Inhibition of mitochondrial protein synthesis by phosphoenolpyruvate
| Autor: | G. David McCoy, Kenneth A. Doeg |
|---|---|
| Rok vydání: | 1972 |
| Předmět: |
Male
education Biophysics Mitochondria Liver In Vitro Techniques Mitochondrion Biology Cell Fractionation Biochemistry Acetone Phosphoenolpyruvate Adenine nucleotide Trioses Protein biosynthesis Animals Phosphoric Acids Glycolysis Glycosides Atractyloside Molecular Biology Carbon Isotopes Adenine Nucleotides Biological Transport Valine Cell Biology Molecular biology In vitro Rats Adenosine Diphosphate Kinetics Glycerophosphates Protein Biosynthesis cardiovascular system Phosphorylation Phosphoenolpyruvate carboxykinase Drug Antagonism circulatory and respiratory physiology |
| Zdroj: | Biochemical and Biophysical Research Communications. 46:1411-1417 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/s0006-291x(72)80133-5 |
| Popis: | Summary Phosphoenolpyruvate (PEP) has been found to inhibit the endogenous rate of in vitro protein synthesis and to increase significantly the amount of exogenous ADP required for maximum rates of in vitro protein synthesis in isolated rat liver mitochondria. This observed PEP inhibition can be blocked by the addition of atractyloside. Several other 3-carbon phosphorylated intermediates of glycolysis do not duplicate the PEP effect. Mitochondria whose adenine nucleotide pools have been pre-labeled with 14C-ADP show a rapid, atractyloside sensitive loss of radioactivity in the presence of PEP. These observations strongly suggest that the PEP inhibition of in vitro mitochondrial protein synthesis is due to stimulation of adenine nucleotide efflux via the atractyloside sensitive adenine nucleotide translocase system. |
| Databáze: | OpenAIRE |
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