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(Received for publication, June 23, 1995, and in revised form, April 2, 1996)
From the Adenine nucleotide metabolism was characterized
in intact insulin secreting HIT-T15 cells during the transition from
non-stimulated (i.e. 0.2 mM glucose) to the
glucose-stimulated secretory state. Metabolic dynamics were monitored
by assessing rates of appearance of 18O-labeled phosphoryls
of endogenous nucleotides in cells incubated in medium enriched in
[18O]water. Most prominent of the metabolic alterations
associated with stimulated insulin secretion was the suppression in the
rate of adenylate kinase (AK)-catalyzed phosphorylation of AMP by ATP.
This was manifest as a graded decrease of up to 50% in the rate of
appearance of
Volume 271, Number 28,
Issue of July 12, 1996
pp. 16544-16552
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
Department of Pharmacology,
Division
of Diabetes, Endocrinology, and Metabolism, Department of Medicine, and
'' Department of Biochemistry, University of Minnesota,
Minneapolis, Minnesota 55455
-18O-labeled species of ADP and ATP and
corresponded to the magnitude of the secretory response elicited over a
range of stimulatory glucose concentrations. The only nucleotide
exhibiting a significant concentration change associated with
suppression of AK activity was AMP, which decreased by about 50%,
irrespective of the glucose concentration. Leucine-stimulated secretion
also decreased the rate of AK-catalyzed phosphotransfer. This secretory
stimulus-related suppression of AK-catalyzed phosphotransfer occurs
within 45 s of glucose addition, precedes insulin secretion,
depends on the internalization and metabolism of glucose, and is
independent of membrane depolarization and the influx of extracellular
calcium. The secretory stimulus-induced decrease in AK-catalyzed
phosphotransfer, therefore occurs prior to or at the time of
K+ATP channel closure but it is not
associated with or a consequence of events occurring subsequent to
K+ATP channel closure. These results
indicate that AK-catalyzed phosphotransfer may be a determinant of ATP
to ADP conversion rates in the K+ATP
channel microenvironment; secretory stimuli-linked decreased
rates of AK-catalyzed ADP generation from ATP (and AMP) would translate
into an increased probability of ATP-liganded and, therefore, closed
state of the channel.
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