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

The potato inhibitors of proteases inhibit the activation of trypsinogen, chymotrypsinogen, proelastase, procarboxypeptidase A and B induced by trypsin. These inhibitors do not inhibit the activation of trypsinogen induced by enterokinase. Potato inhibitors have no influence on pepsinogen autoactivation and on pepsin activity.
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PMID:The action of potato inhibitors on activation of zymogen forms of digestive system proteases. 52 19

Peptide YY (PYY) and neuropeptide Y (NPY) inhibit agonist-induced adenosine 3',5'-cyclic monophosphate (cAMP) production and pepsinogen secretion from chief cells. We used radiolabeled PYY and NPY to characterize receptors on chief cells from guinea pig stomach. Binding of 125I-labeled PYY was rapid (70% maximal within 10 min) and specific (not inhibited by secretin, vasoactive intestinal peptide, cholecystokinin, carbachol, prostaglandin E2, forskolin, or cholera toxin). Measurement of the ability of PYY to inhibit binding of 125I-PYY indicated the presence of 1.8 x 10(3) high-affinity [dissociation constant (Kd) = 1.7 nM] and 5.1 x 10(4) low-affinity (Kd = 83.3 nM) sites/cell. Internalization of bound 125I-PYY was suggested by slow and incomplete dissociation in the presence of unlabeled PYY (50% after 2 h) and was examined further by measuring residual binding after washing with acetic acid (pH 2.5), glycine (pH 10.5), or trypsin. After 30 min at 37 degrees C, internalization of radioligand was evidenced by the failure of washing with these solutions to remove 50-65% of bound radioactivity. At 4 degrees C, internalization of 125I-PYY was nearly abolished. Binding of 125I-PYY and 125I-NPY was inhibited by NPY-(13-36) but not by [Leu31,Pro34]NPY indicating that these are Y2 receptors. In guinea pig chief cells, PYY and NPY modulate cAMP-mediated pepsinogen secretion by interacting with specific high-affinity Y2 receptors.
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PMID:Y2 receptors for peptide YY and neuropeptide Y on dispersed chief cells from guinea pig stomach. 131 99

Fusion genes combining the 5'-transcriptional regulatory region of the rat trypsin I gene and the structural gene of human growth hormone as a reporter were expressed to the high levels characteristic of the endogenous trypsin I gene selectively in the acinar cells of the pancreas of transgenic mice. As little as 232 base pairs of trypsin gene sequences containing the transcriptional start site and upstream promoter elements were sufficient to direct pancreatic expression. The tissue-specific expression was controlled transcriptionally. Trypsin-human growth hormone fusion transgenes also were expressed, although at low levels, in the stomach, an unexpected site for the expression of pancreatic digestive enzymes. Expression in the stomach of endogenous trypsin, elastase, and amylase genes in both normal and transgenic mice verified that transgene expression was consistent with normal expression of pancreatic genes. Endogenous amylase colocalizes with pepsinogen in the acinar cell-like Chief cells of the glandular portion of the mouse stomach. The expression of pancreatic genes in stomach cells is probably the consequence of similar developmental origins of pancreatic and gastric acinar cells from the primordial gut.
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PMID:Selective expression of trypsin fusion genes in acinar cells of the pancreas and stomach of transgenic mice. 146 18

Radioimmunoassay was used to determine trypsin, pepsinogen and gastrin content in the blood serum with the use of kits produced by the firm "Oris" (France). A total of 43 patients with peptic ulcer (25 with duodenal ulcer and 18 with gastric ulcer), 20 patients with chronic gastritis and 10 normal subjects were investigated. The study was conducted on an empty stomach and after a test breakfast consisting of 2 boiled eggs, 100 g of cheese, 100 g of white bread, 25 g of butter, 50 g of sugar and 200 g of tea (57 g of proteins, 63 g of fats, 103 g of carbohydrates; calorie value comprised 1212 kcal). It has been shown that food intake is a regulator of gastrin, pepsinogen and trypsin production that permits evaluating functional possibilities of gastrin-producing cells, the main gastric cells and acinar cells of the pancreas. The investigation conducted has evidenced that compensatory shifts in the levels of gastrin, pepsinogen and trypsin taking place in gastroduodenal disease are directed to the improvement of digestive processes.
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PMID:[The effect of food intake on the content of proteolytic enzymes and gastrin in the blood of patients with peptic ulcer and chronic atrophic gastritis]. 179 41

Blood serum insulin, glucagon, pepsinogen, trypsin was studied by radioimmunological methods in 95 patients with ulcer disease. Fasting values and values 1 and 2 hours after a standard breakfast (1212 kcal) were evaluated. It was established that all patients showed a statistically valid increase of the basal level of glucagon while patients with gastric ulcer showed an increase of the basal insulin level. Use of a test breakfast showed reserve and compensatory capacities of the hormonal pancreatic function. Patients with gastric and duodenal ulcer revealed an increase of the pepsinogen level under conditions of basal secretion and after a test breakfast.
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PMID:[Pancreatic hormonal function and proteolytic activity in peptic ulcer]. 208 6

