<p>This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</p> <p>Hepatic glucokinase (GK) is acutely regulated by
binding to its nuclear-anchored regulatory protein
(GKRP). Although GK release by GKRP is tightly
coupled to the rate of glycogen synthesis, the nature
of this association is obscure. To gain insight into
this coupling mechanism under physiological stimulating 
conditions in primary rat hepatocytes, we
analyzed the subcellular distribution of GK and
GKRP with immunofluorescence, and glycogen deposition
with glycogen cytochemical fluorescence,
using confocal microscopyand quantitative image
analysis. Following stimulation, a fraction of the GK
signal translocated from the nucleus to the cytoplasm.
The reduction in the nuclear to cytoplasmic
ratio of GK, an index of nuclear export, correlated
with a &gt;50% increase in glycogen cytochemical
fluorescence over a 60min stimulation period. Furthermore,
glycogen accumulation was initially deposited
in a peripheral pattern in hepatocytes
similar to that of GK. These data suggest that a compartmentalization
exists of both active GK and the
initial sites of glycogen deposition at the hepatocyte
surface.</p>
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Int J Exp Diabetes Res. 2001; 2(3):173-186