induced DSBs in 
      BCR-ABL1-positive leukemia cells suggesting that histone acetylation and 
      chromatin re-modeling is important for efficient repair of numerous DSBs.
CI  - Copyright (c) 2011 Elsevier Ltd. All rights reserved.
FAU - Falinski, Rafal
AU  - Falinski R
AD  - Department of Microbiology and Immunology, School of Medicine, Temple University, 
      Philadelphia, PA 19140, USA.
FAU - Nieborowska-Skorska, Margaret
AU  - Nieborowska-Skorska M
FAU - Skorski, Tomasz
AU  - Skorski T
LA  - eng
GR  - R01CA123014/CA/NCI NIH HHS/United States
GR  - R01 CA089052-04/CA/NCI NIH HHS/United States
GR  - R01 CA123014-04/CA/NCI NIH HHS/United States
GR  - R01CA089052/CA/NCI NIH HHS/United States
GR  - R01 CA089052/CA/NCI NIH HHS/United States
GR  - R01 CA089052-05/CA/NCI NIH HHS/United States
GR  - R01 CA123014/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20111028
PL  - England
TA  - Leuk Res
JT  - Leukemia research
JID - 7706787
RN  - 0 (Histones)
RN  - 0 (Reactive Oxygen Species)
RN  - 50SG953SK6 (Mitomycin)
RN  - EC 2.3.1.48 (Histone Acetyltransferases)
RN  - EC 2.7.10.2 (Fusion Proteins, bcr-abl)
RN  - EC 3.5.1.98 (Histone Deacetylases)
SB  - IM
MH  - Acetylation
MH  - Animals
MH  - Cells, Cultured
MH  - *Chromatin Assembly and Disassembly
MH  - *DNA Breaks, Double-Stranded
MH  - DNA Damage
MH  - DNA Repair
MH  - Fusion Proteins, bcr-abl/*metabolism
MH  - Hematopoietic Stem Cells
MH  - Histone Acetyltransferases/metabolism
MH  - Histone Deacetylases/metabolism
MH  - Histones/*metabolism
MH  - Humans
MH  - Leukemia, Myelogenous, Chronic, BCR-ABL Positive/genetics/*metabolism
MH  - Mice
MH  - Mitomycin/pharmacology
MH  - Reactive Oxygen Species/metabolism
PMC - PMC3249465
MID - NIHMS335752
COIS- The authors declare no conflict of interest.
EDAT- 2011/11/01 06:00
MHDA- 2012/02/18 06:00
PMCR- 2013/02/01
CRDT- 2011/11/01 06:00
PHST- 2011/07/27 00:00 [received]
PHST- 2011/09/28 00:00 [revised]
PHST- 2011/10/08 00:00 [accepted]
PHST- 2011/11/01 06:00 [entrez]
PHST- 2011/11/01 06:00 [pubmed]
PHST- 2012/02/18 06:00 [medline]
PHST- 2013/02/01 00:00 [pmc-release]
AID - S0145-2126(11)00504-2 [pii]
AID - 10.1016/j.leukres.2011.10.007 [doi]
PST - ppublish
SO  - Leuk Res. 2012 Feb;36(2):241-4. doi: 10.1016/j.leukres.2011.10.007. Epub 2011 Oct 
      28.