Abstract
Objective:
To investigate the effects of AICAR on the activity of transcription factor FOXO1 and expression of ubiquitin ligase MuRF1 in rat cardiomyocytes, and explore the possible role of AMP-activated protein kinase (AMPK) in proteolysis pathways.
Methods:
In vitro cultured neonatal rat cardiac myocytes were treated with AICAR, and Western blotting was used to detect the phosphorylation of FOXO1 and expression of MuRF1 in the cells.
Results:
AICAR activated AMPK in rat cardiac myocytes. Activated AMPK significantly inhibited the phosphorylation of FOXO1 and increased MuRF1 protein expression.
Conclusion:
AMPK may regulate proteolysis by activating FOXO1 transcription factor and up-regulating MuRF1 expression.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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AMP-Activated Protein Kinases / metabolism*
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Aminoimidazole Carboxamide / analogs & derivatives
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Aminoimidazole Carboxamide / pharmacology
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Animals
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Cells, Cultured
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Forkhead Transcription Factors / metabolism*
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Muscle Proteins / metabolism*
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Myocytes, Cardiac / metabolism*
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Nerve Tissue Proteins / metabolism*
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Rats
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Rats, Sprague-Dawley
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Ribonucleotides / pharmacology
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Tripartite Motif Proteins
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Ubiquitin-Protein Ligases / metabolism*
Substances
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Forkhead Transcription Factors
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Muscle Proteins
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Nerve Tissue Proteins
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Ribonucleotides
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Tripartite Motif Proteins
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Foxo1 protein, rat
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Aminoimidazole Carboxamide
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Trim63 protein, rat
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Ubiquitin-Protein Ligases
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AMP-Activated Protein Kinases
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AICA ribonucleotide