Sources
Help build the largest human-edited directory on the web.
Submit a site - Become an editor
Wikipedia. Licensed under the GNU Free Documentation License.
Are you an expert in this subject? Join the discussion and share your knowledge at Wikipedia.org.
Exocrine pancreas
From Wikipedia, the free encyclopedia
The exocrine pancreas has ducts which are arranged in clusters called acini (singular acinus). Pancreatic secretions are secreted into the lumen of the acinus, and then accumulate in intralobular ducts that drain to the main pancreatic duct, which drains directly into the duodenum.
Control of the exocrine function of the pancreas are via the hormones gastrin, cholecystokinin and secretin, which are hormones secreted by cells in the stomach and duodenum, in response to distension and/or food and which cause secretion of pancreatic juices.
There are two main classes of exocrine pancreatic secretions:
| Secretion | Cell producing it | Primary signal |
| bicarbonate ions | Centroacinar cells | Secretin |
| digestive enzymes | Basophilic cells | CCK |
Pancreatic secretions from ductal cells contain bicarbonate ions and are alkaline in order to neutralize the acidic chyme that the stomach churns out.
The pancreas is also the main source of enzymes for digesting fats (lipids) and proteins. (The enzymes that digest polysaccharides, by contrast, are primarly produced by the walls of the intestines.)
The cells are filled with secretory granules containing the precursor digestive enzymes. The major proteases which the pancreas secretes are trypsinogen and chymotrypsinogen. Secreted to a lesser degree are pancreatic lipase and pancreatic amylase).
It is important to synthesize inactive enzymes in the pancreas to avoid autodegradation, which can lead to pancreatitis. These granules are termed zymogen granules (the term "zymogen" referring to the inactive precursor enzymes). Trypsinogen is an inactivated forms of trypsin, and chymotrypsinogen is an inactivated form of chymotrypsin.
Once released in the intestine, the enzyme enterokinase present in the intestinal mucosa activates trypsinogen by cleaving it to form trypsin. The free trypsin then cleaves the rest of the trypsinogen and chymotrypsinogen to their active forms.
