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(Received for publication, November 25, 1996, and in revised form, January 28, 1997)
From the A key event leading to exocytosis of pancreatic
acinar cell zymogen granules is the inositol 1,4,5-trisphosphate
(InsP3)-mediated release of Ca2+ from
intracellular stores. Studies using digital imaging microscopy and
laser-scanning confocal microscopy have indicated that the initial
release of Ca2+ is localized to the apical region of the
acinar cell, an area of the cell dominated by secretory granules.
Moreover, a recent study has shown that InsP3 is capable of
releasing Ca2+ from a preparation enriched in secretory
granules (Gerasimenko, O., Gerasimenko, J., Belan, P., and Petersen, O. H., (1996) Cell 84, 473-480). In the present study, we
have investigated the possibility that zymogen granules express
InsP3 receptors and are thus Ca2+ release
sites. Immunofluorescence staining, obtained with antisera specific to
types I, II, or III InsP3 receptors and analyzed by confocal fluorescence microscopy revealed that all InsP3
receptor types were present in acinar cells. The type II receptor
localized exclusively to an area close to or at the luminal plasma
membrane. While types I and III InsP3 receptors displayed a
similar luminal distribution, these receptors were also present at low
levels in nuclei. The localization of InsP3 receptor was in
marked contrast to the distribution of amylase, a zymogen granule
content protein. In a zymogen granule fraction prepared in an identical
manner to the aforementioned report demonstrating
InsP3-induced Ca2+ release, immunoblotting
demonstrated the presence of types I, II, and III InsP3
receptors. Ca2+ release from this preparation in response
to InsP3, but not thapsigargin, could also be demonstrated.
In contrast, when the zymogen granules were further purified on a
Percoll gradient, InsP3 receptors were undetectable, and
InsP3 failed to release Ca2+. Transmission
electron microscopy performed on both preparations showed that the
Percoll-purified granule preparation consisted of essentially pure
zymogen granules, whereas the granules prepared without this step were
enriched in granules but also contained significant contamination by
mitochondria, endoplasmic reticulum, and nuclei. It is concluded that
zymogen granules do not express InsP3 receptors and thus
are not a site of Ca2+ release relevant to the secretory
process in the pancreatic acinar cell.
Volume 272, Number 14,
Issue of April 4, 1997
pp. 9093-9098
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
DEFINING THE DISTRIBUTION OF INOSITOL 1,4,5-TRISPHOSPHATE
RECEPTORS IN PANCREATIC ACINAR CELLS
,
and
Departments of Physiology and ¶ Anatomy
and Cell Biology, University of Michigan Medical School, Ann Arbor,
Michigan 48109 and the 
Department of Pharmacology, State
University of New York Health Science Center at Syracuse, Syracuse, New
York 13210
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