AJP - GI Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Gastrointest Liver Physiol 253: G711-G719, 1987;
0193-1857/87 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by De Lisle, R. C.
Right arrow Articles by Williams, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by De Lisle, R. C.
Right arrow Articles by Williams, J. A.

AJP - Gastrointestinal and Liver Physiology, Vol 253, Issue 6 711-G719, Copyright © 1987 by American Physiological Society


ARTICLES

Zymogen granule acidity is not required for stimulated pancreatic protein secretion

R. C. De Lisle and J. A. Williams
Cell Biology Laboratory, Mount Zion Hospital, San Francisco, California 94120-7921.

It has been demonstrated recently by acridine orange fluorescence that pancreatic zymogen granules are acidic in situ, with respect to the cytoplasm. To evaluate the relationship between the acidic intragranular pH and hormone-stimulated secretion, mouse pancreatic acini were treated with lysosomotropic agents to collapse the zymogen granule pH gradient. Methylamine, monensin, and chloroquine collapsed the granule pH gradient as evidenced by a disappearance of acridine orange fluorescence. Cholecystokinin octapeptide (CCK-8)-stimulated acinar amylase secretion was unaffected in the presence of up to 30 mM methylamine and slightly enhanced in the presence of 0.3-10 microM monensin or 3-300 microM chloroquine. Acini were also preincubated for 15 min before addition of either CCK-8 or bombesin with concentrations of the lysosomotropic agents that dissipated the granule acridine orange fluorescence within this time. With preincubation, basal amylase release was unaffected, while stimulated secretion was slightly enhanced by all three lysosomotropic agents. Monensin and methylamine caused vacuolization of Golgi and lysosomal membranes and inhibition of intracellular transport of newly synthesized proteins. Chloroquine affected lysosomes similarly but had little effect on Golgi membranes or on intracellular protein transport. We also demonstrate that parotid secretory granules are acidic in situ by the acridine orange technique. Thus acidified secretory granules may be a general feature of exocrine secretory granules, but the acid pH is not requisite for the final steps in protein secretion from isolated pancreatic acini.


This article has been cited by other articles:


Home page
Am. J. Physiol. Cell Physiol.Home page
F. Thevenod
Ion channels in secretory granules of the pancreas and their role in exocytosis and release of secretory proteins
Am J Physiol Cell Physiol, September 1, 2002; 283(3): C651 - C672.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. E. Sorensen and I. Novak
Visualization of ATP Release in Pancreatic Acini in Response to Cholinergic Stimulus. USE OF FLUORESCENT PROBES AND CONFOCAL MICROSCOPY
J. Biol. Chem., August 24, 2001; 276(35): 32925 - 32932.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online