|
|
||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
B activation, I
B-
degradation, and proteasome activity in neutrophils
1 Medicine, University of Alabama at Birmingham, Birmingham, Alabama, United States
* To whom correspondence should be addressed. E-mail: eabraham{at}uab.edu.
Although reactive oxygen species can participate in modulating the activity of the transcriptional factor NF-
B and expression of NF-
B dependent genes, the mechanisms involved and the roles of specific reactive oxygen species have not been fully determined. In particular, individual reactive oxygen species appear to have differing effects on NF-
B activation dependent on the cell population studied. In the present studies, we examined the ability of hydrogen peroxide (H2O2) to affect NF-
B activation in LPS stimulated murine neutrophils and macrophages. Exposure of bone marrow or peritoneal neutrophils to H2O2 was associated with reduced nuclear translocation of NF-
B and decreased production of the NF-
B dependent cytokines, TNF-
and MIP-2. H2O2 treatment resulted in diminished trypsin- and chymotrypsin-like proteasome activity. The degradation of I
B-
normally found in LPS-treated neutrophils was prevented when H2O2 was added to cell cultures. In contrast to the effects found in neutrophils, H2O2 did not affect chymotrypsin-like proteasomal activity or cytokine production in LPS-stimulated macrophages, even though trypsin-like proteasomal activity was reduced. These results demonstrate that the effects of H2O2 on NF-
B and proteasomal activity are cell population specific.
This article has been cited by other articles:
![]() |
J. W. Zmijewski, S. Banerjee, and E. Abraham S-Glutathionylation of the Rpn2 Regulatory Subunit Inhibits 26 S Proteasomal Function J. Biol. Chem., August 14, 2009; 284(33): 22213 - 22221. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Lorne, X. Zhao, J. W. Zmijewski, G. Liu, Y.-J. Park, Y. Tsuruta, and E. Abraham Participation of Mammalian Target of Rapamycin Complex 1 in Toll-Like Receptor 2- and 4-Induced Neutrophil Activation and Acute Lung Injury Am. J. Respir. Cell Mol. Biol., August 1, 2009; 41(2): 237 - 245. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. W. Zmijewski, E. Lorne, X. Zhao, Y. Tsuruta, Y. Sha, G. Liu, and E. Abraham Antiinflammatory Effects of Hydrogen Peroxide in Neutrophil Activation and Acute Lung Injury Am. J. Respir. Crit. Care Med., April 15, 2009; 179(8): 694 - 704. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. W. Zmijewski, E. Lorne, S. Banerjee, and E. Abraham Participation of mitochondrial respiratory complex III in neutrophil activation and lung injury Am J Physiol Lung Cell Mol Physiol, April 1, 2009; 296(4): L624 - L634. [Abstract] [Full Text] [PDF] |
||||
![]() |
X. Zhao, J. W. Zmijewski, E. Lorne, G. Liu, Y.-J. Park, Y. Tsuruta, and E. Abraham Activation of AMPK attenuates neutrophil proinflammatory activity and decreases the severity of acute lung injury Am J Physiol Lung Cell Mol Physiol, September 1, 2008; 295(3): L497 - L504. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. W. Zmijewski, E. Lorne, X. Zhao, Y. Tsuruta, Y. Sha, G. Liu, G. P. Siegal, and E. Abraham Mitochondrial Respiratory Complex I Regulates Neutrophil Activation and Severity of Lung Injury Am. J. Respir. Crit. Care Med., July 15, 2008; 178(2): 168 - 179. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Lorne, J. W. Zmijewski, X. Zhao, G. Liu, Y. Tsuruta, Y.-J. Park, H. Dupont, and E. Abraham Role of extracellular superoxide in neutrophil activation: interactions between xanthine oxidase and TLR4 induce proinflammatory cytokine production Am J Physiol Cell Physiol, April 1, 2008; 294(4): C985 - C993. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| Visit Other APS Journals Online |