Computer modeling identifies glucokinase as glucose sensor of pancreatic beta-cells.
Previous work from this laboratory indicates that glucokinase serves as the glucose sensor of pancreatic islets. Here we show by nonlinear computer optimization that the kinetic properties of glucokinase (together with hexokinase, known to be present in islets) account for the observed glycolytic rates in islets as a function of glucose level. Alternative enzymes that have been suggested to perform the same function as glucokinase, N-acetyl-D-glucosamine kinase and glucose-6-phosphatase, are shown to have incompatible properties, including a poor fit, different curve shapes, and unreasonable parameter values resulting from optimization. Their activities in islets are shown to be too low to account for observed glucose usage rates. This work endorses our previous proposal that glucokinase acts as the glucose sensor in pancreatic islet cells.
D001786:Blood Glucose / Q000502:physiology*; D005941:Glucokinase / Q000302:isolation & purification / Q000502:physiology*; D005947:Glucose / Q000378:metabolism; D005952:Glucose-6-Phosphatase / Q000502:physiology; D007515:Islets of Langerhans / Q000378:metabolism / Q000502:physiology*; D008358:Mannose / Q000378:metabolism; D008954:Models, Biological; D010770:Phosphotransferases / Q000502:physiology; D017853:Phosphotransferases (Alcohol Group Acceptor)
D001786:Blood Glucose; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); D005941:Glucokinase; C018716:N-acetylglucosamine kinase; D005952:Glucose-6-Phosphatase; D005947:Glucose; D008358:Mannose