Skip Navigation

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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Ueda, H.
Right arrow Articles by Kamada, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ueda, H.
Right arrow Articles by Kamada, T.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1988, Vol. 104, No. 1 81-86
© 1988 Japanese Biochemical Society


research-article

Changes in Aerobic and Anaerobic ATP-Synthesizing Activities in Hypoxic Mouse Brain1

Hirokazu Ueda*, Tadao Hashimoto*, Eisuke Furuya*, Kunio Tagawa*,2, Kazuo Kitagawa**, Masayasu Matsumoto**, Shotaro Yoneda**, Kazufumi Kimura** and Takenobu Kamada**

*Department of Physiological Chemistry, Osaka University Medical School Kita-ku, Osaka, Osaka 530
**First Department of Internal Medicine, Osaka University Medical School Kita-ku, Osaka, Osaka 530

1 To whom correspondence should be addressed

The changes in cerebral metabolism in mice in severe hypoxia were investigated by analyses of changes in the levels of energy metabolites and near-infrared spectro photometric assessment of the states of hemoglobin and cytochrome oxidase. Under 4.4% 02, the contribution of anaerobic ATP production was at most about 20% of the demand. However, the cerebral ATP level was kept at the control level until about 1 mm before death. Pentobarbital anesthesia, which reduced the cerebral rate of metabolism, prolonged the survival time, although anaerobic ATP production still did not support ATP demand. Under these conditions, deoxygenation of hemoglobin and reduction of cytochrome oxidase proceeded rapidly within 1 mm. Hemoglobin reached the maximum state of deoxygenation in the middle phase of hypoxia, with no further change until death. However, cytochrome oxidase was reduced slowly with one phase of partial reoxidation due to increase of cere bral blood volume, and reached the completely reduced state at death. From these results it was concluded that the aerobic ATP synthesis, which supplied more than 80% of the cerebral demand, decreased gradually because of limitation of oxygen supply, and that the failure of oxidative phosphorylation to meet demand triggered the decrease in the cellular ATP level that led to death.

This work was supported in part by Grants.in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Am. J. Physiol. Cell Physiol.Home page
Y. Bando, S. Ogawa, A. Yamauchi, K. Kuwabara, K. Ozawa, O. Hori, H. Yanagi, M. Tamatani, and M. Tohyama
150-kDa oxygen-regulated protein (ORP150) functions as a novel molecular chaperone in MDCK cells
Am J Physiol Cell Physiol, June 1, 2000; 278(6): C1172 - C1182.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Ozawa, K. Kuwabara, M. Tamatani, K. Takatsuji, Y. Tsukamoto, S. Kaneda, H. Yanagi, D. M. Stern, Y. Eguchi, Y. Tsujimoto, et al.
150-kDa Oxygen-regulated Protein (ORP150) Suppresses Hypoxia-induced Apoptotic Cell Death
J. Biol. Chem., March 5, 1999; 274(10): 6397 - 6404.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
A. Matsunaga, Y. Nomura, S. Kuroda, M. Tamura, J. Nishihira, and N. Yoshimura
Energy-dependent redox state of heme a + a3 and copper of cytochrome oxidase in perfused rat brain in situ
Am J Physiol Cell Physiol, October 1, 1998; 275(4): C1022 - C1030.
[Abstract] [Full Text] [PDF]


Home page
StrokeHome page
J.-Y. Li, H. Ueda, A. Seiyama, M. Nakano, M. Matsumoto, and T. Yanagihara
A Near-Infrared Spectroscopic Study of Cerebral Ischemia and Ischemic Tolerance in Gerbils
Stroke, July 1, 1997; 28(7): 1451 - 1457.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
S. Du Yan, Y. Zhu, E. D. Stern, Y. C. Hwang, O. Hori, S. Ogawa, M. P. Frosch, E. S. Connolly Jr., R. McTaggert, D. J. Pinsky, et al.
Amyloid beta -Peptide-binding Alcohol Dehydrogenase Is a Component of the Cellular Response to Nutritional Stress
J. Biol. Chem., August 25, 2000; 275(35): 27100 - 27109.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.