Am J Physiol Cell Physiol Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 257: C435-C441, 1989;
0363-6143/89 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Aw, T. Y.
Right arrow Articles by Jones, D. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Aw, T. Y.
Right arrow Articles by Jones, D. P.

AJP - Cell Physiology, Vol 257, Issue 3 C435-C441, Copyright © 1989 by American Physiological Society

ARTICLES

Cyanide toxicity in hepatocytes under aerobic and anaerobic conditions

T. Y. Aw and D. P. Jones
Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.

The effect of cyanide on cell viability and mitochondrial function was studied in hepatocytes exposed to air or argon. Cells were more susceptible to cyanide toxicity under air than under argon. Analysis of the disposition of cyanide showed that the difference in susceptibility to KCN was not due to O2-dependent differences in cyanide metabolism or elimination. Studies of mitochondrial function revealed that cyanide under aerobic conditions resulted in substantial swelling of the mitochondria, which corresponded to a matrix loading of phosphate. In addition, cyanide caused a loss of the mitochondrial protonmotive force. This was in contrast to the results for cells exposed to 30 min of anoxia alone in which there was no loss of mitochondrial delta pH, no detectable change in mitochondrial volume, and little matrix loading of phosphate. These results show that at least some of the protective mechanisms elicited by anoxia (B. S. Andersson, T. Y. Aw, and D. P. Jones. Am. J. Physiol. 252 (Cell Physiol. 21): C349-C355, 1987) are not elicited by cyanide alone. Thus cyanide under aerobic conditions does not provide a completely valid model for simple anoxia. Moreover, the results suggest that the molecular sensor necessary to signal suppression of metabolic and transport functions during neahypoxia is dependent on O2 and is neither stimulated nor antagonized by KCN.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Cell Physiol.Home page
V. Sridharan, J. Guichard, R. M. Bailey, H. Kasiganesan, C. Beeson, and G. L. Wright
The prolyl hydroxylase oxygen-sensing pathway is cytoprotective and allows maintenance of mitochondrial membrane potential during metabolic inhibition
Am J Physiol Cell Physiol, February 1, 2007; 292(2): C719 - C728.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
D. W. Killilea, R. Hester, R. Balczon, P. Babal, and M. N. Gillespie
Free radical production in hypoxic pulmonary artery smooth muscle cells
Am J Physiol Lung Cell Mol Physiol, August 1, 2000; 279(2): L408 - L412.
[Abstract] [Full Text] [PDF]

Home page
 J. Appl. Physiol.Home page
G. G. Haddad
Enhancing our understanding of the molecular responses to hypoxia in mammals using Drosophila melanogaster
J Appl Physiol, April 1, 2000; 88(4): 1481 - 1487.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. R. Samari and P. O. Seglen
Inhibition of Hepatocytic Autophagy by Adenosine, Aminoimidazole-4-carboxamide Riboside, and N6-Mercaptopurine Riboside. EVIDENCE FOR INVOLVEMENT OF AMP-ACTIVATED PROTEIN KINASE
J. Biol. Chem., September 11, 1998; 273(37): 23758 - 23763.
[Abstract] [Full Text] [PDF]


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