1994
DOI: 10.1042/bj2980237
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Control of glucokinase translocation in rat hepatocytes by sorbitol and the cytosolic redox state

Abstract: In rat hepatocytes cultured in 5 (A50 550,uM). These substrates also stimulate glucose conversion into glycogen with a similar relative potency, suggesting that conversion of glucose into glycogen is dependent on the binding and/or location of glucokinase within the hepatocyte. Ethanol and glycerol inhibited the effects of fructose, sorbitol and glucose on glucokinase translocation, whereas dihydroxyacetone had a small additive effect at sub-maximal substrate stimulation. The converse effects of glycerol an… Show more

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Cited by 59 publications
(80 citation statements)
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“…Bar (31) tagatose and D-psicose increase liver glycogen deposition and liver weight remain unknown. However, the following pathway is supported by the results of many studies (34)(35)(36). Three ketohexoses appear to stimulate the formation of glycogen from glucose.…”
Section: Discussionsupporting
confidence: 57%
See 1 more Smart Citation
“…Bar (31) tagatose and D-psicose increase liver glycogen deposition and liver weight remain unknown. However, the following pathway is supported by the results of many studies (34)(35)(36). Three ketohexoses appear to stimulate the formation of glycogen from glucose.…”
Section: Discussionsupporting
confidence: 57%
“…In the liver, glucokinase catalyzes the phosphorylation of glucose to glucose-6-phosphate. In experiments with isolated hepatocytes, D-fructose and D-tagatose were found to stimulate the glucokinase reaction at a concentration of 0.1 mM (35,36). The authors ascribed this enzyme activation either to D-fructose-1-phosphate (or D-tagatose-1-phosphate) acting on a glucokinase-regulatory protein complex (37,38).…”
Section: Discussionmentioning
confidence: 99%
“…However, the glucose effect on GK translocation could not be explained solely by increased F-1-P, since more translocation of GK was observed with the same concentration of F-1-P in the presence of an elevated concentration of glucose than in the presence of fructose or sorbitol, at a low concentration of glucose (41). The effect of inhibition of aldose reductase in the polyol pathway in which glucose is converted to F-1-P on GK translocation is controversial (1,41). In our in vivo studies, furthermore, hepatic F-1-P contents (nmol/g liver) were not increased during a hyperglycemic clamp (17 Ϯ 3) compared with that under the basal condition (15 Ϯ 4) in normal rats and were not different between 10-wk-old ZDF rats and the lean littermates (unpublished data).…”
Section: Discussionmentioning
confidence: 99%
“…The only known physiological activators of GK in liver are precursors of fructose 1-phosphate (fructose and sorbitol), which causes dissociation of GK from GKRP (20,34). To test the efficacy of GKA1 and GKA2 at stimulating glucose metabolism in hepatocytes, we compared their effects with sorbitol, which is taken up by hepatocytes more rapidly than fructose and is thereby more effective at stimulating glucose metabolism (20,34). As expected, sorbitol caused a concentration-dependent increase in free GK, glucose phosphorylation, glycolysis, and glycogen synthesis (Fig.…”
Section: Stimulation By Glucokinase Activatorsmentioning
confidence: 99%