Hexose-6-phosphate dehydrogenase (H6PD) is the main NADPH generating enzyme in the lumen of the endoplasmic reticulum. H6PD is regarded as an ancillary enzyme in prereceptorial glucocorticoid activation and probably acts as a nutrient sensor and as a prosurvival factor. H6PD expression was determined in a variety of rat and human tissues by detecting mRNA and protein levels, and by measuring its dehydrogenase and lactonase activities. It was found that H6PD was present in all investigated tissues; both expression and activity remained within an order of magnitude. Correlation was found between the dehydrogenase activity and protein or mRNA levels. The results confirmed the supposed housekeeping feature of the enzyme.
Marcolongo, P., Senesi, S., Giunti, R., Csala, M., Fulceri, R., Banhegyi, G., et al. (2011). Expression of hexose-6-phosphate dehydrogenase in rat tissues. JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY, 126(3-5), 57-64 [10.1016/j.jsbmb.2011.05.006].
Expression of hexose-6-phosphate dehydrogenase in rat tissues
MARCOLONGO, P.;GIUNTI, R.;FULCERI, R.;BENEDETTI, A.
2011-01-01
Abstract
Hexose-6-phosphate dehydrogenase (H6PD) is the main NADPH generating enzyme in the lumen of the endoplasmic reticulum. H6PD is regarded as an ancillary enzyme in prereceptorial glucocorticoid activation and probably acts as a nutrient sensor and as a prosurvival factor. H6PD expression was determined in a variety of rat and human tissues by detecting mRNA and protein levels, and by measuring its dehydrogenase and lactonase activities. It was found that H6PD was present in all investigated tissues; both expression and activity remained within an order of magnitude. Correlation was found between the dehydrogenase activity and protein or mRNA levels. The results confirmed the supposed housekeeping feature of the enzyme.
| File | Dimensione | Formato | |
|---|---|---|---|
|
Marcolongo J Steroid Biochem 2011.pdf
non disponibili
Tipologia:
PDF editoriale
Licenza:
NON PUBBLICO - Accesso privato/ristretto
Dimensione
992.02 kB
Formato
Adobe PDF
|
992.02 kB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
https://hdl.handle.net/11365/20221
Attenzione
Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo