Pancreas amylase lipase

Lumenal metabolism. This may be triggered by digestive enzymes secreted from the pancreas (amylase, lipases, and peptidases including trypsin and a-chymotrypsin), and those derived... 

Exocrine pancreatic insufficiency is most commonly caused by cystic fibrosis, chronic pancreatitis, or pancreatic resection. When secretion of pancreatic enzymes falls below 10% of normal, fat and protein digestion is impaired and can lead to steatorrhea, azotorrhea, vitamin malabsorption, and weight loss. Pancreatic enzyme supplements, which contain a mixture of amylase, lipase, and proteases, are the mainstay of treatment for pancreatic enzyme insufficiency. Two major types of preparations in use are pancreatin and pancrelipase. Pancreatin is an alcohol-derived extract of hog pancreas with relatively low concentrations of lipase and proteolytic enzymes, whereas pancrelipase is an enriched preparation. On a per-weight basis, pancrelipase has approximately 12 times the lipolytic activity and more than 4 times the proteolytic activity of pancreatin. Consequently, pancreatin is no longer in common clinical use. Only pancrelipase is discussed here. 

The liver and the pancreas are not part of the digestive tract as such, but they provide enzymes and secretions required for digestion to occur in the small intestine. The pancreas secretes amylase, lipase, and nuclease enzymes, as well as several enzymes involved in breaking down proteins and peptides. As discussed below with digestion of fats, the liver secretes a substance called bUe that is stored in the gallbladder and then secreted into the duodenum when needed for digestion of fats. 

A 17-year-old man took clozapine in a dose that was gradually increased to 175 mg/day, and 23 days after the start of treatment developed mild epigastric pain (188). He had raised pancreas amylase (140 U/l) and lipase (463 U/l) activities, and four days later developed increasing pain in both shoulders and a large pericardial effusion. 

In duodenum digestive enzymes are added from the pancreas (pancreatic amylase, lipases, proteases), pH is neutralized, and detergents (bile acids) are added from gall bladder. 

The primary functions of the small intestine are digestion and absorption of food. The adult small intestine is approximately 6 m in length and is composed of the duodenum, ileum, and jejunum. Digestion occurs primarily in the upper small intestine and requires the action of pancreatic enzymes such as amylase, lipase, and trypsin, which are released from the pancreas into the duodenum, and bile salts from the biliary system. Absorption largely takes place in lower portions of the small intestine. 

Total volume of pancreatic juice, amount or concentration of bicarbonate, and activities of pancreatic enzymes are measured in duodenal contents. The enzyme most commonly measured is trypsin, but amylase, lipase, chy-motrypsin, and elastase may also be evaluated. The Lundh test consists of administering a standardized meal consisting of 5% protein, 6% fat, 15% carbohydrate, and 74% nonnutrient fiber. Advantages of the Lundh meal are that it provides a physiological stimulus to the pancreas and is simple to administer. However, administration of the meal prevents determination of the total enzyme and bicarbonate or secretory volume. Moreover, it provides inadequate or no stimu-... 

A09A A Enzyme Preparations Enzymes can be used therapeutically. Some are of animal origin (from the stomach and pancreas of food animals), some of vegetable origin and others of microbiological origin. Examples of the first type include pepsin and pancreatin, a mixture of amylase, lipase and trypsin (a protease) which catalyses the metabolism of proteins into smaller peptides and amino-acids. Pancreatin is frequently prescribed for patients with cystic fibrosis. 

The two common preparations of pancreatic enzymes for replacement therapy are obtained from the pancreas of the hog (Sus scrofa Linne var. domesticus Gray). Pancreatin (Don-nazyme, others) contains amylase, lipase, and protease, and has one-twelfth of the lipolytic activity of pancrelipase, on a weight-by-weight basis. Pancrelipase is more commonly used and is available in uncoated forms, as weU as capsules containing enteric-coated microspheres and enteric-coated microtablets, which withstand gastric acid (lipase is inactivated by acid) and disintegrate at pH > 6. Familiarity with these two classes of preparations is important clinically. 

Sokolowski, A., H. Spormaim, and G. Letko.1987. Influence of pancreatic edema and shortterm ischemia of rat pancreas on lipase and alpha-amylase activities in the serum and in the pancreas. Deutsche Zeitschrift filr Verdauungs und Stojfwechsekrankheiten 47 119-127. 

Protein mixture isolated from porcine or bovine pancreas, sometimes called pancreatin. Contains 3 enzymes amylase, lipase, and protease (chymotrypsin). 

In the second phase of these investigations on protein synthesis, an attempt was made to study the process in vitro. At first, intact cells had to be used. Amino acid incorporation was studied in liver slices amylase, lipase, and ribonuclease synthesis was investigated in slices of pigeon pancreas and the incorporation of glycine into reticulocyte hemoglobin was measured. The first of the above systems was exploited with exceptional success in Zamecnik s laboratory [138]. 

