Reference : Expression of 25 kDa thiamine triphosphatase in rodent tissues using quantitative PCR an...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/4628
Expression of 25 kDa thiamine triphosphatase in rodent tissues using quantitative PCR and characterization of its mRNA
English
Lakaye, Bernard mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique >]
Verlaet, Myriam mailto [Université de Liège - ULg > Services généraux (Faculté de médecine) > Service administratif de la Faculté (Médecine) >]
Dubail, Johanne [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Protéines et glycoprot. de matr.extracell. et membran.basal. >]
Czerniecki, Jan [Université de Liège - ULg > > Biochimie et physiologie humaine et pathologique >]
Bontems, Sébastien mailto [Université de Liège - ULg > > Virologie - Immunologie >]
Makarchikov, Alexander F [> > > >]
Wins, Pierre [> > > >]
Piette, Jacques mailto [Université de Liège - ULg > Département des sciences de la vie > Virologie - Immunologie >]
Grisar, Thierry mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique]
Bettendorff, Lucien mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique >]
2004
International Journal of Biochemistry & Cell Biology
Pergamon-Elsevier Science Ltd
36
10
2032-2041
Yes (verified by ORBi)
International
1357-2725
Oxford
[en] thiamine triphosphate ; thiamine triphosphatase ; quantitative PCR ; post-transcriptional control ; testis
[en] Thiamine triphosphate (ThTP) is found in most organisms, but its biological role remains unclear. In mammalian tissues, cellular ThTP concentrations remain low, probably because of hydrolysis by a specific 25 kDa thiamine triphosphatase (ThTPase). The aim of the present study was to use quantitative PCR, for comparing the 25 kDa ThTPase mRNA expression in various mouse tissues with its enzyme activities. ThTPase mRNA was expressed at only a few copies per cell. The highest amount of mRNA was found in testis, followed by lung and muscle, while the highest enzyme activities were found in liver and kidney. The poor correlation between mRNA levels and enzyme activities might result either from tissue-specific post-transcriptional regulation of mRNA processing and/or translation or from the regulation of enzyme activities by post-translational mechanisms. Purified recombinant human ThTPase was phosphorylated by casein kinase 11, but this phosphorylation did not modify the enzyme activity. However, the characterization of the 3'-untranslated mRNA region revealed a unique, highly conserved, 200-nucleotide sequence that might be involved in translational control. In situ hybridization studies in testis suggest a predominant localization of ThTPase mRNA in poorly differentiated spermatogenic cells. This is the first study demonstrating a cell-specific 25 kDa ThTPase mRNA expression, suggesting that this enzyme might be related to the degree of differentiation or the metabolic state of the cell. (C) 2004 Elsevier Ltd. All rights reserved.
http://hdl.handle.net/2268/4628
10.1016/j.biocel.2004.03.004

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