AJP - Lung Watch the video to learn how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Lung Cell Mol Physiol 281: L969-L981, 2001;
1040-0605/01 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
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 ISI Web of Science (4)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Audi, S. H.
Right arrow Articles by Roerig, D. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Audi, S. H.
Right arrow Articles by Roerig, D. L.
Vol. 281, Issue 4, L969-L981, October 2001

Oxygen dependency of monoamine oxidase activity in the intact lung

Said H. Audi1,2, Christopher A. Dawson1,3,4,5, Susan B. Ahlf5, and David L. Roerig4,5

1 Department of Biomedical Engineering, Marquette University, Milwaukee 53201-1881; 2 Department of Pulmonary and Critical Care Medicine, 3 Department of Physiology, and 4 Departments of Anesthesiology and Pharmacology/Toxicology, Medical College of Wisconsin, Milwaukee 53226; and 5 Zablocki Veterans Affairs Medical Center, Department of Veterans Affairs, Milwaukee, Wisconsin 53295-1000

Hydrogen peroxide generated by monoamine oxidase (MAO)-mediated deamination of biogenic amines has been implicated in cell signaling and oxidative injury. Because the pulmonary endothelium is a site of metabolism of monoamines present in the venous return, this brings into question a role for MAO in hyperoxic lung injury. The objective of this study was to evaluate the O2 dependency of the MAO reaction in the lung. To this end, we measured the pulmonary venous effluent concentrations of the MAO substrate [14C]phenylethylamine and its metabolite [14C]phenylacetic acid after the bolus injection of either phenylethylamine or phenylacetic acid into the pulmonary artery of perfused rabbit lungs over a range of PO2 values from 16 to 518 Torr. The apparent Michaelis constant for O2 was ~18 µM, which is more than an order of magnitude less that measured for purified MAO. The results suggest a minimal influence of high O2 on MAO activity in the normal lung and demonstrate the importance of measuring reaction kinetics in the intact organ.

multiple indicator dilution; mathematical modeling; endothelial cells; pargyline; semicarbazide


This article has been cited by other articles:


Home page
 J. Appl. Physiol.Home page
S. H. Audi, M. P. Merker, G. S. Krenz, T. Ahuja, D. L. Roerig, and R. D. Bongard
Coenzyme Q1 redox metabolism during passage through the rat pulmonary circulation and the effect of hyperoxia
J Appl Physiol, October 1, 2008; 105(4): 1114 - 1126.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
S. H. Audi, R. D. Bongard, G. S. Krenz, D. A. Rickaby, S. T. Haworth, J. Eisenhauer, D. L. Roerig, and M. P. Merker
Effect of chronic hyperoxic exposure on duroquinone reduction in adult rat lungs
Am J Physiol Lung Cell Mol Physiol, November 1, 2005; 289(5): L788 - L797.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
S. H. Audi, R. D. Bongard, C. A. Dawson, D. Siegel, D. L. Roerig, and M. P. Merker
Duroquinone reduction during passage through the pulmonary circulation
Am J Physiol Lung Cell Mol Physiol, November 1, 2003; 285(5): L1116 - L1131.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online