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  • 1
    Electronic Resource
    Electronic Resource
    General and selective inhibition of pancreatic enzyme discharge using a proteinase inhibitor (FOY-305) (1984)
    Springer
    Journal of molecular medicine 62 (1984), S. 406-411 
    Details
    ISSN: 1432-1440
    Keywords: Pancreatic secretion ; Intracellular transport ; Proteinase inhibitor ; Two-dimensional gel electrophoresis ; FOY-305
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01742297
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  • 2
    Electronic Resource
    Electronic Resource
    Tissue-type transglutaminase expression in the Dunning tumor (1993)
    Springer
    Urological research 21 (1993), S. 9-15 
    Details
    ISSN: 1434-0879
    Keywords: Dorsal prostate ; Enzyme activity ; Immunohistochemistry ; Mammary gland ; Secretory transglutaminase ; Tissue-type transglutaminase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Transglutaminases with different functions and tissue distribution patterns can be distinguished by specific antibodies and by inhibition of enzyme activity in the presence of guanosine triphosphate (GTP). The most common form is the so-called tissue-type transglutaminase that is apparently involved in membrane, stabilization processes, e.g. during apoptosis, and can be inhibited by incubation with GTP at low calcium concentrations. A secretory transglutaminase that cannot be inhibited by GTP is synthesized in an androgen-dependent manner in the dorsal prostate of the rat, the site suggested to represent the origin of the Dunning tumor used as an experimental model in prostate cancer research. Here we studied the expression of transglutaminases in different Dunning tumor lines — mainly in the highly differentiated H subline - and characterized the enzyme both biochemically and immunocytochemically. A very high enzyme activity was found only in the less well differentiated HI-F tumor line. Immunohistochemical reactions and Western blot analysis showed that there is no secretory transglutaminase present in any of the Dunning tumor lines studied. Transglutaminase activity of the Dunning tumor results from the so-called tissue-type enzyme that is nonorgan specific. The absence of a secretory form of transglutaminase does not suport the contention of a prostatic origin o the Dunning tumor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00295185
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  • 3
    Electronic Resource
    Electronic Resource
    Immunological characterization and activity of transglutaminases in human normal and malignant prostate and in prostate cancer cell lines (1995)
    Springer
    Urological research 23 (1995), S. 301-310 
    Details
    ISSN: 1434-0879
    Keywords: Transglutaminases ; Prostate cancer ; Metastasis ; Cellular wound repair
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Using biochemical assays, we compared enzyme activities with the immunoreactivity of antibodies against rat seminal transglutaminase (TGase), human erythrocyte TGase and guinea pig liver TGase in human normal prostate, primary prostatic carcinomas and prostatic carcinoma cell lines. Glandular cells of the epithelium were only exceptionally positive with the antibody against (rat) secretory TGase. Using the antibodies against tissue-type TGase, most immunoreactive cells were found in the basal cell layer of prostatic epithelium as well as in stroma (fibroblasts, endothelial cells), whereas immunoreactive glandular cells were sparse. In the case of benign prostatic hyperplasia, few, irregularly distributed secretory cells along with a small number of stromal cells were also immunoreactive with the tissue-type TGase antibody. In dedifferentiated carcinomas, immunoreactive cells were nearly completely absent. Of the prostate cancer cell lines, the LNCaP line showed neither TGase enzyme activity nor immunoreactivity, whereas the PC-3 cell line displayed significant enzyme activity and immunoreactivity. No hormone-dependent changes in either enzyme activity or immunoreactivity were recorded after in vitro treatment of the respective cell lines with estrogens, androgens and antiandrogens. As there is no correlation between androgen deprivation and TGase expression in nonmalignant and malignant human prostatic epithelial cells, TGase activity more likely indicates cellular lesions and consecutive repair mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00300018
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  • 4
    Electronic Resource
    Electronic Resource
    Purification of glycollate oxidase from greening cucumber cotyledons (1982)
    Springer
    Planta 156 (1982), S. 566-571 
    Details
    ISSN: 1432-2048
    Keywords: Cucumis ; Glycollate oxidase (purification) ; Peroxisome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Glycollate oxidase (glycollate: oxygen oxidoreductase, EC 1.1.3.1) was purified to apparent homogeneity from crude extracts of greening cucumber cotyledons (Cucumis sat vus). Molecular sieving and chromatofocusing resulted in 700-fold purification and specific activity of 1 μkat mg-1 protein. The enzyme exhibited a Mr of 180,000, or 700,000, respectively, and is a tetramer or 16-mer made of identical subunits of Mr 43,000. Monospecific antibodies were raised against the homogeneous protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392782
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  • 5
    Electronic Resource
    Electronic Resource
    Stimulation of pancreatic secretory process in the rat by low-molecular weight proteinase inhibitor (1987)
    Springer
    Cell & tissue research 247 (1987), S. 187-193 
    Details
    ISSN: 1432-0878
