Abstract
The phosphorylation state of P42, the phosphorylated, catalytically inactive, α-subunit of pyruvate dehydrogenase (PDH), decreased markedly (42.4%) in response to K +-depolarization of synaptosomes. The dephosphorylation was rapid (5–15 s), calcium-dependent and could also be observed in isolated mitochondria exposed to a rise in extramitochondrial calcium, suggesting that P42 dephosphorylation may act as a calcium sensor in the mitochondrial matrix. The depolarization-dependent dephosphorylation rate of P42 was decreased in synaptosomes derived from 24-month-old animals with respect to 3-month-old adults. The relevance of these results in terms of PDH activation during ageing is discussed.
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