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 effect of proglumide (400 mg/kg), spantide (400 g/kg) and ranitidine (20 mg/kg) on pancreatic secretory and trophic response to bombesin (10 micrograms/kg) was studied in the rat. Drugs were administered alone or combined with bombesin three times daily for 5 days. Saline-treated rats were used as controls. At the end of treatment, animals were anaesthetized and pancreatic juice was collected for 1 h after caerulein stimulation (1 microgram/kg intraperitoneally). Afterwards, rats were sacrificed and the weight and composition of pancreatic tissue were determined. As compared with control (saline) values, the volume of pancreatic juice and the output of trypsin and amylase were increased by treatment with bombesin. Neither proglumide nor spantide affected basal and caerulein-stimulated pancreatic exocrine secretion. Ranitidine, although unable to modify protein and enzyme content of pancreatic secretion, significantly reduced the volume of pancreatic juice in both basal conditions and after caerulein stimulation. Bombesin increased pancreatic weight as well as the protein and enzymatic contents of the gland. Neither the weight of the pancreas nor its composition were significantly affected by CCK-antagonist proglumide, the putative bombesin antagonist spantide or the H2-receptor antagonist ranitidine. These results show that bombesin has a trophic effect on rat pancreas and concomitantly increases its secretory capacity. Both effects are likely to be mediated through a direct action of the peptide on the pancreatic gland.
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PMID:Bombesin-induced pancreatic secretion and growth in rats: effect of proglumide, spantide and ranitidine. 171 15

Ejaculated spermatozoa from brush-tailed possums and tammar wallabies were washed by a 'swim up' procedure into Hanks Balanced Salt Solution (HBSS), and then exposed to test solutions. Spermatozoa were incubated at 33 degrees C, or room temperature when long-term sperm survival (greater than 10 h) was required. Exposure of spermatozoa to calcium ionophore A23187, cyclic nucleotides, phosphoinositide pathway intermediates, lysophospholipids, trypsin or 'capacitating' high ionic-strength medium (380 mosmol) followed by 3% bovine serum albumin for periods up to 24 h did not induce acrosomal loss. However, there were major changes within the acrosome: large numbers of empty membrane-bound vesicles were formed, the electron density of the acrosomal matrix decreased and the acrosome swelled slightly. The origin of the vesicles is unclear but the acrosomal membranes and the plasma membrane remained intact.
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PMID:Stability of the acrosome of the brush-tailed possum (Trichosurus vulpecula) and tammar wallaby (Macropus eugenii) in vitro and after exposure to conditions and agents known to cause capacitation or acrosome reaction of eutherian spermatozoa. 184 24

A new approach to the assay of proteinases is described. The method relies on water-insoluble protein substrates, such as gluten and fibrin, which form expanded gels in the presence of sodium dodecyl sulfate (SDS) reagent. Powdered substrate is dispersed in buffer and aliquots are pipetted into long, narrow, 400-microliters tubes made of clear polypropylene. After the addition of enzyme and a period of incubation, a SDS reagent is added, the tubes are centrifuged, and the height of the SDS-protein gel is measured. Reduction of gel height gives a direct measure of enzyme activity. Salt concentration, pH, and incubation times must be consistent for both test and control reactions in order to obtain reproducible results. Examples of proteinases measured by this method are trypsin, chymotrypsin, elastase, pronase, papain, pepsin, an insect (Nysius huttoni) salivary proteinase, and wheat proteinase. The assay could detect enzyme in crude extracts or in purified form. In 1-h incubations, 10 ng of pepsin and elastase or 20 ng of purified insect proteinase could be detected. The assay was simple, fast, economical, and sensitive.
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PMID:General proteinase assay by formation of SDS-protein gels of proteolyzed substrate proteins. 195 67

The effect of ranitidine (20 mg . kg-1) and cimetidine (50 mg . kg-1) on pancreatic secretory and trophic responses to caerulein (1 microgram . kg-1) was studied in the rat. Ranitidine or cimetidine were administered alone or combined with caerulein twice a day for 7 days. Saline-treated rats were used as controls. At the end of treatment animals were anesthetized and pancreatic juice was collected for 1 h after intravenous secretin plus CCK-PZ (8 U . kg-1). Afterwards rats were sacrificed and growth and composition of pancreatic tissue were determined. Compared with control (saline) values, volume of pancreatic juice and output of trypsin and amylase were increased by treatment with caerulein. Ranitidine, when given combined with caerulein, completely abolished the secretory response induced by the peptide, whereas it was totally ineffective when given alone. Cimetidine (alone or combined with caerulein) was always ineffective. Caerulein increased pancreatic weight, total pancreatic trypsin, amylase and RNA content. Here again ranitidine, combined with caerulein, abolished almost completely the trophic effect of caerulein on the pancreas, but when given alone it did not influence pancreatic growth and composition. Also in this case, cimetidine was completely inactive. These results suggest that ranitidine affects exocrine pancreas with an action independent of the H2-receptor blockade.
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PMID:Inhibition of pancreatic secretory and trophic response to caerulein by the H2-receptor antagonist ranitidine in the rat. 240 51

