Release of Proteolytic Enzymes in Bile-Induced Pancreatitis in Dogs

Ohlsson, Kjell; Eddeland, Allan

doi:10.1016/s0016-5085(19)32469-2

Cited by 55 publications

(10 citation statements)

References 18 publications

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“…Pancreatitis was induced as described earlier by infusion of 0.5 ml/ kg body weight of autologous bile at a pressure higher than 50 cm HzO into the main pancreatic duct under laparotomy (20). In one group of five dogs 20 mg/kg body weight of rhPSTI in 2.0 ml of saline was injected immediately before the bile.…”

Section: Methodsmentioning

confidence: 99%

Local Administration of Human Pancreatic Secretory Trypsin Inhibitor Prevents the Development of Experimental Acute Pancreatitis in Rats and Dogs

Ohlsson

Olsson

Björk

et al. 1989

Scandinavian Journal of Gastroenterology

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The objective of this investigation was to test the capacity of recombinant human pancreatic secretory trypsin inhibitor (rhPSTI) to provide prophylaxis against experimental pancreatitis. Acute hemorrhagic pancreatitis was induced by intraductal injection of sodium taurocholate in rats and by intraductal injection of bile in dogs. In one treatment group of rats the injection of taurocholate was preceded by injection of rhPSTI. In a second group of rats the rhPSTI was given intraperitoneally starting 15 min after the induction of acute pancreatitis. The survival rate in a control group of rats was 13%. In contrast, the survival rate in groups receiving rhPSTI intraductally or intraperitoneally was 80% and 63%, respectively. The survival rate in a control group of dogs was 40% at 24 h and 0% at 48 h. In contrast, all the dogs receiving a single intraductal dose of rhPSTI, either immediately before the bile injection or mixed with the bile, survived for up to 6 weeks. Detailed biochemical and immunohistologic studies in the dog indicate that, whereas rhPSTI cannot prevent the initial bile-induced injury, it does prevent the subsequent development of that injury to the point where there is massive damage to the pancreas and the surrounding tissues, and changes in blood chemistry. The development of the initial injury is, therefore, presumed to involve activation of trypsinogen. Since rhPSTI prevents the serious consequences of experimental pancreatic injury by blocking the action of trypsin, and since the pathobiochemistry of human acute pancreatitis also implies an important role for trypsin, it is possible that rhPSTI could protect humans from the pancreatitis that complicates endoscopic retrograde cholangiopancreatography and endoscopic papillotomy.

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Section: Methodsmentioning

confidence: 99%

Local Administration of Human Pancreatic Secretory Trypsin Inhibitor Prevents the Development of Experimental Acute Pancreatitis in Rats and Dogs

Ohlsson

Olsson

Björk

et al. 1989

Scandinavian Journal of Gastroenterology

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“…The exocrine pancreas is the main organic source of trypsinogen and trypsin (1,18). Therefore, pancreatic alterations have significant implications for production and degradation of trypsinogen and trypsin (5-7).…”

Section: Discussionmentioning

confidence: 99%

Determination of Plasma Trypsin-Like Activity in Healthy Subjects, Patients With Mild to Moderate Alcoholic Chronic Pancreatitis, and Patients With Nonjaundice Pancreatic Cancer

et al. 2005

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Trypsin-like activity is released after stimulation of the exocrine pancreas. We investigated under basal conditions and after stimulation by a meal whether patients suffering from pancreatic disorders differ with respect to plasma trypsin-like activity (PTLA). In 45 subjects (healthy volunteers: n = 18, mild/moderate alcoholic chronic pancreatitis: n = 16, nonjaundice pancreatic cancer n = 7, and calcifying chronic pancreatitis: n = 4), basal and postprandial levels of PTLA were measured over a period of 2 hours. Basal plasma levels were similar in the first 3 groups. After stimulation, healthy volunteers and patients with pancreatic cancer showed significant decreases in trypsin-like activity; however, plasma levels did not decrease in patients with mild/moderate chronic pancreatitis (P < .001). Healthy individuals demonstrate a consistent decrease in postprandial trypsin-like plasma activity. This response is not altered in patients with pancreatic cancer, and it is not seen in patients with mild/moderate alcoholic chronic pancreatitis.

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“…This conclusion is further strengthened by the earlier finding of large amounts of pancreatic proteases in complex with «! -antitrypsin in ascitic fluid from dogs with bileinduced pancreatitisl 16 !.…”

Section: Discussionmentioning

confidence: 99%

Immunoreactive Trypsins in Sera from Dogs Before and After Induction of Experimental Pancreatitis

Borgström¹,

Ohlsson²

1980

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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Radioimmunoassays for anionic and cationic dog trypsins are described. Characterization of the immunoreactivities in sera from fasting dogs demonstrated the presence of the two proenzymes only. Fasting sera from 10 dogs contained anionic and cationic trypsinogen in concentrations between 17-110 §// and 7-19 ßg/l, respectively. Induction of experimental pancreatitis in dogs was accompanied by a large increase of immunoreactive anionic and cationic trypsins in the circulation. During the progress of the pancreatitis, immunoreactive trypsin with larger molecular weight than trypsinogen appeared. This high molecular weight immunoreactive trypsin was not seen in serum after intravenous injection of pancreatic juice in dogs. The high molecular weight immunoreactive trypsin probably consists of trypsin in complex with protease inhibitors. In vitro studies showed that the immunoreactivity of trypsin decreased considerably after binding to cq-antitrypsin or a-macroglobulins. Immunreaktive Trypsine im Serum des Hundes vor und nach Induktion einer experimentellen PankreatitisZusammenfassung: Es werden Radioimmuntests für anionische und kationische Hunde-Trypsine beschrieben. Im Serum fastender Hunde konnte durch eine Charakterisierung der Immunreaktivitäten nur das Vorkommen der beiden Proenzyme nachgewiesen werden. Von 10 fastenden Hunden enthielten die Seren anionisches und kationisches Trypsinogen in Konzentrationen von -10 g// bzw. 7-19 g//. Die Induktion einer experimentellen Pankreatitis war von einem starken Anstieg des immunreaktiven anionischen und kationischen Trypsins im Kreislauf begleitet. Mit fortschreitender Pankreatitis tauchte immunreaktives Trypsin mit einem größeren Molekulargewicht als Trypsinogen auf. Dieses hochmolekulare immunreaktive Trypsin wurde nach intravenöser Injektion vonPankreassaftnicht beobachtet. Es stellt möglicherweise Komplexe aus Trypsin und Proteaseinhibitoren dar. In-vitro-Untersuchungen zeigten, daß die Immunreaktivität von Trypsin nach Bindung an aj-Antitrypsin oder a-Makroglobulin bedeutend abnahm.

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Release of Proteolytic Enzymes in Bile-Induced Pancreatitis in Dogs

Cited by 55 publications

References 18 publications

Local Administration of Human Pancreatic Secretory Trypsin Inhibitor Prevents the Development of Experimental Acute Pancreatitis in Rats and Dogs

Local Administration of Human Pancreatic Secretory Trypsin Inhibitor Prevents the Development of Experimental Acute Pancreatitis in Rats and Dogs

Determination of Plasma Trypsin-Like Activity in Healthy Subjects, Patients With Mild to Moderate Alcoholic Chronic Pancreatitis, and Patients With Nonjaundice Pancreatic Cancer

Immunoreactive Trypsins in Sera from Dogs Before and After Induction of Experimental Pancreatitis

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