Pancreatic enzymes amylase

The thick tenacious secretions clog the panereatic ducts, resulting in a decrease of the pancreatic enzymes amylase and Kpase in the small intestines. The mother must administer these enzymes with every meal or snack to ensure digestion of carbohydrates and fats. 

Acute pancreatitis occurs most commonly as a result of obstruction of the pancreatic duct. Diseases of the biliary tract and alcoholism are factors which can lead to this condition. The symptoms of acute pancreatitis include abdominal pain and shock and these are thought to be due to pancreatic enzymes in the abdominal cavity. The biochemical features of acute pancreatitis include raised serum levels of pancreatic enzymes (amylase being the one most commonly measured) and hypo-... 

Amylase enters the blood largely via the lymphatics. An increase in hydrostatic pressure in the pancreatic ducts leads to a fairly prompt rise in the amylase concentration of the blood. Neither an increase in volume flow of pancreatic juice nor stimulation of pancreatic enzyme production will cause an increase in senm enzyme concentration. Elevation of intraductal pressure is the important determinant. Stimulation of flow in the face of obstruction can, however, augment the entry of amylase into the blood, as can disruption of acinar cells and ducts. A functional pancreas must be present for the serum amylase to rise. Serum amylase determination is indicated in acute pancreatitis in patients with acute abdominal pain where the clinical findings are not typical of other diseases such as appendicitis, cholecystitis, peptic ulcer, vascular disease or intestinal obstruction. In acute pancreatitis, the serum amylase starts to rise within a few hours simultaneously with the onset of symptoms and remains elevated for 2 to 3 days after which it returns to normal. The peak level is reached within 24 hours. Absence of increase in serum amylase in first 24 hours after the onset of symptoms is evidence against a diagnosis of acute pancreatitis (76). 

Zinterhofer, L. Wardlaw, S. Jatlow, P. and Seligson, D. Nephlometric determination of pancreatic enzymes I. amylase. Clin. Chim. Acta (1973), 43, 5-12. 

Supplementation with pancreatic enzymes may reduce the pain and fatty diarrhea associated with chronic pancreatitis (Table 20-3). Best results are achieved in patients who have mild non-alcoholic pancreatic disease. Common pancreatic enzyme supplements contain lipase, amylase, and protease in varying proportions. Thus, the dose can be tailored to the patient s requirement for exogenous enzyme supplementation and response to therapy. 

Non-enteric-coated pancreatic enzyme supplements can be used for initial therapy. The relative dose of amylase, lipase, and protease may be increased until control of pain and fatty diarrhea is achieved or the patient experiences intolerable side effects. If pain and diarrhea control are achieved, the patient can be transitioned to an enteric-coated supplement to maximize compliance. A reasonable example starting regimen is Viokase-8, six tablets with each meal and at bedtime, given with famotidine 20 mg at bedtime. 

Pancreatic enzyme supplements should be taken immediately prior to meals to aid in the digestion and absorption of food. Alternately, patients can supplement their diet with medium chain triglycerides (MCTs) or ingest foods rich in MCTs since they do not require pancreatic enzymes for absorption. An appropriate regimen incorporates the successful doses of each enzyme (amylase, lipase, and protease) from the starting non-enteric-coated regimen. As with the previous example, a patient stabilized on Viokase-8, six tablets with each meal, can be transitioned to Pancrease MT-16 three tablets with meals. The famotidine can then be discontinued. 

Amylase A pancreatic enzyme that cleaves starches. 

Some of the pancreatic enzymes in the lumen include pancreatic amylase, pancreatic lipase, elastase, trypsin, a-chymotrypsin, and carboxypeptidase A. For example, the aspirin derivatives aspirin phenylalanine ethyl ester, aspirin phenyllactic ethyl ester, and aspirin phenylalanine amide have been studied as substrates for carboxypeptidase A [67,68], with the phenylalanine ethyl ester derivative proving to be the best substrate. This study indicated that the carboxypeptidase A may serve as a reconversion site for many drug derivatives. 

Most patients with malabsorption require pancreatic enzyme supplementation (Fig. 28-2). The combination of pancreatic enzymes (lipase, amylase, and protease) and a reduction in dietary fat (to less than 25 g/meal) enhances nutritional status and reduces steatorrhea. An initial dose containing about 30,000 international units of lipase and 10,000 international units of trypsin should be given with each meal. 

Steatorrhea occurs in patients whose lipase output is at 10% or less of normal. Lipase and other pancreatic enzyme insufficiencies are observed in cystic fibrosis and chronic alcoholic pancreatitis. Patients with various liver diseases may also present with steatorrhea [18]. For these patients, pancreatic enzymes—mainly lipase, protease, and amylase—extracted with alcohol from porcine pancreases have been shown to provide amelioration of diarrhea. These enzymes are enriched and formulated in... 

Gastrointestinal enzyme activities tend to be lower in the newborn than in the adult. Activities of -amylase and other pancreatic enzymes in the duodenum are low in infants up to 4 months of age. Neonates also have low concentrations of bile acids and lipase, which may decrease the absorption of lipid-soluble drugs. 

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 purification of the pancreatic alpha amylase was effected on an affinity adsorbent prepared from enzymically degraded starch plus agarose activated with bisoxirane.14 The fractions from the affinity column were analyzed for protein components by u.v. absorbance, and for alpha amylase activity by incubating the fractions with starch and measuring the increase in reducing sugars. The results are shown in Fig. 5. 

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. 

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. 

Figure 5.13 Interaction of an amylose chain in the vicinity and in the hydrolytic site of pig pancreatic a-amylase. The impossibility of fitting a double helix in the hydrolytic site has been clearly established, along with determination ofthe direction of binding of the amylosic substrate in the cleft of the enzyme. (Reproduced with permission from reference 51)...

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