Pancreas amylase

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. 

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... 

Saliva and pancreatic juice both contain a-amylase. The activity of this enzyme in saliva is not significant compared with that in the pancreatic juice released into the gut. Release of amylase from the pancreas is controlled by a mechanism similar or identical to the one that stimulates the release of tr)rpsinogen, namely by the influence of CCK on the exocrine pancreas. Amylase catalyzes the hydrolysis of starch at interior positions rather than at the ends of the polymer. This activity yields products such as maltose and longer-chain-length oligomers of glucose. Also, amylase does not catalyze the hydrolysis of starches at branching points. Therefore, small branched-chain structures called dextrins are formed that are not hydrolyzed by the er zyme. 

Since elsinan has a unique structural feature, its digesta-bility and also methanism of the enzymatic degradation have attracted our attention. In the searches of enzymes capable of degrading this glucan, we became aware of susceptibility of elsinan to particular type of a-amylase, such as salivary and pancreas amylase. This prompted us to examine various amylolytic enzymes, and isolation of the degradation products. 

These oligosaccharides were analyzed by h.p.l.c. It must be noted that the main products by the actions of salivary, hog pancreas and bacterial saccharifying a-amylase appear to be identical to each other. It was characterized as 4-0 -a-nigerosyl-D-glucose. The mode of action with Taka amylase seems to differ from those with salivary and pancreas amylases. 

Rat pancreas amylase activity was found to be irreversibly destroyed when subjected to polyacrylamide gel electrophoresis.The measure of enzyme inactivation was dependent on the duration of electrophoresis. In the presence of urea the amylase denaturing effect was enhanced. 

Trypsin does not digest the a-amylase molecule unless the metal ion has been removed. The enzyme-substrate complex (amylase and starch) probably tightens the configuration of the amylase molecule, thereby further strengthening the binding of the metal. These observations are of interest because of the close association between amylase and proteolytic enzymes. In the pancreas, amylase is synthesized in the endoplasmic reticulum and is then transferred, probably... 

Diastase or amylase is formed when malt is produced by the germination of barley grains. Malt is therefore a good source of the enzyme. Diastase is also secreted by the salivary glands (when it is known as ptyalin), and also by the pancreas. Its function is to hydrolysef starch to a mixture of maltose and dextrin ... 

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). 

The rate of urine amylase excretion is a sensitive reflection of the amylase released into the blood. The urine amylase remains abnormal 1-2 weeks after the serum returns to normal because the renal clearance of amylase rises 3-fold in acute pancreatitis and takes 1-2 weeks to return to normal. In pancreatitis, a number of investigators have reported a higher percentage of urinary amylase elevations, as contrasted with serum amylase elevations, particularly when the urinary amylase output over an interval is measured. Random urine collections for one, two and 24 hours are 792-4264 (2926 1074 S.D.) units per 24 hours. However, the wide range of normals make interpretation of results difficult. Of 107 patients with elevated serum or urine amylases, 16 were found to have a normal pancreas at operation (78). 

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). 

KATAOKA K, DiMAGNO E p (1998) Effect of chronic amylase inhibition on pancreatic growth and acinar cell secretory function in rats. Pancreas. 17 50-56. 

Pancreas Fever, graft tenderness and swelling, abdominal pain, ileus, malaise Increased FBS, leukocytosis, decreased human C-peptide and urinary amylase levels... 

Polysaccharide (starch) Amylase Fragment polysaccharides into disaccharides (maltose) Salivary glands pancreas Mouth stomach small intestine... 

Kleene, R. et al. (2000) SH3 binding sites of ZG29p mediate an interaction with amylase and are involved in condensation sorting in the exocrine rat pancreas. Biochemistry 39, 9893-9900. 

Fischer, brilliant results were achieved, and in succession the a-amylases of pig pancreas, of Bacillus subtilis, of human saliva, of human pancreas, and of Aspergillus oryzae, and the /3-amylase of malt, were successfully crystallized. Important biological deductions were gained from this study whereas the amylases of human pancreas and saliva cannot be distinguished from one another, amylases from pig pancreas and from human pancreas are different. These differences are manifested in molecular weight, crystalline forms, electrophoretic mobility, and influence of the pH on the activity however, all the amylases have the same specific biochemical action. The identity of the enzymes seems to be dependent on the species and not on the organ. Interest in biologically active proteins led Meyer to a study of the protein hormones, a field in which he was very active at the time of his death. 

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. 

The fiber fraction was washed several times with water, ratio 1 5, the washings being added to the starch fraction (Figure 2). Final traces of starch were removed from the fiber by incubation with 2% alpha-amylase (Sigma Chemical Co., type V-A from hog pancreas) for 16 hr at 37°C, and washing several times with distilled water before freeze-drying. 

Pancreatic amylase Infants with this deficiency begin life unable to digest starch. However, after a few months, the pancreas starts to produce sufficient amylase. Adults produce such an excess of this enzyme that even patients with severe pancreatitis (who are unable to produce sufficient lipolytic or proteolytic enzymes) can produce sufficient amylase to cope with a normal amount of starch in the diet. 

Amylase, the most important endoglyco-sidase in the pancreas, catalyzes the hydrolysis of al 4 bonds in the polymeric carbohydrates starch and glycogen. This releases maltose, maltotriose, and a mixture of other oligosaccharides. 

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. 

When the acidic stomach contents reach the small intestine, they are neutralized by bicarbonate secreted by the pancreas, and pan creatic a-amylase continues the process of starch digestion. 

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