Investigation of the mechanism by which glucose analogues cause translocation of glucokinase in hepatocytes: evidence for two glucose binding sites.

@article{Agius2000InvestigationOT,
  title={Investigation of the mechanism by which glucose analogues cause translocation of glucokinase in hepatocytes: evidence for two glucose binding sites.},
  author={L. Agius and M. Stubbs},
  journal={The Biochemical journal},
  year={2000},
  volume={346 Pt 2},
  pages={
          413-21
        }
}
  • L. Agius, M. Stubbs
  • Published 2000
  • Medicine, Biology
  • The Biochemical journal
  • Glucokinase translocates between the cytoplasm and nucleus of hepatocytes where it is bound to a 68 kDa protein. The mechanism by which glucose induces translocation of glucokinase from the nucleus was investigated using glucose analogues that are not phosphorylated by glucokinase. There was strong synergism on glucokinase translocation between effects of glucose analogues (glucosamine, 5-thioglucose, mannoheptulose) and sorbitol, a precursor of fructose 1-phosphate. In the absence of glucose… CONTINUE READING
    Glucokinase and molecular aspects of liver glycogen metabolism.
    • 281
    • PDF
    Stimulation of hepatocyte glucose metabolism by novel small molecule glucokinase activators.
    • 129
    • PDF
    Glucose 6-phosphate regulates hepatic glycogenolysis through inactivation of phosphorylase.
    • 56
    • PDF
    Subcellular localization, mobility, and kinetic activity of glucokinase in glucose-responsive insulin-secreting cells.
    • 44
    • PDF
    Treatment of type 2 diabetes by adenoviral-mediated overexpression of the glucokinase regulatory protein.
    • 62
    • PDF