Intramitochondrial protein synthesis is regulated by matrix adenine nucleotide content and requires calcium

Archives of Biochemistry and Biophysics
J L JoyalJ R Aprille

Abstract

The hypothesis that fluctuations in matrix adenine nucleotide content (ATP + ADP + AMP) may regulate intramitochondrial protein synthesis was investigated in newborn and adult rat liver mitochondria. Protein synthesis in mitochondria from 0-h-old newborns, which contain 3.4 +/- 0.3 nmol adenine nucleotide/mg protein, was > 90% lower than protein synthesis in mitochondria from 4-h-old newborns, which contain 9.1 +/- 0.2 nmol adenine nucleotide/mg protein. If 0-h newborn mitochondria were preincubated to accumulate adenine nucleotides to 16.8 nmol/mg protein in vitro, the protein synthesis rate increased 25-fold compared to control. Adult rat liver mitochondria normally contain 12-14 nmol adenine nucleotide/mg protein and exhibit a brisk rate of protein synthesis. Following a preincubation to deplete adenine nucleotides in vitro down to 3 nmol/mg protein, protein synthesis in adult liver mitochondria was nearly abolished. Conversely, when adult mitochondria were preincubated to superload adenine nucleotides (to 29 nmol/mg protein), the rate of protein synthesis was doubled. Protein synthesis was also inhibited when the matrix ATP/ADP ratio was lowered by adding FCCP or by omitting phosphate. In adult mitochondria, protein synthes...Continue Reading

Citations

May 20, 1998·Archives of Physiology and Biochemistry·J H Wani, V M Srivastava
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