    Keywords: Exocrine pancreas ; Proteinase inhibitor ; Feedback regulation ; Cholecystokinin ; Fine structure ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Application of a single dose of a new type of proteinase inhibitor camostate (FOY-305) via orogastric tube was used in rats to study the dose-response relationship of resulting pancreatic stimulation. Doses up to 10 mg/ kg failed to elicit any response, while significant decrease in enzyme content and increase in serum CCK-levels were observed with doses ranging from 25 to 400 mg/kg. A single dose of 100 mg/kg was selected for a time-sequence analysis, which revealed a 60 to 70% depletion of enzyme stores persisting over 6 h and reverting to control levels by 12 h. Peak increases in serum CCK-levels (15-fold above the elevation observed after regular food intake) were found after 30 min and persisted as an 8-to 10-fold elevation for at least 3 h, then declined to control levels by 9 h. This prolonged endogenous hormone release and resulting pancreatic stimulation were also verified in a separate group of animals in which volume, protein, and enzyme output were measured after cannulation of the pancreatic duct. While volume secretion was not altered by feeding a single dose of 100 mg/kg FOY-305, protein and enzyme output increased 2-to 3-fold over a period of 7 h. Fine-structural analysis of the pancreas demonstrated efficient depletion of zymogen granules from acinar cells with all doses between 50 and 400 mg/kg, accompanied by the appearance of membrane material in the acinar lumina at 3 and 6 h. The same transient increase in the number of lysosomal bodies predominantly containing mitochondria with all doses above 50 mg/kg was interpreted as increased organelle turnover due to persisting hormonal stimulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00216561
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  • 6
    Electronic Resource
    Electronic Resource
    In-vivo stimulation of rat pancreatic acinar cells by infusion of secretin (1985)
    Springer
    Cell & tissue research 242 (1985), S. 633-639 
    Details
    ISSN: 1432-0878
    Keywords: Secretin ; Pancreas ; Enzyme secretion ; Protein synthesis ; Fine structure ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Infusion of synthetic secretin in conscious unrestricted rats for periods up to 24 h was used to study the structural and functional adaptation of pancreatic acinar cells to this secretagogue. Initial dose-response studies established 16 clinical units (CU) per kg and h (corresponding to 4.64 ug x kg-1 x h-1) as optimal dose for persistent stimulation of enzyme discharge. Infusion of this dose led to a slow but progressive depletion of enzyme stores with minimal content by 12 h stimulation. As a result of persistent stimulation total protein synthesis in the acinar cells increased after a lag period of 3 h and reached maximal values 90% above controls by 6 and 12 h secretin infusion. No structural equivalent for pronounced fluid and bicarbonate secretion was observed for either acinar or duct cells over the entire dose range (1 to 64 CU x kg-1 x h-1) and infusion period (1–24 h), except an increased number of coated vesicles in duct cells. Discharge of enzymes from acinar cells was paralleled by a high frequency of exocytotic images at the luminal plasma membrane and was accompanied by the occurrence of membrane fragments in the luminal space, especially after 3 and 6 h secretin infusion. An increased number of lysosomal bodies at these time points especially in the vicinity of the Golgi complex was interpreted in relation to membrane recycling following massive exocytosis. This pattern of structural and functional adaptation of acinar cells following secretin infusion corresponds to previously described changes following caerulein and carbamylcholine stimulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225430
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  • 7
    Electronic Resource
    Electronic Resource
    Stimulation of pancreatic secretory process in the rat by low-molecular weight proteinase inhibitor (1987)
    Springer
    Cell & tissue research 249 (1987), S. 63-67 
    Details
    ISSN: 1432-0878
    Keywords: Exocrine pancreas ; Proteinase inhibitor ; Cholecystokinin ; Protein synthesis ; Enzyme synthesis ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 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 15h. 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00215419
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  • 8
    Electronic Resource
    Electronic Resource
    In-vivo stimulation of rat pancreatic acinar cells by infusion of secretin (1985)
    Springer
    Cell & tissue research 242 (1985), S. 641-644 
    Details
    ISSN: 1432-0878
    Keywords: Secretin ; Pancreas ; Protein synthesis ; Enzyme synthesis ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Intravenous infusion of synthetic secretin for periods up to 24 h in conscious rats was combined with invitro amino acid incorporation in isolated pancreatic lobules and high-resolution separation of individual enzyme proteins by two-dimensional isoelectric focusing and SDS gel electrophoresis. With this method persistent changes in the biosynthesis of ten enzyme and isoenzyme proteins can be studied as a result of prolonged secretin stimulation. Three major patterns of response were observed: progressive increases in the synthetic rates were found in six out of ten enzyme proteins with most pronounced changes in the synthetic rates of lipase (4.10-fold increase), two forms of proelastase (2.80-fold increase, respectively), the two acidic forms of trypsinogen and chymotrypsinogen (2.60-and 2.40-fold increase, respectively), and of ribonuclease (2.30-fold increase). Only moderate changes (1.30- to 1.90-fold increase) occured in the synthetic rates of four isoenzymatic forms of procarboxypeptidase and the basic forms of chymotrypsinogen and trypsinogen, respectively. No absolute change in the rate of synthesis was observed in both forms of amylase. These data obtained after secretin stimulation differ significantly from previous results after caerulein stimulation, but it is not clear so far whether this is due to differential effects of the two second messengers released by each of the hormones on the level of transcription or translation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225431
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