Thyroid hormone effect on rat heart mitochondrial proteins and affinity labeling with N‐bromoacetyl‐3,3′,5‐triiodo‐L‐thyronine Lack of direct effect on the adenine nucleotide translocase

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Abstract
N‐bromoacetyl‐3,3′,5‐tri[3′‐125I]iodo‐L‐thyronine was used to label intact heart mitochondria from eu‐, hypo‐ and hyperthyroid rats in order to identify proteins involved in T3‐regulated mitochondrial processes. The results show strong labeling, competed for by T3 and other analogues, of two proteins with a molecular mass of 48 000 and 49 200 Da. No labeling is seen of the adenine nucleotide translocase, a likely target, neither at 0°C, at room temperature, nor after preincubation with the substrates or specific inhibitors. No difference in labeling intensity or distribution is seen in mitochondria from eu‐, hypo‐ or hyperthyroid rats, and the abundance of the adenine nucleotide translocase is unchanged, but five other proteins show differential abundance.

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