This study deals with the stimulatory effect of caerulein on pancreatic and somatic growth in CFY suckling rats before weaning. After birth, caerulein (0.25, 0.5, 1, 3, 10 and 30 micrograms/kg) was given subcutaneously (s.c.) 3 times daily for 10 days. Saline-treated newborn rats were used as control. Caerulein increased pancreatic weight and total pancreatic trypsin activity reaching the maximum at 1 microgram/kg dose; higher doses did not cause higher values. On this basis 1 microgram/kg caerulein was applied s.c. 3 times daily for 3, 5, 10 and 20 days. At the end of the treatment pancreatic weight, total pancreatic protein, DNA content, trypsin and amylase activity was measured. Increases in body weight due to caerulein treatment were found from 6 days of treatment. Caerulein treatment increased pancreatic weight, total pancreatic DNA and protein content, and trypsin and amylase activity when applied for 5, 10 and 20 days. Treatment for 3, 5, 10 and 20 days with caerulein preferentially increased pancreatic trypsin activity compared to amylase activity. Trypsin activity per mg DNA increased with time in each caerulein-treated group demonstrating that the effect of caerulein increases with duration of treatment. In the saline-treated control group, however, pronounced increase in pancreatic amylase activity compared to that of trypsin activity was found in the age between days 11 and 21. This may be explained by the observation that the plasma corticosterone level increased during this period of postnatal life. The effect of caerulein in promoting pancreatic and somatic growth of suckling rats before weaning may be attributed to a specific enhancing effect of the peptide on proteolytic (e.g. trypsin) enzyme production of the pancreas.
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PMID:Caerulein stimulates pancreatic growth and somatic growth in suckling rats. 244 76

Thirty male Wistar rats were randomly divided into two groups. One group received 15% (vol/vol) ethanol as their only drinking solution for 12 weeks; the rest of the animals served as controls, receiving tap water only. Acute haemorrhagic pancreatitis (AHP) was induced with a retrograde infusion of 5% sodium taurocholate into the pancreatic ducts, and the generated peritoneal exudate was collected 5 h after induction. When compared with the water-receiving control rats, chronic ethanol ingestion decreased amylase activity (p less than 0.001) and trypsin-inhibiting capacity (TIC) (p less than 0.001), whereas protein concentration was increased (p less than 0.001) in the peritoneal exudate collected from the ethanol-receiving group. The toxicity of the peritoneal exudate was assessed by intraperitoneal injections of the exudate from rats into mice (n = 90). Saline or injections of the peritoneal exudate from the rats that received water did not kill any mice, and exudate from the rats that had been drinking the mixture of ethanol and water killed one mouse. In conclusion, chronic ethanol ingestion does not increase the toxicity of the peritoneal exudate secreted during AHP in this experimental model. In AHP, however, ethanol consumption increases protein concentration and decreases TIC in peritoneal exudate. Hence, the balance of the protease-antiprotease system may be of importance to the outcome of AHP.
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PMID:Long-term ethanol ingestion does not increase the toxicity of peritoneal exudate generated during acute haemorrhagic pancreatitis in rats. 244 64

The effect of equimolar doses (6 nmol/kg) of bombesin and its mammalian counterpart, GRP, on pancreatic growth and secretion was studied in adult rats. Both peptides were administered intraperitoneally three times a day for 5 consecutive days. Saline-treated rats were used as controls. At the end of the treatment, animals were anaesthetized and pancreatic juice was collected in basal conditions and after caerulein (0.75 nmol/kg i.p.) stimulation. Afterwards, the rats were sacrificed and growth and composition of the pancreatic tissue were determined. Compared with the control (saline) values, either basal or stimulated secretion was significantly increased after short-term treatment with both peptides. In addition, both bombesin and GRP increased pancreatic weight, total pancreatic protein, trypsin and amylase content. The DNA content was also increased by both peptides, although only the GRP effect proved to be significant. These results demonstrate that both bombesin and GRP have a growth-promoting effect on rat pancreas and concomitantly increase its secretory capacity. The mechanism of this peculiar biological action is likely to be connected with a direct stimulatory action on the gland.
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PMID:Effect of bombesin and its mammalian counterpart, GRP, on exocrine pancreas in the rat. 246 44

