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• W2006799477 abstract "Prelamin A processing is unique amongst mammalian proteins and results in the production of a farnesylated and carboxymethylated peptide. We examined the effect of pathogenic LMNA mutations on prelamin A processing, and of the covalently modified peptide on cardiac and skeletal myoblast differentiation. Here we report a mutation associated with dilated cardiomyopathy prevents prelamin A peptide production. In addition, topical application of the covalently modified C-terminal peptide to proliferating skeletal and cardiac myoblasts induced myotube and striated tissue formation, respectively. Western blot analysis revealed that skeletal and cardiac myoblasts are the first cell lines examined to contain unprocessed prelamin A, and immunostaining of peptide-treated cells revealed a previously unidentified role for prelamin A in cytoskeleton formation and intercellular organization. These results demonstrate a direct role for prelamin A in myoblast differentiation and indicate the prelamin A peptide may have therapeutic potential." @default.
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• W2006799477 date "2007-05-01" @default.
• W2006799477 modified "2023-09-27" @default.
• W2006799477 title "The prelamin A pre-peptide induces cardiac and skeletal myoblast differentiation" @default.
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• W2006799477 doi "https://doi.org/10.1016/j.bbrc.2007.03.062" @default.
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