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- W2885771444 abstract "Background— Calcineurin (CnA) is important in the regulation of myocardial hypertrophy. We demonstrated that targeted proteolysis of the CnA autoinhibitory domain under pathological myocardial workload leads to increased CnA activity in human myocardium. Here, we investigated the proteolytic mechanism leading to activation of CnA. Methods and Results— In patients with diseased myocardium, we found strong nuclear translocation of CnA. In contrast, in normal human myocardium, there was a cytosolic distribution of CnA. Stimulation of rat cardiomyocytes with angiotensin (Ang) II increased calpain activity significantly (433±11%; P<0.01; n=6) and caused proteolysis of the autoinhibitory domain of CnA. Inhibition of calpain by a membrane-permeable calpain inhibitor prevented proteolysis. We identified the cleavage site of calpain in the human CnA sequence at amino acid 424. CnA activity was increased after Ang II stimulation (310±29%; P<0.01; n=6) and remained high after removal of Ang II (214±17%; P<0.01; n=6)..." @default.
- W2885771444 created "2018-08-22" @default.
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- W2885771444 date "2005-03-01" @default.
- W2885771444 modified "2023-09-24" @default.
- W2885771444 title "Targeted Proteolysis Sustains Calcineurin Activation" @default.
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