Pancreatic juice secretion

Dietary triacylglycerols are degraded to a small extent (via fatty acid release) by lipases in the low-pH environment of the stomach, but mostly pass untouched into the duodenum. Alkaline pancreatic juice secreted into the... 

Free biotin is subsequently released by the action of another and specific enzyme, namely biotinidase. The latter step is critical as it conditions efficient absorption and optimal bioavailability of dietary biotin. The carboxyl group of the valeric acid moiety of the biotin molecule must be free for its recognition by the involved transport mechanism through the intestinal enterocytes (Said and Redha 1987). Intestinal biotinidase is found in pancreatic juice, secretion of the intestinal glands, bacterial flora and the brush-border membranes. 

FIGURE 24.3 (a) A duct at the junction of the pancreas and duodenum secretes pancreatic juice into the duodenum, the first portion of the small intestine, (b) Hydrolysis of triacylglycerols by pancreatic and intestinal lipases. Pancreatic lipases cleave fatty acids at the C-1 and C-3 positions. Resulting monoacylglycerols with fatty acids at C-2 are hydrolyzed by intestinal lipases. Fatty acids and monoacylglycerols are absorbed through the intestinal wall and assembled into lipoprotein aggregates termed chylomicrons (discussed in Chapter 25). 

There are two main classes of proteolytic digestive enzymes (proteases), with different specificities for the amino acids forming the peptide bond to be hydrolyzed. Endopeptidases hydrolyze peptide bonds between specific amino acids throughout the molecule. They are the first enzymes to act, yielding a larger number of smaller fragments, eg, pepsin in the gastric juice and trypsin, chymotrypsin, and elastase secreted into the small intestine by the pancreas. Exopeptidases catalyze the hydrolysis of peptide bonds, one at a time, fi"om the ends of polypeptides. Carboxypeptidases, secreted in the pancreatic juice, release amino acids from rhe free carboxyl terminal, and aminopeptidases, secreted by the intestinal mucosal cells, release amino acids from the amino terminal. Dipeptides, which are not substrates for exopeptidases, are hydrolyzed in the brush border of intestinal mucosal cells by dipeptidases. 

During normal processes, approximately 9 liters of fluid traverse the gastrointestinal tract daily. Of this amount, 2 liters represent gastric juice, 1 liter is saliva, 1 liter is bile, 2 liters are pancreatic juice, 1 liter is intestinal secretions, and 2 liters are ingested. Of these 9 L of fluid presented to the intestine, only about 150 to 200 mL remain in the stool after reabsorptive processes occur. 

Exocrine glands within the pancreas secrete an aqueous fluid referred to as pancreatic juice. This fluid is alkaline and contains a high concentration of bicarbonate ion it is transported to the duodenum by the pancreatic duct. 

Pancreatic juice neutralizes the acidic chyme entering the duodenum from the stomach. Neutralization not only prevents damage to the duodenal mucosa, but also creates a neutral or slightly alkaline environment optimal for the function of pancreatic enzymes. The pancreas also secretes several enzymes involved in the digestion of carbohydrates, proteins, and lipids. 

Most pancreatic secretion takes place during the intestinal phase. The intestinal hormone secretin stimulates release of a large volume of pancreatic juice with a high concentration of bicarbonate ion. Secretin is released in response to acidic chyme in the duodenum (maximal release at pH < 3.0). The intestinal hormone cholecystokinin is released in response to the presence of the products of protein and lipid digestion. Cholecystokinin then stimulates the release of digestive enzymes from the pancreas. 

Bile is secreted by the liver, stored in the gallbladder, and used in the small intestine. It is transported toward the small intestine by the hepatic duct (from the liver) and the cystic duct (from the gallbladder), which join to form the common bile duct. Pancreatic juice is transported toward the small intestine by the pancreatic duct. The common bile duct and the pancreatic duct join to form the hepatopancreatic ampulla, which empties into the duodenum. The entrance to the duodenum is surrounded by the Sphincter of Oddi. This sphincter is closed between meals in order to prevent bile and pancreatic juice from entering the small intestine it relaxes in response to the intestinal hormone cholecystokinin, thus allowing biliary and pancreatic secretions to flow into the duodenum. 

The observed calcium/phosphate ratio of 4.5 at the intercept of the calcium and phosphate retention curves that should minimize the sum of the urine calcium plus urine phosphate losses was difficult to believe in view of both the known Ca/P ratio of bone and the amounts we were adding to these solutions. This disparity between the optimal ratio determined experimentally and what we had assumed this ratio should be on the basis of known body composition is partially reconciled by the experiment of Sutton and Barltrop. They fed preterm infants stable Ca46 and observed that up to 20% of the isotope absorbed was subsequently excreted in the stool. Our infants also were undoubtedly having unmeasured calcium losses from the bile, pancreatic juice and succus entericus secreted into their intestine... 