Pancreatic secretion for many, if not most, species is regulated in order to insure adequate protein digestion. Correspondingly, protease inhibitors have a greater impact on pancreatic secretion than do inhibitors of amylase and lipase (Toskes, 1986). The secretory response of the exocrine pancreas to protease inhibitors can be rapid (< 10 min), does not involve parallel increases in the secretion of all enzymes (Holm et al., 1992), and is probably mediated by a signaling pathway (see below). 

The answer is d. (Hardman, p 935.) Pancrelipase is an alcoholic extract of hog pancreas that contains lipase, trypsin, and amylase. It is effective in reducing the steatorrhea of pancreatic insufficiency None of the other drugs mentioned have significant action in the digestion of fats... 

Acute pancreatitis (AP) is an inflammatory disorder of the pancreas characterized by severe pain in the upper abdomen and increased serum concentrations of pancreatic lipase and amylase. 

Serum lipase is specific to the pancreas, and concentrations are usually elevated. The increases persist longer than serum amylase elevations and can be detected after the amylase has returned to normal. 

These agents are administered to aid in the digestion of food. The primary digestant preparations contain pancreatic enzymes or bile salts. Pancreatic enzymes such as amylase, trypsin, and lipase are responsible for digestion of carbohydrates, proteins, and lipids, respectively. These enzymes are normally synthesized in the pancreas and secreted into the duodenum via the pancreatic duct. Bile salts are synthesized in the liver, stored in the gallbladder, and released into the duodenum via the common bile duct. Bile salts serve to emulsify lipids in the intestinal tract and are important in lipid digestion and absorption. 

Hydrolytic enzymes Pancreatin Hydrolysis of starch (amylase), fat (lipase), and protein (protease) Porcine pancreas Digestive aid... 

Lipase (EC 3.1.1.3). Among the pancreatic enzymes applied to diagnose AP is lipase, which is released to blood similarly to amylase after the pancreas epithelial structure has been damaged. The determination of lipase activity has a higher diagnostic sensitivity (87.2-98%) in AP diagnosis than amylase (G12, L16) (Table 1). A five-to sixfold increase in the enzyme activity is observed... 

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. 

Relevant quality control should not be restricted to the usual triad of activities of pancreas lipase, a-amylase, and trypsin, but should be extended to the content of colipasc, the activities of the two other lipolytic enzymes present in pancreatine (phospholipase Aj and carboxylester lipase), and the dissolution characteristics of enteric-coated preparations as a function of time and pH (Fig. 16). The availability of such information will certainly contribute to a better tailoring of flic management of maldigestion in the individual patient and to a more appropriate correction of the obligate nonphysio logical route of delivery of these enzyme supplements. 

The lipolytic activity is determined by comparing the rate at which a suspension of pancreas powder hydrolyzes a substrate of olive oil emulsion with ihe rate at which a supiiuiuu of pancreas puwucf (amylase arid lipase) BnF hydrolyses ihe same substrate under the same conditions. The test is carried out under nitrogen. 

A = activity of pancreas powder (amylase and lipase) BRP in Ph. Bur. Units per milligram... 

Small quantities of pancreatic enzymes are released from the pancreas into the bloodstream even physiologically and are detectable as low serum activities and/or concentrations of lipase, amylase, trypsinogen, and chymotrypsino-gen, respectively. Since progressive destruction of the organ occurs in chronic pancreatitis, this should theoretically be reflected by decreased serum enzymes, but so far these tests are not clinically useful because of their low accuracy. 

The pancreas secretes a variety of enzymes into the gut. These include proteolytic enzymes, such as trypsin and chymotrypsin, lipase and amylase. The salivary glands also produce an amylase. The major hormones produced by the pancreas are insulin, glucagon and somatostatin. 

A common duct from the pancreas and gall bladder enters the duodenum. Duodenal pH is 6 to 6.5 due to the presence of bicarbonate that neutralizes the acidic ch5une emptied from the stomach. The pH is optimum for enzymatic digestion of protein and peptide food. Pancreatic juice containing enzymes is secreted into the duodenum from the bile duct. Trypsin, ch5unotrypsin, and carboxypeptidase are involved in the hydrolysis of proteins into amino acids. Amylase is involved in the digestion of carbohydrates. Pancreatic lipase secretion hydrolyzes fats into fatty acids... 

Pancreatic enzyme supplements are used to treat people who lack pancreatic secretions. Pancreatm, the British Pharmacopoeia standard, is an extract of pancreas, and contains enzymes with proteinase, amylase, and lipase activity most commercial formulations are similar or identical (SEDA16, 358). 

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