Using isolated cells and subcellular fractions from pig gastric mucosa, antigenic structures with specific binding of IgG from sera of patients with auto-immune atrophic gastritis were characterized by means of immunoblotting and enzyme-linked immunosorbent assay. In immunoblotting experiments using mucosal cells as the antigen source, two dominating bands of 94 and 41 kDa were found. The two major antigens were identified as the H,K-ATPase (94 kDa), which constitutes the parietal cell acid pump, and pepsinogen (41 kDa) located in the chief cells. There was also a small but significant binding of antibodies to a preparation of Na,K-ATPase, an enzyme which is about 60% homologous to H,K-ATPase. Commercial preparations of hog gastric pepsinogen and pepsin bound pernicious anaemia IgG with equal efficacy. When sera from seven patients with the diagnosis pernicious anaemia were tested, all were found to contain auto-antibodies against H,K-ATPase as well as pepsinogen. In intact, isolated H,K-ATPase-containing vesicles the cytosolic part of the ATPase molecule is facing the outside of the vesicles. Both intact and trypsinized vesicles were incubated with patient sera and with a monoclonal antibody against H,K-ATPase. Pernicious anaemia IgG was found to bind to a cytosolic, trypsin-resistant structure, but the binding of the monoclonal antibody was lost upon trypsinization. The present results indicate that intracellular structures of the gastric mucosa, due to cell damage, may be exposed to immune-competent cells, which do not recognize these structures as 'self'.
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PMID:Characterization of antigenic structures in auto-immune atrophic gastritis with pernicious anaemia. The parietal cell H,K-ATPase and the chief cell pepsinogen are the two major antigens. 252 90

Altogether 25 patients with peptic ulcer and 26 patients with chronic pancreatitis were examined for gastric and pancreatic secretion. Histamine dihydrochloride (0.008-0.024 mg/kg) was employed to stimulate gastric secretion whereas cholecystokinin (2U/kg/h) and calcium gluconate (16 mg/kg) were used to stimulate pancreatic secretion. Lidocain (1.2 mg/kg), a blocker of Ca2+-channels, and lithium hydroxybutyrate (12 mg/kg), a blocker of phosphatidylinositol transformations, were employed for suppression of gastric and pancreatic secretion. The content of HCl, pepsinogen, fucose, cAMP and cGMP was measured in gastric juice, that of bicarbonates, amylase, lipase, trypsin, cAMP and cGMP in pancreatic juice. It has been shown that mechanisms dependent on cAMP and on extra- and intracellular Ca2+ are involved in the initiation and maintenance of gastric and pancreatic secretion. However, the contribution of those mechanisms is different as applied to the regulation of ions and enzymes, on the one hand, and to various enzymes, on the other.
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PMID:[General mechanisms of regulation of the activity of the stomach and pancreas in peptic ulcer and chronic pancreatitis]. 272 25

Pepsinogen has previously been shown to bind non-specifically to immune complexes and aggregated immunoglobulins. We demonstrate here using a solid-phase immunoassay that immunoglobulins aggregated by heat or glutaraldehyde bind non-specifically to several different enzymes. Some of these, including pepsinogen (marketed as pepsin), hyaluronidase and trypsin, are used in the breakdown of tissues or biochemical preparations during the preparation of antigens. Contamination of impure antigens by enzyme is likely to lead to products which bind non-specifically to immune complexes. This can cause misidentification of complexes as antibodies. We recommend that all tests for specific antibody involving the use of antigens prepared by these or other enzymes should include a control with aggregated immunoglobulin substituted for the test serum.
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PMID:Binding of monomeric and aggregated immunoglobulin to enzymes. A source of artefact in antibody assays. 291 Oct 16

This study has shown that ileal and colonic mucosa contained roughly 1.2 microg/g of irPSTI. irPSTI from gastrointestinal mucosa eluted in a similar way to that of native PSTI after chromatographic separation and inhibited trypsin in a 1-1 molar way. The PSTI immunoreactive material was localized in the Paneth cells and the goblet cells in the small and large intestine. In normal gastric mucosa it was found in the foveolar cells while the acid and pepsinogen producing cells lacked PSTI immunoreactive material. In gastric mucosa with intestinal metaplasia a marked deficiency of PSTI was found. These findings indicate that gastrointestinal mucosa could be an additional source of irPSTI. Further studies are needed to elucidate if PSTI is involved in the defence of the gastrointestinal mucosa.
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PMID:Immunoreactive pancreatic secretory trypsin inhibitor in gastrointestinal mucosa. 324 86

Protein digestion is a complex process in which most aspects have a developmental pattern of activity. Gastric pH and intestinal peptide and amino acid transport as well as the activities of pepsinogen, trypsin, chymotrypsin, enterokinase and intestinal dipeptidases vary during development. No one species has been assessed for all these aspects and it is not possible to present an integrated developmental view of protein digestion. The following developmental changes, however, have been observed. Gastric pH declines, and peptic and pancreatic proteases exhibit increasing activity in pigs and rats after birth. The increase in pigs is gradual over several weeks starting at birth, whereas the increases in the rat begin at 2 wk, just prior to the time of weaning. The activities of dipeptidases in the rat and pig, peptide transport systems in the guinea pig and rabbit and amino acid transport systems in the rat, rabbit, guinea pig and chicken, however, appear (with few exceptions) to be active in the small intestine at the time of birth. Frequently, these activities peak in the neonate and decline during the postnatal period. In the rat, dietary protein tends to increase the activities of pancreatic proteases and intestinal peptidases and to increase the rate of uptake of amino acids by the intestinal epithelium. Individual dietary amino acids also influence amino acid transport systems. The data indicate that most processes in protein digestion undergo marked changes during prenatal and postnatal development and are influenced by the level of feeding and composition of the diet.
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PMID:Development and adaptation of protein digestion. 388 40


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