Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Joan J. Guinovart"'
Autor:
J.P. Pontigo, Juan C. Slebe, Ilona I. Concha, Romina Bertinat, Rody San Martín, Moisés Pérez, Alejandro J. Yáñez, Joan J. Guinovart
Publikováno v:
JOURNAL OF CELLULAR BIOCHEMISTRY
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
MOLECULAR AND CELLULAR BIOCHEMISTRY
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
MOLECULAR AND CELLULAR BIOCHEMISTRY
Using a streptozotocin-induced type 1 diabetic rat model, we analyzed and separated the effects of hyperglycemia and hyperinsulinemia over the in vivo expression and subcellular localization of hepatic fructose 1,6-bisphosphatase (FBPase) in the mult
Publikováno v:
Biochemical Journal. 351:811-816
We have used recombinant adenoviruses (AdCMV-RLGS and AdCMV-GK) to overexpress the liver isoforms of glycogen synthase (GS) and glucokinase (GK) in primary cultured rat hepatocytes. Glucose activated overexpressed GS in a dose-dependent manner and ca
The Role of the Regulatory Protein of Glucokinase in the Glucose Sensory Mechanism of the Hepatocyte
Publikováno v:
Journal of Biological Chemistry. 275:10597-10603
Glucokinase has a very high flux control coefficient (greater than unity) on glycogen synthesis from glucose in hepatocytes (Agius et al., J. Biol. Chem. 271, 30479-30486, 1996). Hepatic glucokinase is inhibited by a 68-kDa glucokinase regulatory pro
Publikováno v:
Journal of Biological Chemistry. 271:30479-30486
Glucokinase reversibly partitions between a bound and a free state in the hepatocyte in response to the metabolic status of the cell. Maximum binding occurs at low [glucose] (
Autor:
Monique Beullens, Bruno Guigas, Alexander von Wilamowitz-Moellendorff, Mark H. Rider, Kei Sakamoto, Liliane Maisin, Joan J. Guinovart, Louis Hue, Nusrat Hussain, Didier Vertommen, Marc Foretz, Benoit Viollet, Laurent Bultot
Publikováno v:
Biochemical Journal, 443, 193-203
Recombinant muscle GYS1 (glycogen synthase 1) and recombinant liver GYS2 were phosphorylated by recombinant AMPK (AMP-activated protein kinase) in a time-dependent manner and to a similar stoichiometry. The phosphorylation site in GYS2 was identified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1295ece1555a9a75f353f2bc5b0e93a
https://hdl.handle.net/1887/111301
https://hdl.handle.net/1887/111301
Publikováno v:
Biochemical Journal. 281:443-448
Incubation of rat hepatocytes with glucose results in a decrease in the amount of glycogen synthase activity found in supernatants obtained after centrifugation of cell homogenates at 9200 g. The enzymic activity was quantitatively recovered in the s
Publikováno v:
Scopus-Elsevier
In hepatocytes from starved streptozocin-induced diabetic rats, vanadate increases the glycolytic flux because it raises the levels of fructose-2,6-bisphosphate (Fru-2,6-P2), the main regulatory metabolite of this pathway. This effect of vanadate on
Publikováno v:
Archives of biochemistry and biophysics. 457(1)
Incubation of rat hepatocytes with LiCl resulted in an overall increase in the activity ratio of glycogen synthase (GS), concomitantly with a decrease in active GS kinase-3 levels. GS total activity was also increased in a dose- and time-dependent ma
Publikováno v:
Archives of biochemistry and biophysics. 300(2)
In rat hepatocytes fructose at low concentrations (below 1 mM) stimulated the glycolytic flux as measured by the release of 3H2O from [3-3H]glucose and increased fructose 2,6-bisphosphate [Fru(2,6)P2] levels, without modifying the activity of 6-phosp
Publikováno v:
Scopus-Elsevier
Universitat Autònoma de Barcelona
Universitat Autònoma de Barcelona
Vanadate inactivated rat hepatocyte glycogen synthase and activated glycogen phosphorylase in a dose- and time-dependent manner. These effects were observed in hepatocytes from both fasted as well as fed rats. When rat hepatocytes were preincubated w