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Involvement of eukaryotic translation initiation factor 5A (eIF5A) in skeletal muscle stem cell differentiation

✍ Scribed by Augusto D. Luchessi; Tavane D. Cambiaghi; Sandro M. Hirabara; Rafael H. Lambertucci; Leonardo R. Silveira; Igor L. Baptista; Anselmo S. Moriscot; Claudio M. Costa-Neto; Rui Curi


Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
373 KB
Volume
218
Category
Article
ISSN
0021-9541

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✦ Synopsis


Abstract

The eukaryotic translation initiation factor 5A (eIF5A) contains a special amino acid residue named hypusine that is required for its activity, being produced by a post‐translational modification using spermidine as substrate. Stem cells from rat skeletal muscles (satellite cells) were submitted to differentiation and an increase of eIF5A gene expression was observed. Higher content of eIF5A protein was found in satellite cells on differentiation in comparison to non‐differentiated satellite cells and skeletal muscle. The treatment with N1‐guanyl‐1,7‐diaminoheptane (GC7), a hypusination inhibitor, reversibly abolished the differentiation process. In association with the differentiation blockage, an increase of glucose consumption and lactate production and a decrease of glucose and palmitic acid oxidation were observed. A reduction in cell proliferation and protein synthesis was also observed. L‐Arginine, a spermidine precursor and partial suppressor of muscle dystrophic phenotype, partially abolished the GC7 inhibitory effect on satellite cell differentiation. These results reveal a new physiological role for eIF5A and contribute to elucidate the molecular mechanisms involved in muscle regeneration. J. Cell. Physiol. 218: 480–489, 2009. © 2008 Wiley‐Liss, Inc.


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## Abstract Eukaryotic translation initiation factor 5A (eIF5A) has a unique character: the presence of an unusual amino acid, hypusine, which is formed by post‐translational modifications. Even before the identification of hypusination in eIF5A, the correlation between hypusine formation and prote