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Biochem Biophys Res Commun. 2007 May 18;356(4):872-9. Epub 2007 Mar 19.

The prelamin A pre-peptide induces cardiac and skeletal myoblast differentiation.

Author information

1
Division of Medical Oncology, Department of Medicine, University of Colorado at Denver and Health Sciences Center, Denver, CO 80262, USA. Gary.Brodsky@uchsc.edu

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.

PMID:
17389141
DOI:
10.1016/j.bbrc.2007.03.062
[Indexed for MEDLINE]

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