Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum samples were obtained from 43 children 14 years old or younger in Malaysia and Guatemala. The levels of the serum glycoprotein alpha 2-macroglobulin (alpha 2-M) were assayed by two methods: the trypsin-binding assay of Ganrot (Clin. Chim. Acta 14:493, 1960) and a radial immunodiffusion assay against alpha 2-M antiserum. The two methods gave the same results. When serum alpha 2-M levels were plotted against serum vitamin A concentrations, they were significantly correlated (r = 0.505, P less than 0.001); children with serum vitamin A levels greater than 40 micrograms/100 ml had alpha 2-M levels of 3.71 +/- 0.79 mg/ml (mean +/- SD, n = 13), while those with level less than 40 micrograms/100 ml had alpha 2-M levels of 2.78 +/- 0.51 mg/ml (n = 30); the difference was significant (P less than 0.001). Normal, apparently healthy children had alpha 2-M levels of 3.90 +/- 0.39 mg/ml. Most of the children sampled suffered from a variety of infections; of these, measles appeared to counteract the effect of vitamin A deficiency by elevating alpha 2-M levels. Vitamin A-deficient children with measles had alpha 2-M levels not significantly lower than those of normal children. The difference between deficient and normal values of alpha 2-M was still significant (P less than 0.05) when expressed per milligram of serum protein, showing that the effect was not caused by lowered serum protein concentrations associated with protein-calorie malnutrition, from which most of the deficiency children suffered.
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PMID:alpha 2-Macroglobulin in vitamin A-deficient children. 8 10

In order to characterize the response of the pancreas to undernutrition during the critical neonatal growth phase, acquired postnatal malnutrition was induced in the rat, using the expanded litter. An experimental nursing litter of 16 rats and control litters of 7 to 8 rats were formed. At 19 days of age, the pups were killed. Mean pancreatic wet weight was decreased in the malnourished rat to a greater extent than the decrease in total body weight (49 versus 60%). Decreased organ weight was predominantly the result of a decrease in DNA content and cell number. Enzyme activities expressed per total organ were all diminished; lipase to the greatest extent; trypsin and amylase to an intermediate extent; followed by chymotrypsin and the carboxypeptidases. The specific activities of lipase and trypsin were decreased with lipase, the most severely effected. The low trypsin levels can be attributed to trypsin inhibitor. It is possible therefore, that only the specific activity of lipase is significantly decreased. The decrease in enzyme activities, expressed both as specific activities and as total organ activities were decreased in a nonparallel fashion.
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PMID:Effect of postnatal malnutrition on pancreatic zymogen enzymes in the rat. 31 98

Enterokinase initiates digestion of protein by conversion of trypsinogen into trypsin. The interactions between enterokinase and trysin were investigated in 6 patients with intractable diarrhea of infancy and 34 children with celiac disease. The six infants between 2 and 3 months with intractable diarrhea of infancy had reduced mucosal enterokinase activity (9.5 +/- 4.8muM per gram of protein per minute) and reduced intraluminal trypsin activity (2.9 +/- 0.7muM per gram of protein per minute) as compared with healthy controls (109 +/- 34.2muM per gram of protein per minute and 14.3 +/- 5.8muM per gram of protein per minute) respectively. The activities of all enzymes returned toward normal following treatment with intravenous alimentation. The mucosal morphology of all pretreatment biopsies in all cases showed Grade III atrophy which improved. These findings suggest that enterokinase deficiency and reduced intraluminal trypsin activity in intractable diarrhea of infancy may be one of the contributing factors to protein malabsorption and consequent malnutrition. Thirty-four children with celiac disease were between the age of 9 months and 13 years. The 11 newly diagnosed patients with celiac disease demonstrated Grade III to IV atrophy of the mucosa. The 23 patients with treated celiac disease on a gluten-free diet showed a normal to Grade II atrophy. In both treated and untreated celiac disease the enterokinase activities and the intraluminal trypsin activity were within normal limits. The enterokinase activity in celiac disease is near normal in contrast to the marked reduction noted in intractable diarrhea of infancy even though the intestinal mucosa shows marked morphological alteration and the disaccharidase activities are greatly reduced in celiac disease. After a prolonged alimentary fast of up to 26 days on intravenous alimentation, two patients with intractable diarrhea of infancy showed improvement in the activities of enterokinase and trypsin. These findings demonstrate that enterokinase and trypsin activities in the gut were present and improved in the absence of oral feeding.
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PMID:The interrelationship of enterokinase and trypsin activities in intractable diarrhea of infancy, celiac disease, and intravenous alimentation. 80 41

