J Physiol Society Membership
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


Physiology in Press

First published online on May 16, 2003.
Copyright © 2003 by The Physiological Society
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
550/2/447    most recent
2003.041525v1
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Morgan, D.
Right arrow Articles by DeCoursey, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Morgan, D.
Right arrow Articles by DeCoursey, T.

Received February 11, 2003
Accepted after revision April 23, 2003

Temperature dependence of nicotinamide adenine dinucleotide phosphate oxidase in human eosinophils

Deri Morgan1, Vladimir V. Cherny1, Ricardo Murphy1, Wei Xu2, Larry L. Thomas2, and T. DeCoursey3*

1 Department of Molecular Biophysics and Physiology, Rush Presbyterian St Luke's Medical Center, Chicago, IL 60612, USA
2 Department of Immunology/Microbiology, Rush Presbyterian St Luke's Medical Center, Chicago, IL 60612, USA
3 Department of Molecular Biophysics and Physiology, Rush Presbyterian St Luke's Medical Center, 1750 W. Harrison, Chicago, IL 60612, USA

* To whom correspondence should be addressed. E-mail: tdecours{at}rush.edu.

The phagocyte NADPH oxidase helps kill pathogens by producing superoxide anion, O2-. This enzyme is electrogenic because it translocates electrons across the membrane, generating an electron current, Ie. Using the permeabilized patch voltage-clamp technique, we studied the temperature dependence of Ie in human eosinophils stimulated by phorbol myristate acetate PMA, from room temperature to > 37°C. For comparison, NADPH oxidase activity was assessed by cytochrome c reduction. The intrinsic temperature dependence of the assembled, functioning NADPH oxidase complex measured during rapid temperature increases to 37°C was surprisingly weak: the Arrhenius activation energy Ea was only 14 kcal mol-1 (Q10, 2.2). In contrast, steady-state NADPH oxidase activity was strongly temperature dependent at 20-30°C, with Ea 25.1 kcal mol-1 (Q10, 4.2). The maximum Ie measured at 34°C was -30.5 pA. Above 30°C, the temperature dependence of both Ie and O2- production was less pronounced. Above 37°C, Ie was inhibited reversibly. After rapid temperature increases, a secondary increase in Ie ensued, suggesting that high temperature promotes assembly of additional NADPH oxidase complexes. Evidently, about twice as many NADPH oxidase complexes are active near 37°C than at 20°C. Thus, the higher Q10 of steady-state Ie reflects both increased activity of each NADPH oxidase complex and preferential assembly of NADPH oxidase complexes at high temperature. In summary, NADPH oxidase activity in intact human eosinophils is maximal precisely at 37°C.




This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
B. Musset, D. Morgan, V. V. Cherny, D. W. MacGlashan Jr, L. L. Thomas, E. Rios, and T. E. DeCoursey
A pH-stabilizing role of voltage-gated proton channels in IgE-mediated activation of human basophils
PNAS, August 5, 2008; 105(31): 11020 - 11025.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
B. Musset, V. V. Cherny, D. Morgan, Y. Okamura, I. S. Ramsey, D. E. Clapham, and T. E. DeCoursey
Detailed comparison of expressed and native voltage-gated proton channel currents
J. Physiol., May 15, 2008; 586(10): 2477 - 2486.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
D. Morgan, V. V. Cherny, A. Finnegan, J. Bollinger, M. H. Gelb, and T. E. DeCoursey
Sustained activation of proton channels and NADPH oxidase in human eosinophils and murine granulocytes requires PKC but not cPLA2{alpha} activity
J. Physiol., March 1, 2007; 579(2): 327 - 344.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
J. K. Femling, V. V. Cherny, D. Morgan, B. Rada, A. P. Davis, G. Czirjak, P. Enyedi, S. K. England, J. G. Moreland, E. Ligeti, et al.
The Antibacterial Activity of Human Neutrophils and Eosinophils Requires Proton Channels but Not BK Channels
J. Gen. Physiol., May 30, 2006; 127(6): 659 - 672.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
D. Morgan, V. V. Cherny, R. Murphy, B. Z. Katz, and T. E. DeCoursey
The pH dependence of NADPH oxidase in human eosinophils
J. Physiol., December 1, 2005; 569(2): 419 - 431.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
G. Obermeyer and S. D. Tyerman
NH4+ Currents across the Peribacteroid Membrane of Soybean. Macroscopic and Microscopic Properties, Inhibition by Mg2+, and Temperature Dependence Indicate a SubpicoSiemens Channel Finely Regulated by Divalent Cations
Plant Physiology, October 1, 2005; 139(2): 1015 - 1029.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
S. Arbogast and M. B. Reid
Oxidant activity in skeletal muscle fibers is influenced by temperature, CO2 level, and muscle-derived nitric oxide
Am J Physiol Regulatory Integrative Comp Physiol, October 1, 2004; 287(4): R698 - R705.
[Abstract] [Full Text] [PDF]


Home page
Sci SignalHome page
T. E. DeCoursey
During the Respiratory Burst, Do Phagocytes Need Proton Channels or Potassium Channels, or Both?
Sci. Signal., May 18, 2004; 2004(233): pe21 - pe21.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2003 The Physiological Society.