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J. Biol. Chem., Vol. 261, Issue 18, 8314-8319, 06, 1986
CB Wollheim and TJ Biden
The second messenger function of inositol 1,4,5-trisphosphate (Ins-
1,4,5-P3) was investigated in carbamylcholine-stimulated RINm5F cells by
analysis of the early changes in inositol phosphates, cytosolic free Ca2+
concentration ([Ca2+]i), and insulin secretion. After a lag of 2 s, [Ca2+]i
rose to a peak at 13 +/- 2 s, a response which was due mainly to
mobilization from intracellular stores since it persisted even in the
absence of extracellular Ca2+. The Ca2+ response had already declined
toward prestimulatory levels by the time insulin secretion reached its
maximal rate (2-3 min). Although the rises in inositol trisphosphate
preceded those of both inositol bisphosphate and monophosphate, all three
attained maximal concentrations after 1 min and remained elevated for at
least 10 min. The accumulation of inositol trisphosphate was truly
Ca2+-independent since it persisted under conditions in which the rise in
[Ca2+]i was abolished by prior depletion of intracellular Ca2+ pools.
Further analysis by high performance liquid chromatography revealed the
presence of the two isomers, Ins-1,4,5-P3 and Ins-1,3,4-P3 in stimulated
cells. The latter was virtually absent under nonstimulatory conditions but
started to accumulate after a 5-s lag and reached maximal levels after 30 s
of stimulation. Ins-1,4,5-P3 doubled within 1 s of carbamylcholine
addition, reached a peak after 5 s, and, although declining thereafter,
remained slightly elevated for at least 3 min. Hence, both the onset and
peak of the rise of Ins-1,4,5-P3 preceded that of [Ca2+]i, which in turn
preceded the peak in insulin release. These results strongly suggest that
Ins-1,4,5-P3 acts as the second messenger by which carbamylcholine
mobilizes intracellular Ca2+ during the initiation of insulin release.
Second messenger function of inositol 1,4,5-trisphosphate. Early changes in inositol phosphates, cytosolic Ca2+, and insulin release in carbamylcholine-stimulated RINm5F cells
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