AI Article Synopsis
- The study focused on how phospholipids affect the secretion of amylase from rat pancreatic acinar AR42J cells when stimulated by cholecystokinin octapeptide (CCK-8).
- The inhibitor wortmannin was used to show that blocking phosphoinositide 3-kinase (PI3K) reduced amylase secretion in a dose-dependent way.
- CCK-8 stimulation caused a rapid increase in phosphatidic acid (PtdOH) levels in the cell membranes, a rise that was suppressed by wortmannin, indicating that PtdOH production is crucial for amylase secretion through PI3K pathways.
Article Abstract
To investigate the role of phospholipids in exocytotic secretory events, we utilized rat pancreatic acinar AR42J cells that secreted amylase in response to cholecystokinin octapeptide (CCK-8). Wortmannin, an inhibitor of phosphoinositide 3-kinase (PI3K), was found to inhibit the secretion in a dose-dependent manner. When changes in cell membrane phospholipids were investigated before and after CCK-8 stimulation using [32P]orthophosphoric acid-labeled AR42J cells, we observed a rapid increase in phosphatidic acid (PtdOH) levels right after stimulation, which was not observed in non-stimulated cells. The increase, however, was suppressed by wortmannin pre-treatment, which also inhibited amylase secretion. Changes in other major phospholipids were not significant. These results indicate that CCK-8 induces amylase secretion through PI3K-regulated production of PtdOH in cell membranes.
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| http://dx.doi.org/10.1016/s0006-291x(03)01078-7 | DOI Listing |
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