PMID- 20370538
OWN - NLM
STAT- MEDLINE
DCOM- 20100617
LR  - 20240312
IS  - 1537-6524 (Electronic)
IS  - 1537-6516 (Print)
IS  - 1537-6516 (Linking)
VI  - 20
IP  - 5
DP  - 2010 Jun
TI  - Effects of butyltin exposures on MAP kinase-dependent transcription regulators in 
      human natural killer cells.
PG  - 227-33
LID - 10.3109/15376511003746034 [doi]
AB  - Natural killer (NK) cells are a major immune defense mechanism against cancer 
      development and viral infection. The butyltins (BTs), tributyltin (TBT) and 
      dibutyltin (DBT), have been widely used in industrial and other applications and 
      significantly contaminate the environment. Both TBT and DBT have been detected in 
      human blood. These compounds inhibit the lytic and binding function of human NK 
      cells and thus could increase the incidence of cancer and viral infections. 
      Butyltin (BT)-induced loss of NK function is accompanied by activation of mitogen 
      activated protein kinases (MAPKs) and decreases in expression of cell-surface and 
      cytolytic proteins. MAPKs activate components of the transcription regulator AP-1 
      and activate the transcription regulator Elk-1. Based on the fact that BTs 
      activate MAPKs and alter protein expression, the current study examined the 
      effect of BT exposures on the levels and phosphorylation states of the components 
      of AP-1 and the phosphorylation state of Elk-1. Exposure to 300 nM TBT for 10 min 
      increased the phosphorylation of c-Jun in NK cells. One hour exposures to 300 nM 
      and 200 nM TBT increased the phosphorylation and overall level of c-Jun. During a 
      300 nM treatment with TBT for 1 h the binding activity of AP-1 was significantly 
      decreased. There were no significant alterations of AP-1 components or of Elk-1 
      with DBT exposures. Thus, it appears that TBT-induced alterations on 
      phosphorylation, total levels, and binding activity of c-Jun might contribute to, 
      but are not fully responsible for, TBT-induced alterations of NK protein 
      expression.
FAU - Person, Rachel J
AU  - Person RJ
AD  - Department of Biological Sciences, Tennessee State University, Nashville, TN 
      37209, USA.
FAU - Whalen, Margaret M
AU  - Whalen MM
LA  - eng
GR  - S06 GM008092/GM/NIGMS NIH HHS/United States
GR  - S06 GM008092-34/GM/NIGMS NIH HHS/United States
GR  - 2S06GM-08092-34/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - England
TA  - Toxicol Mech Methods
JT  - Toxicology mechanisms and methods
JID - 101134521
RN  - 0 (Oncogene Proteins v-fos)
RN  - 0 (Organotin Compounds)
RN  - 0 (Proto-Oncogene Proteins c-jun)
RN  - 0 (Transcription Factor AP-1)
RN  - 0 (Trialkyltin Compounds)
RN  - 0 (ets-Domain Protein Elk-1)
RN  - 1002-53-5 (di-n-butyltin)
RN  - 4XDX163P3D (tributyltin)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
SB  - IM
MH  - Humans
MH  - Killer Cells, Natural/*drug effects/metabolism
MH  - Mitogen-Activated Protein Kinases/metabolism
MH  - Oncogene Proteins v-fos/metabolism
MH  - Organotin Compounds/*toxicity
MH  - Proto-Oncogene Proteins c-jun/metabolism
MH  - Transcription Factor AP-1/*metabolism
MH  - Trialkyltin Compounds/*toxicity
MH  - ets-Domain Protein Elk-1/*metabolism
PMC - PMC2874114
MID - NIHMS185054
EDAT- 2010/04/08 06:00
MHDA- 2010/06/18 06:00
PMCR- 2011/06/01
CRDT- 2010/04/08 06:00
PHST- 2010/04/08 06:00 [entrez]
PHST- 2010/04/08 06:00 [pubmed]
PHST- 2010/06/18 06:00 [medline]
PHST- 2011/06/01 00:00 [pmc-release]
AID - 10.3109/15376511003746034 [doi]
PST - ppublish
SO  - Toxicol Mech Methods. 2010 Jun;20(5):227-33. doi: 10.3109/15376511003746034.