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J. Biol. Chem., Vol. 265, Issue 28, 16863-16866, Oct, 1990
Y Liang, H Najafi and FM Matschinsky
In this study, we have used isolated pancreatic islets cultured for 7 days
in 3 or 30 mM glucose to explore whether glucokinase is induced or
activated by high glucose concentrations and has related enzyme activity to
glucose-stimulated insulin release. Islets cultured in low glucose medium
or low glucose medium plus 350 ng/ml insulin did not respond to high
glucose stimulation. Islets cultured in medium containing high glucose
concentrations showed a high rate of basal insulin secretion when perifused
with 5 mM glucose, and the insulin release was greatly augmented in a
biphasic secretion profile when the glucose concentration was raised to 16
mM. Islet glucokinase and hexokinase activities were determined by a
sensitive and specific fluorometric method. Glucokinase activity was
reduced to approximately 50% in islets cultured in low glucose medium with
or without insulin present compared to results with fresh islets. However,
islets cultured in 30 mM glucose showed that glucokinase activity was
elevated to 236% compared to results with fresh islets. It is concluded
that (a) glucose is the physiological regulator of glucokinase in the islet
of Langerhans and that (b) the activity of glucokinase plays a crucial role
in glucose-induced insulin secretion.
Glucose regulates glucokinase activity in cultured islets from rat pancreas
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104.
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