Two therapeutic regimens were compared in 16 infants with protracted diarrhea and malnutrition. Eight patients were treated with total parenteral nutrition given via a central vein (group A); the remaining eight patients received a combination of dilute parenteral nutrients given in a peripheral vein plus continuous enteral feedings of an elemental diet (group B). All patients recovered although two infants in group B were switched to TPN treatment after a poor response to the elemental diet. Intestinal biopsies were performed: (1) before treatment; (2) after 2 to 3 weeks of TPN or elemental diet; and (3) after 2 to 3 weeks of Nutramigen feedings. Before treatment, all patients had atrophic changes in the jejunal epithelium and deficient disaccharidase and trypsin activities. The second biopsy showed morphologic recovery in all patients, incomplete recovery of lactase and trypsin in both treatment groups, and complete recovery of sucrase and maltase activities only in group B patients. The third biopsy showed normal morphology and complete recovery of all enzymes measured. The mean number of hospital days was 46 +/- 4.8 for group A and 34 +/- 1.6 for group B (p less than 0.05) suggesting that patients given enteral feedings early tended to have a more rapid return of intestinal function and of some intestinal enzymes.
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PMID:Protracted diarrhea and malnutrition in infancy: Changes in intestinal morphology and disaccharidase activities during treatment with total intravenous nutrition or oral elemental diets. 81 May 53

Extensive metabolic studies were conducted in five normal controls and in five study patients after total gastric resection with Roux-en-Y (RY) reconstruction to determine the nutritional consequences of this particular technique of restoring gastrointestinal continuity. Although malabsorption of fat (19.2 +/- 2.2%) and nitrogen (22 +/- 2.5%) demonstrated in the study patients was moderate, it was significantly greater than normal ( less than 0.01). In spite of the demonstrated malabsorption, however, positive nitrogen balances (+ 0.33 +/- 0.18 gm/day) were maintained in the RY patients throughout the investigative period. These observations suggest that malabsorption after RY is infrequently of clinical significance, even in this "worst-case" situation characterized by complete removal of gastric tissue. Malnutrition should occur in only those patients with more limited gastric resections and RY reconstruction who are unable to increase caloric intake to cover losses due to malabsorption. A significant decrease in both trypsin and lipase concentrations and a marked delay in secretion of these enzymes was noted in the RY patients in response to a test meal (p less than 0.01). Malabsorption of fat and nitrogen in RY patients improved after exogenous pancreatic enzymes, but not after administration of tetracycline. Bacterial overgrowth as a cause of postoperative malabsorption may be less important than previously thought. Malabsorption after RY is due primarily to maldigestion brought about by duodenal bypass which, in turn, results in either an absolute or a relative pancreatic enzyme insufficiency.
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PMID:Pathophysiology and significance of malabsorption after Roux-en-Y reconstruction. 87 Oct 13

Thirty-three patients with esophageal cancer were studied to assess the relationship between nutritional state and the acute phase protein responses. Blood samples taken preoperatively and days 1, 4, 7 and 14 after operation were analyzed for C-reactive protein, fibrinogen, alpha 1-antitrypsin, alpha 1-acid glycoprotein and haptoglobin. Significant Spearman's coefficients were found between percent of ideal body weight (IBW) and alpha 1-acid glycoprotein (r = -0.42), between prealbumin and alpha 1-anti-trypsin (r = -0.55), and between retinol-binding protein and alpha 1-antitrypsin (r = -0.51). Postoperatively, the levels of C-reactive protein, fibrinogen, alpha 1-anti-trypsin and alpha 1-acid glycoprotein were significantly lower in the poorly nourished group than in the other groups. The changes of acute phase proteins in the immediate postoperative period were affected by the preoperative nutritional state, and were less marked in the poorly nourished patients. Between two groups of patients in whom lymph node dissection was carried out in 2 or 3 areas, no significant differences were observed in the acute phase protein responses postoperatively. The measurement of acute phase proteins is very important in assessing the body defense capacity of the patient, but it should be noted that the changes may be affected by several factors including malnutrition.
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PMID:[Postoperative changes in acute phase protein in patients with esophageal cancer]. 138 Jun 33

It was established that the activity of trypsin and the content of its inhibitors--alpha 1-inhibitor of proteinases and alpha 2-macroglobulin--undergo phase changes of different meaning and direction with the gradual development of traumatic shock. The character of these changes indicates that trypsinemia is an important pathogenetic link of traumatic shock and corresponds to its severity. The compensatory activation of the trypsin inhibitors is directed to increasing the resistance of the body to trypsinemia. Deficiency of the inhibition system leads to activation of organic proteolysis and growth of the content of middle-molecular peptides in the blood. Such a character of homeostasis disorders substantiates the need for the search for effective measures of correction of the trypsin-antitrypsin system and freeing the organism of the excess of middle-molecular molecules.
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PMID:[The trypsin-antitrypsin system and the content of blood middle-molecular peptides in experimental traumatic shock]. 169 70

