l-Dopa decarboxylase expression profile in human cancer cells

l-Dopa decarboxylase (DDC) catalyses the decarboxylation of l-Dopa. It has been shown that the DDC gene undergoes alternative splicing within its 5′-untranslated region (UTR), in a tissue-specific manner, generating identical protein products. The employment of two alternative 5′UTRs is thought to b...

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Published in:Molecular biology reports Vol. 38; no. 2; pp. 1005 - 1011
Main Authors: Chalatsa, Ioanna, Nikolouzou, Eleftheria, Fragoulis, Emmanuel G, Vassilacopoulou, Dido
Format: Journal Article
Language:English
Published: Dordrecht Dordrecht : Springer Netherlands 01-02-2011
Springer Netherlands
Springer Nature B.V
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Summary:l-Dopa decarboxylase (DDC) catalyses the decarboxylation of l-Dopa. It has been shown that the DDC gene undergoes alternative splicing within its 5′-untranslated region (UTR), in a tissue-specific manner, generating identical protein products. The employment of two alternative 5′UTRs is thought to be responsible for tissue-specific expression of the human DDC mRNA. In this study, we focused on the investigation of the nature of the mRNA expression in human cell lines of neural and non-neural origin. Our results show the expression of a neural-type DDC mRNA splice variant, lacking exon 3 in all cell lines studied. Co-expression of the full length non-neural DDC mRNA and the neural-type DDC splice variant lacking exon 3 was detected in all cell lines. The alternative DDC protein isoform, Alt-DDC, was detected in SH-SY5Y and HeLa cells. Our findings suggest that the human DDC gene undergoes complex processing, leading to the formation of multiple mRNA isoforms. The study of the significance of this phenomenon of multiple DDC mRNA isoforms could provide us with new information leading to the elucidation of the complex biological pathways that the human enzyme is involved in.
Bibliography:http://dx.doi.org/10.1007/s11033-010-0196-x
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ISSN:0301-4851
1573-4978
DOI:10.1007/s11033-010-0196-x