The effect of proglumide and lorglumide, two CCK-receptor antagonists, on caerulein-induced pancreatic secretion and growth was studied in the rat. In anaesthetised animals, caerulein (1 microgram/kg) significantly increased the volume of pancreatic juice and protein output. Lorglumide (5 and 10 mg/kg), administered intraperitoneally 15 min before stimulation, reduced peptide-induced pancreatic exocrine secretion. By contrast, proglumide (100 and 400 mg/kg) was completely ineffective. In experiments dealing with the trophic effect of caerulein, both drugs were administered alone or combined with the peptide (1 microgram/kg) 3 times daily for 5 d. Saline-treated rats served as controls. At the end of the experiment, rats were sacrificed, and growth and composition of pancreatic tissue were determined. Pretreatment of the animals with either proglumide or lorglumide did not affect pancreatic size and composition. Caerulein increased the weight of the pancreas, the total pancreatic protein, trypsin, amylase, and DNA content. After pretreatment with proglumide, all these parameters were not significantly different from those obtained with caerulein alone. In contrast, when lorglumide was given together with caerulein, it significantly reduced caerulein-induced pancreatic growth and decreased enzymatic protein content of the gland. These results show that lorglumide is a much more potent and effective CCK-receptor antagonist than proglumide. Its ability to antagonize the pancreatic secretory and trophic action of a CCK-analogue (i.e. caerulein) supports the view that these physiological actions of CCK are mediated through an interaction of the hormone with specific receptors.
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PMID:Pancreatic secretory and trophic response to caerulein in rats: effect of proglumide and lorglumide. 247 19

The ultrastructure of the peritrophic membrane of the female sandfly Phlebotomus papatasi has been studied at various times after blood meals. The membrane begins to form within four hours of the blood meal with the secretion by the entire midgut epithelium of an electron-dense amorphous material. Subsequently, the membrane is stabilized and strengthened by the production of a layer of irregular chitinous microfibres, the whole membrane then forming a complete and resilient sac apparently unaffected by boiling 9 M potassium hydroxide. The membrane appears redundant 48 hours after the blood meal and fragments, possibly as a result of chitinase activity. The membrane's main functions are probably the prevention of clogging of the microvillous brush border by the blood meal and the confinement of large proteins, particularly serum trypsin inhibitors, to the endoperitrophic space while allowing sandfly proteases access to the blood meal periphery. Blood is not required to stimulate membrane production. Saline taken by blood feeding into the midgut also stimulates membrane formation. Phlebotomus papatasi females may lack an efficient anticoagulant, at least in the midgut, as blood meals frequently include fibrin clots.
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PMID:The peritrophic membrane of the female sandfly Phlebotomus papatasi. 325 79

The human colon adenocarcinoma cell line HT 29 grows virtually without tight junctions (TJ) under standard culture conditions. Earlier studies have shown that focal TJ (fasciae occludentes) can be rapidly assembled in this cell line under the influence of various proteases. Here we show that focal TJ can be induced in this cell line by a brief treatment with appropriate salt solutions. Induction by ammonium sulfate in Hanks' buffer reached a maximum value after 15 to 30 min. The amount of TJ increased with the salt concentration and reached a plateau value at a concentration of 160 mM ammonium sulfate. The amount and complexity of TJ induced by ammonium sulfate were similar to those in experiments using trypsin as inducing agent as shown by morphometric analysis. At 0 degrees C, no TJ were formed under the influence of the salt. A comparative study of TJ induction using a variety of inorganic and organic salts gave the following results. All alkali sulfates induced TJ, although with different yield. Both calcium and magnesium chloride were potent inducers. Ammonium and sodium salts encompassing a variety of anions covered a wide range from maximum induction (sulfate, citrate) to almost complete absence of induction (nitrate). Sodium chloride did not induce any TJ. It follows that the induction of TJ is a specific effect of individual ionic components of the solution as opposed to a general effect of osmolarity and ionic strength. The data suggest tentatively that antichaotropic but not chaotropic ions have the potential to trigger the formation of TJ in this experimental system.
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PMID:Rapid formation of tight junctions in HT 29 human adenocarcinoma cells by hypertonic salt solutions. 339 Dec 41


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