Skin lesions associated with alpha 1-antitrypsin deficiency are becoming better defined and understood. Deficiency in this major antiproteinase, which neutralizes multiple proteolytic enzymes ranging from collagenases and elastases to trypsin and chymotrypsin, thus results in significant tissue autodigestion. This anti-proteinase is secreted by activated lymphocytes and macrophages, suggesting the existence of homeostasis which titrates the release of proteolytic enzymes by these cells, and the adequate neutralization of these proteases in order to prevent excessive tissue autodigestion each time these inflammatory cells are activated. We report a patient with alpha 1-antitrypsin deficiency who, following insect bites and cellulitis developed widespread itching and scratching, leading to widespread lesions of prurigo nodularis. The colonization of his multiple skin lesions with Staphylococcus aureus and the release of potent T cell mitogens, such as Protein A and enterotoxin A from the bacterial cell membrane may have resulted in the release of additional proteolytic enzymes by the activated lymphocytes and macrophages, without the concomitant secretion of alpha 1-antitrypsin with subsequent aggravation of his pruritus. These concepts are supported by electron microscopic evidence of excessive tissue autodigestion, and by immunocytochemical data identifying the presence of T helper and T cytotoxic/suppressor lymphocytes as well as macrophages within the upper dermis.
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PMID:Alpha-1 antitrypsin deficiency in a patient with widespread prurigo nodularis. 182 11

Thirty-six infants suffering from gastrointestinal diseases during infancy were evaluated for exocrine pancreatic function by means of the pancreozymin-secretin test. Duodenal fluid volume, protein content, and content and peak-specific activity of amylase, lipase, and trypsin were determined following intravenous administration of either pancreozymin (CCK) or secretin. Seven infants receiving long-term parenteral nutrition and 17 infants receiving oral feedings and exhibiting first-degree malnutrition in association with chronic diarrhea underwent testing. Results were compared to those of a group of 12 age-matched infants with chronic diarrhea and weight loss. Four patients receiving total parenteral nutrition (TPN) suffered from severe short bowel syndrome and three had intractable diarrhea of infancy. The total duration of TPN ranged from 1.5-12 months, and the period of exclusive TPN in the absence of oral feedings ranged from 1-4 months. The heights, weights, and weight-for-height relationships were at or above the fifth percentile for all seven infants. The weight-for-height relationship of each patient in the control group was above the fifth percentile, while that of all malnourished infants was below the fifth percentile. No significant difference was found in the volume of fluid collected following either CCK or secretin administration. The content and concentration of amylase and lipase were lower in those patients receiving TPN. The levels were statistically significant (p less than 0.05) following secretin administration. In contrast, the peak-specific activity and total trypsin content, as well as protein content, was not significantly different in patients receiving TPN, controls, and malnourished patients.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Nutrition and exocrine pancreatic function in infancy: effects of total parenteral nutrition and first degree malnutrition. 244 51

Chronic reserpine treatment (500 micrograms/kg) of the rat results in generalized exocrinopathy, impaired pancreatic secretion, and decreased pancreatic amylase. These characteristics are similar to those in cystic fibrosis and are the basis for use of this experimental model for cystic fibrosis. Pancreatic enzymes adapt to diet, but it is not known whether chronic reserpine treatment affects this response. Due to the malnutrition induced by this treatment, another dose of reserpine was required that would alter pancreatic function but not induce malnutrition in order to evaluate dietary adaptation. Male rats (100-120 g) were injected subcutaneously daily for 7 days with 1) no injection (control); 2) 1.0 ml/kg vehicle or sham (pair fed-sham); or 3) reserpine: 500, 50, or 5 micrograms/kg. Food consumption was comparable among control and reserpine-treated (50 and 5 micrograms/kg) rats and significantly greater (200%) than pair fed-sham and 500 micrograms/kg reserpine-treated rats. Pancreatic amylase, however, was significantly lower in all reserpine-treated rats (500 micrograms/kg, 74%; 50 micrograms/kg, 56%; 5 micrograms/kg, 52%) than in control rats. To evaluate dietary adaptation, control and reserpine-treated (5 micrograms/kg) rats were fed high carbohydrate, high fat or high protein diets. Both groups adapted to these diets with the greatest amylase, lipase, and trypsin activities in high carbohydrate-, high fat-, and high protein-fed rats, respectively. Reserpine-treated rats fed high carbohydrate, however, had significantly lower (64%) amylase activity than high carbohydrate-fed control rats. Although reserpine-treated rats can adapt pancreatic enzymes to diet, the adaptation of amylase to carbohydrate is impaired.
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PMID:Effects of reserpine treatment on dietary adaptation of the rat exocrine pancreas. 245 Dec 6


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