Foreign compounds may also enter the gut by direct diffusion or secretion across the gut wall, elimination in the saliva, pH partitioning of bases into the low pH of the stomach, and elimination in the pancreatic juice. 

In the small intestine, ribonuclease and deoxyribonuclease I, which are secreted in the pancreatic juice, hydrolyze nucleic acids mainly to oligonucleotides. The oligonucleotides are further hydrolyzed by phosphodiesterases, also secreted by the pancreas, to yield 5 - and 3 -mononucleotides. Most of the mononucleotides are then hydrolyzed to nucleosides by various group-specific nucleotidases or by a variety of nonspecific phosphatases. The resulting nucleosides may be absorbed intact by the intestinal mucosa, or they may un-... 

Four major enzyme groups are secreted lipolytic, proteolytic, amylolytic, and nucleic acid splitting enzymes. These pancreatic enzymes, some of which are secreted in multipile forms, possess specificities complementary to die intestinal membrane-bound enzymes (Tabic 1). Fresh, uncontsnkinated pancreatic juice is without proteolytic activity because these enzymes am in the form of inactive zymogens. An important fraction of the calcium in pancreatic juice accompanies the enzymes, especially ct-amylase. Human pancreatic juice is moat dose to that of the pig, with high proportions of lipase and a-amylase in comparison with other mammals [1]. Therefore, pig pancreas extract, pancreatin, has up to now been die oreferred enzvme source for therapeutic tuncreas substitution. 

The other group of enzymes of major concern to our discussion are the nucleases secreted by the pancreas, which are very much in the minority as they constitute less than 1% of the pancreatic juice protein (Scheele et al. 1981). Again this is in quantitative protein terms, and I can find no information concerning their actual activity in the lumen of the intestine. 

Depending on nutrient intake, the human pancreas secretes about 3 L of alkaline juice per day. Pancreatic juice contains hydrolytic enzymes... 

The flow of pancreatic juice and bile was tested before and after the experiment by means of an intravenous bolus of 5 pmol/kg secretin. Before the experiment the duodenum was continuously perfused at a rate of 2 ml/min for 435 min with isotonic saline containing phenol red (10 mg/1) as a marker. After drug treatment (intravenous infusion of gastrin-releasing peptide or duodenal HC1 perfusion) pancreatic and hepatic secretions were collected in 15-min periods and the volumes determined by weighing. Duodenal effluents were collected in 15-min periods and phenol red concentrations determined spectrophotometrically. Blood sampled were withdrawn for determination of secretin by radioimmunoassay. 

When not in use, the cannula is sealed from the exterior by inserting a threaded plug which allows pancreatic juice to enter the duodenum in the normal manner (Fig. 2, part C). For collection of juice this plug is removed and a long obturator is inserted (Fig. 2, part D). The latter effectively isolates the pancreatic secretion from other duodenal contents. 

As the stomach empties, the hydrochloric acid in the material entering the small intestine is neutralized by secretions from the pancreatic ducts, bile, and pancreatic juice. The digestion of the starch dextrins is continued by the action of the pancreatic a-amylase. 

Q10 Normally, pancreatic secretion is stimulated by eating. The factors involved are both nervous and hormonal. Pancreatic secretion is increased by vagal (parasympathetic) stimulation and inhibited by sympathetic stimulation. Cholecystokinin (CCK), released from the wall of the duodenum, stimulates pancreatic juice, which is rich in enzymes. Secretin (the first hormone to be discovered, by Bayliss and Starling), which is also produced in the duodenum, stimulates a pancreatic fluid with a high bicarbonate content. 

Most biotin in foods is present as biocytin, incorporated into enzymes, which is released on proteolysis, then hydrolyzed by biotinidase in the pancreatic juice and intestinal mucosal secretions to yield free biotin. Biocytin is not absorbed to any significant extent. 

The pancreas of all mammals so far investigated contain an elastase with similar enzymatic reactions (Lewis et al., 1956 Marrama et al., 1959), but immunological differences have been observed between pancreatic elastases from different species (Moon and Mclvor, 1960). Elastase is secreted in the pancreatic juice as an inactive zymogen, proelastase (Grant and Robbins, 1955 Lamy and Lansing, 1961) which, like other pancreatic enzymes, is activated by trypsin or enterokinase. 

In this condition the normal pathway of secretion of pancreatic juice into the intestine is obstructed. Thus the zymogens of the proteolytic enzymes are converted to the active forms inside the pancreatic cells, prematurely. This active proteolytic enzymes act on the pancreatic tissue itself, causing serious destruction of pancreas, which is very painful and can be fatal. 

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