Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs.

Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs. Abstract Text:

F Watanabe,T Hashimoto,K Tagawa,

Preservation of the oxidative phosphorylation capacity of mitochondria by addition of ATP under anaerobic conditions was analyzed by use of non-metabolizable adenine nucleotide analogs. The capacity was well preserved in the presence of ATP and did not require the hydrolysis of ATP, since ATP analogs, such as beta, gamma-methylene adenosine triphosphate (AMPPCP), alpha, beta-methylene adenosine triphosphate (AMPCPP), and adenylyl imidodiphosphate (AMPPNP), were as effective as ATP. These analogs were incorporated into mitochondria through ATP/ADP translocase to maintain the original level of total adenine nucleotides in the mitochondria. ADP apparently had the same effect as ATP, but its effect was shown to be due to ATP generated from it by adenylate kinase in mitochondria. An analog of ADP, alpha, beta-methylene adenosine diphosphate (AMPCP), which was found to be a substrate of the translocase but not of adenylate kinase, could not replace ADP or ATP. From these results, it was concluded that the oxidative phosphorylation capacity of mitochondria was maintained by ATP, but not ADP, through a process not requiring energy.

Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs. Publishing Authors By Initials

F Watanabe,T Hashimoto,K Tagawa,

For similar animals: animal population groups: animals, inbred strains: rats, inbred strains research abstracts see: animals: animal population groups: animals, inbred strains: rats, inbred strains research

PUBMED ID PMID:

MEDLINE DATE:

Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 97

Page Numbers: 1229-34

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Apr

YEAR: 1985

Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs. Keywords Mesh Terms:

KEYWORDS: Rats, Inbred Strains

MESH TERMS: drug effects

Chemical & Substance for Abstract: Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs. Information

Substance Name: Adenosine Diphosphate

Registry Number: 58-64-0

Grant and Affiliation Information for Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs Related Publications

• 8-Epi-iridodial glucoside from Boschniakia rossica.
• A direct colorimetric method for the determination of phospholipids with dithiocyanatoiron reagent.
• A simple method for measuring phosphatidylcholine as its hydrophobic complex with tetrathiocyanatocobaltate.
• A stabilizing factor of yeast mitochondrial F1F0-ATPase-inhibitor complex: common amino acid sequence with yeast ATPase inhibitor and E. coli epsilon and bovine delta subunits.
• Amino acid sequence of an intrinsic inhibitor of mitochondrial ATPase from yeast.
• An immuno-light- and electron-microscopic study of the expression of bone morphogenetic protein-2 during the process of ectopic bone formation in the rat.
• Binding of intrinsic ATPase inhibitor to mitochondrial ATPase--stoichiometry of binding of nucleotides, inhibitor, and enzyme.
• Binding properties of 9K protein to F1-ATPase: a counterpart ligand to the ATPase inhibitor.
• Binding properties of an intrinsic ATPase inhibitor and occurrence in yeast mitochondria of a protein factor which stabilizes and facilitates the binding of the inhibitor to F1F0-ATPase.
• Botulinum toxin treatment for blepharospasm associated with myasthenia gravis.
• Cell-free synthesis of mitochondrial ATPase inhibitor precursor and its transport into yeast mitochondria.
• Change in P-450 content accompanying aerobic formation of mitochondria in yeast.
• Characterization of the development of ectopic chondroid/bone matrix and chondrogenic/osteogenic cells during osteoinduction by rhBMP-2: a histochemical and ultrastructural study.
• Decrease in mitochondrial levels of adenine nucleotides and concomitant mitochondrial dysfunction in ischemic rat liver.
• Development of mitochondrial membranes in anaerobically grown yeast cells.
• Energy-independent protection of the oxidative phosphorylation capacity of mitochondria against anoxic damage by ATP and its non-metabolizable analogs.
• Existence of stoichiometric amounts of an intrinsic ATPase inhibitor and two stabilizing factors with mitochondrial ATP synthase in yeast.
• Hepatic accumulation of pyrophosphate during acetate metabolism.
• Interaction of mitochondrial aspartate aminotransferase with negatively charged lecithin liposomes.
• Involvement of Ca2+ release and activation of phospholipase A2 in mitochondrial dysfunction during anoxia.
• Kinetics of hydroperoxide degradation by NADP-glutathione system in mitochondria.
• Localization of cytochrome c peroxidase in anaerobically grown yeast cells.
• Non-mitochondrial electron transfer system in anaerobically grown yeast cells.
• Partial amino terminal sequence of the precursor of mitochondrial ATPase inhibitor protein synthesized with mRNA partially purified by gel permeation chromatography.
• Properties of binding sites for adenine nucleotides on ATPase from yeast mitochondria.
• Purification and properties of factors in yeast mitochondria stabilizing the F1F0-ATPase-inhibitor complex.
• Simultaneous bindings of ATPase inhibitor and 9K protein to F1F0-ATPase in the presence of 15K protein in yeast mitochondria.
• [Hypertension in dialysis patients]
• [Hypotension in dialysis patients]
• pH-Induced conformational change of ATPase inhibitor from yeast mitochondria. A proton magnetic resonance study.