| Literature DB >> 18852063 |
Manuela Cervelli1, Emiliano Fratini, Roberto Amendola, Marzia Bianchi, Emanuela Signori, Elisabetta Ferraro, Antonella Lisi, Rodolfo Federico, Lucia Marcocci, Paolo Mariottini.
Abstract
Spermine oxidase (SMO) is a FAD-containing enzyme involved in animal cell polyamines (PA) homeostasis, selectively active on spermine and producing H(2)O(2), spermidine, and the 3-aminopropanal. In the present study, we have examined the SMO gene expression during the mouse myoblast C2C12 cell differentiation induced with two different stimuli by RT-PCR analysis, polysome-mRNP distribution and enzyme activity. SMO transcript accumulation and enzymatic activity increases during C2C12 cell differentiation and correlates with the decrease of spermine content. Many proteins are highly regulated during the phenotypic conversion of rapidly dividing C2C12 myoblasts into fully differentiated post-mitotic myotubes. The SMO gene induction represents a novel and additional marker of C2C12 cell differentiation. The sub-cellular localization of the SMOalpha and SMOmu splice variants is not involved in the differentiation processes. Nuclear localization of only the SMOmu protein was confirmed.Entities:
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Year: 2008 PMID： 18852063 DOI： 10.1016/j.biocel.2008.09.009
Source DB: PubMed Journal: Int J Biochem Cell Biol ISSN： 1357-2725 Impact factor: 5.085