trypsinogen and camostat

trypsinogen has been researched along with camostat* in 2 studies

Other Studies

2 other study(ies) available for trypsinogen and camostat

ArticleYear
Stimulation of pancreatic secretory process in the rat by low-molecular weight proteinase inhibitor. II. Regulation of total protein and individual enzyme biosynthesis.
    Cell and tissue research, 1987, Volume: 249, Issue:1

    Oral application of a single dose of a new synthetic proteinase inhibitor Camostate (Foy-305) in male Wistar rats was carried out together with studies of in vitro amino acid incorporation followed by separation of proteins by two-dimensional gel electrophoresis. The aim of this experiment was to analyze changes produced by the inhibitor in total protein and individual enzyme biosynthesis. Administration of 100 mg/kg Foy-305 resulted in significant inhibition of total pancreatic protein synthesis, without changes in fractional rates for individual enzymes. 50 mg/kg Foy-305 induced a 10-fold elevation of cholecystokinin (CCK) levels in serum; this persisted for 3 h and led to a significant increase in the total rate of protein synthesis with peak values at 6 and 9 h (78% and 84% above control levels, respectively), returning to control by 15 h. Changes in fractional rates of synthesis occurred with a latency of 6 h and were restricted to amylase and the anionic form of trypsinogen and chymotrypsinogen. Amylase biosynthesis decreased by about 40% from control levels at 9 h to return to control levels by 15 h. Increased synthesis of trypsinogen and chymotrypsinogen was observed; this was also phasic. The results show similar enzyme-specific regulation as previously described for exogenous CCK stimulation and for the adaptation of the pancreas to diets enriched in protein. They demonstrate the effectiveness of pulsatory endogenous hormone release in the regulation of protein synthesis.

    Topics: Amylases; Animals; Chymotrypsinogen; Esters; Gabexate; Guanidines; Kinetics; Lipase; Male; Pancreas; Protease Inhibitors; Protein Biosynthesis; Rats; Rats, Inbred Strains; Trypsinogen

1987
General and selective inhibition of pancreatic enzyme discharge using a proteinase inhibitor (FOY-305).
    Klinische Wochenschrift, 1984, May-02, Volume: 62, Issue:9

    The guanidino acid esters (FOY, FOY-305) represent a new class of potent proteinase inhibitors and are thought to have a beneficial effect on the course of acute pancreatitis. Because of their structure and low molecular size they might enter cells and interfere with cellular processes. To test this possibility in the case of the exocrine pancreas a series of in vivo and in vitro studies was carried out to analyse intracellular transport and discharge of pancreatic enzymes in the presence of FOY-305. The infusion of FOY-305 to conscious rats led to a transient inhibition of protein and enzyme discharge from the cannulated pancreas accompanied by lower serum enzyme levels and increased enzyme content in the pancreas. An identical inhibition of discharge of newly synthesized proteins was observed in vitro in the presence of 1 microM FOY-305. The analysis of the release of individual enzymes using separation on two-dimensional gels showed a pronounced inhibition of mainly the release of acidic proteins. FOY-305 not only interfered with discharge of serine proteinases (trypsinogen, chymotrypsinogen, proelastase) but also with procarboxypeptidases and lipase. It was concluded that FOY-305 enters the acinar cell and due to an unspecific binding to acidic proteins interferes with the intracellular transport of individual enzyme proteins during their passage through the membrane-bound cellular compartments. This charge-dependent effect is independent of the inhibitory effect on enzymatic activity of serine proteinases.

    Topics: Amylases; Animals; Carboxypeptidases; Carboxypeptidases A; Chymotrypsinogen; Enzyme Precursors; Esters; Gabexate; Guanidines; Lipase; Male; Pancreas; Pancreatic Elastase; Protease Inhibitors; Rats; Rats, Inbred Strains; Trypsinogen

1984