Journal ArticleDOI
General and selective inhibition of pancreatic enzyme discharge using a proteinase inhibitor (FOY-305).
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TLDR
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.Abstract:
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 µM 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.read more
Citations
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Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.
TL;DR: The results suggest that the endosomal pathway is disadvantageous for HCoV-229E infection of human airway epithelial cells; therefore, clinical isolates are less able to use cathepsin.
Journal ArticleDOI
Heavy chain binding protein (BiP/GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase.
Hiroto Takemoto,Tamotsu Yoshimori,Akitsugu Yamamoto,Yoshihiko Miyata,Ichiro Yahara,Kyoichi Inoue,Yutaka Tashiro +6 more
TL;DR: It is strongly suggested that in rat exocrine pancreatic cells PDI and the other KDEL-bearing proteins found in the extracellular space were not artificially released by cell damage during incubation but were secreted via the normal secretory pathway.
Journal ArticleDOI
Differential effects of atropine and a cholecystokinin receptor antagonist on pancreatic secretion
Guido Adler,Guido Adler,Max Reinshagen,Max Reinshagen,Irmtraut Koop,Irmtraut Koop,Burkhard Göke,Burkhard Göke,Anton Schafmayer,Anton Schafmayer,Lucio C. Rovati,Lucio C. Rovati,Rudolf Arnold,Rudolf Arnold +13 more
TL;DR: It is suggested that the protease inhibitor camostate, by inhibition of the enzymatic activity of trypsin and chymotrypsin, interferes with feedback regulation of basal pancreatic secretion in humans, and this mechanism is predominantly mediated by the cholinergic system.
Journal ArticleDOI
Stimulation of pancreatic secretion in man by a protease inhibitor (camostate).
Guido Adler,A. Müllenhoff,I. Koop,T. Bozkurt,Burkhard Göke,Christoph Beglinger,Rudolf Arnold +6 more
TL;DR: It is suggested that trypsin and chymotrypsin are involved in feedback regulation of pancreatic secretion in man which is, however, not mediated by CCK or secretin.
Journal ArticleDOI
Stimulation of pancreatic secretory process in the rat by low-molecular weight proteinase inhibitor. I. Dose-response study on enzyme content and secretion, cholecystokinin release and pancreatic fine structure.
TL;DR: Application of a single dose of a new type of proteinase inhibitor camostate via orogastric tube was used in rats to study the dose-response relationship of resulting pancreatic stimulation and transient increase in the number of lysosomal bodies predominantly containing mitochondria was interpreted as increased organelle turnover due to persisting hormonal stimulation.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin.
TL;DR: The spectrophotometric procedure proposed by Schwert and Takenaka has been modified and extended to include the application to N-benzoyl-L-tyrosine ethyl ester and α-p-toluenesulphonyl- L-arginine methyl ester, allowing the determination of traces of chymotrypsin in the presence of relatively large amounts of trypsin.
Journal ArticleDOI
Modifications of the diphenylamine reaction giving increased sensitivity and simplicity in the estimation of DNA
TL;DR: A modification of the diphenylamine procedure of Giles and Myers (2) is described which has 30% higher sensitivity and a lower reagent blank than the parent procedure, and is more conveniently carried out.
Journal ArticleDOI
Two-dimensional gel analysis of soluble proteins. Charaterization of guinea pig exocrine pancreatic proteins.
TL;DR: A two-dimensional gel technique using slab gel isoelectric focusing in the first dimension and sodium dodecyl sulfate gradient gel electrophoresis in the second dimension has been developed for the separation of soluble proteins larger than 10,000 daltons.