Increased spermine oxidase (SMO) activity as a novel differentiation marker of myogenic C2C12 cells
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- 作者：Manuela Cervelli ; Emiliano Fratini ; Roberto Amendola ; Marzia Bianchi ; Emanuela Signori ; Elisabetta Ferraro ; Antonella Lisi ; Rodolfo Federico ; Lucia Marcocci ; Paolo Mariottini
- 关键词：Polyamines ; Spermine oxidase ; C2C12 muscle cells ; Cell differentiation
- 刊名：The International Journal of Biochemistry and Cell Biology
- 出版年：2009
- 出版时间：April 2009
- 年：2009
- 卷：41
- 期：4
- 页码：934-944
- 全文大小：2142 K
文摘
Spermine oxidase (SMO) is a FAD-containing enzyme involved in animal cell polyamines (PA) homeostasis, selectively active on spermine and producing H2O2, 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 SMOα and SMOμ splice variants is not involved in the differentiation processes. Nuclear localization of only the SMOμ protein was confirmed.