Effects of urinary trypsin inhibitor on pancreatic enzymes and experimental acute pancreatitis.

Abstract

Therapeutic effect and the mechanism of the action of human urinary trypsin inhibitor (MTI) on experimental acute pancreatitis were studied. MTI significantly increased survival rate of animals with experimental acute pancreatitis induced by the infusion of trypsin or phospholipase A2 into pancreas or by a closed duodenal loop. The efficacy of MTI on these types of pancreatitis were higher than those of aprotinin. Pancreatic enzymes were released from pancreatic slice by trypsin or phospholipase A2, and this release was inhibited by MTI. Further, these pancreatic enzymes caused a secondary release of enzymes from other pancreatic slice, suggesting that these enzymes injured pancreatic tissue and that a chain reaction of pancreatic enzyme activation may play an important role in the pathogenesis of acute pancreatitis. MTI suppressed the secondary enzyme-induced pancreatic injury more strongly than aprotinin. These results suggest that MTI may suppress pathogenesis and development of pancreatitis by inhibiting the chain reaction of pancreatic enzyme activation.

• Authors: H Ohnishi, H Kosuzume, Y Ashida, K Kato, I Honjo
• Journal: Digestive diseases and sciences (Dig Dis Sci) Vol. 29 Issue 1 Pg. 26-32 (Jan 1984) ISSN: 0163-2116 [Print] United States
• PMID: 6363018 (Publication Type: Journal Article)

Chemical References

• Glycoproteins
• Phospholipases A
• Phospholipases A2
• Peptide Hydrolases
• Trypsin
• urinastatin

Topics

• Acute Disease
• Animals
• Glycoproteins (pharmacology)
• Male
• Pancreas (enzymology)
• Pancreatitis (chemically induced, prevention & control)
• Peptide Hydrolases (metabolism)
• Phospholipases A
• Phospholipases A2
• Rats
• Rats, Inbred Strains
• Trypsin