pancreatitis/protease

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Proteases and protease inhibitors in cerulein-induced acute pancreatitis in rats.

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BACKGROUND Proteases and protease inhibitors are important in acute pancreatitis (AP), although little is known about the time course in cerulein-induced AP in the rat. METHODS AP was induced by supramaximal stimulation of cerulein, 10 microgram/kg/h, and during 72 h we measured lipase, amylase,

Evidence of intracellular activation of serine proteases in acute cerulein-induced pancreatitis in rats.

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It is believed that activation of zymogen proteases occurs in the early development of acute pancreatitis. This hypothesis was proved on subcellular fractions of rat pancreas after induction of pancreatitis by infusion of high doses of cerulein for 2 h. Secretory enzyme activities were measured

Protease-activated receptor-2 protects against pancreatitis by stimulating exocrine secretion.

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BACKGROUND Protease-activated receptor-2 (PAR-2) is present in the pancreas, where it has been shown to play a protective role during pancreatitis. However, the mechanism by which it protects against pancreatitis still remains to be elucidated. Acute pancreatitis is associated with premature zymogen

Compartmentalization of the protease-antiprotease balance in early severe acute pancreatitis.

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OBJECTIVE To assess the balance between trypsin and protease inhibitors simultaneously in the systemic circulation and in the thoracic lymph and peritoneal exudate. METHODS Twenty patients with early severe acute pancreatitis were studied. Enzymatically active and immunoreactive trypsin in

[Role of protease activation in pathophysiology of acute pancreatitis].

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For over a century it has been assumed that acute pancreatitis represents an autodigestion of the pancreas by its own, physiologically inactive proteases. Whether, how and where digestive proteases are being activated in the pancreas has remained the topic of much controversy and speculation. We

Levels of leukocyte proteases in plasma and peritoneal exudate in severe, acute pancreatitis.

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Levels of leukocyte elastase and neutrophil protease 4 (NP4(3)) in plasma and peritoneal exudate were studied in 25 patients with severe, acute pancreatitis. Pancreatitis was diagnosed from the clinical picture and an increased serum amylase level. The diagnosis was verified by computerized

Immunoenzymometric determination of trypsin/alpha 1-protease inhibitor complex in plasma of rats with experimental pancreatitis.

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The currently available radioimmunoassays of trypsin measure total immunoreactive trypsin (EC 3.1.1.7), which includes both trypsinogen and alpha 1-protease inhibitor-bound trypsin. Hitherto, the only way to differentiate these two forms of trypsin has been to fractionate them on a gel-filtration

Serum protease inhibitor capacity for elastase and the severity of pancreatitis.

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To clarify the relationship between the diminution of the serum protease inhibitor capacity and the severity of pancreatitis, the binding capacity of serum protease inhibitors for exogenous elastase 1 (E1) was investigated by gel filtration, the elastase activity of the alpha 2-macroglobulin (alpha

Trypsin-alpha 1-protease inhibitor complexes in serum and clinical course of acute pancreatitis.

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The levels of amylase, trypsinogen, and trypsin-alpha 1-protease inhibitor complexes, both in serum and in peritoneal fluid, were correlated to the severity and clinical course in 27 attacks of acute pancreatitis. Serum levels of trypsin-alpha 1-protease inhibitor complexes on admission correlated

Degradation and inactivation of plasma tumor necrosis factor-alpha by pancreatic proteases in experimental acute pancreatitis.

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BACKGROUND Release of TNFalpha is thought to play an important role in mediating systemic effects in acute pancreatitis (AP). We have been unable to find an elevation of plasma TNFalpha in AP and hypothesize that it is susceptible to catabolism by circulating pancreatic proteases. METHODS (1) AP was

Treatment of acute pancreatitis with protease inhibitors: a meta-analysis.

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OBJECTIVE Protease inhibitors are used to treat acute pancreatitis, but their effectiveness remains unclear. We performed a meta-analysis to determine whether treatment with protease inhibitors reduces overall mortality or morbidity from acute pancreatitis. METHODS Articles of randomized controlled

Loss of chymotrypsin-like protease (CTRL) alters intrapancreatic protease activation but not pancreatitis severity in mice

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The digestive enzyme chymotrypsin protects the pancreas against pancreatitis by reducing harmful trypsin activity. Genetic deficiency in chymotrypsin increases pancreatitis risk in humans and pancreatitis severity in mice. Pancreatic chymotrypsin is produced in multiple isoforms including

[Protease inhibitors as immunomodulators in experimental acute pancreatitis and staphylococcal infection].

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The influence of protease-inhibiting preparations on the development of humoral immune response in diseases involving the development of secondary immunodeficiency (experimentally induced acute pancreatitis and staphylococcal infection) has been studied. Five injections of contrycal and

Peritoneal lavage efficiently eliminates protease-alpha-2-macroglobulin complexes and components of the contact system from the peritoneal cavity in patients with severe acute pancreatitis.

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Trypsin (Try), plasma kallikrein (KK) and plasmin activities together with coagulation factor XII (F XII, Hageman factor), high-molecular-weight kininogen (HMWK), plasma prekallikrein (PKK), alpha 2-macroglobulin (alpha 2-M), C1 inhibitor (C1Inh), and functional plasma kallikrein inhibition (KKI)

[Effect of continuous arterial infusion of protease inhibitor on experimental acute pancreatitis induced by closed duodenal loop obstruction].

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The effectiveness of continuous arterial infusion of protease inhibitor on acute experimental pancreatitis was investigated. Acute hemorrhagic pancreatitis was induced by closed duodenal loop obstruction using mongrel dogs. The obstruction was released at 16 hr, and dogs were divided into three

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