Human cationic, pancreatic elastase in acute pancreatitis

Area of Science:

• Biochemistry
• Gastroenterology
• Enzymology

Background:

• Severe acute pancreatitis involves pancreatic enzyme activation and release.
• Understanding the behavior of pancreatic elastase in this condition is crucial for diagnosis and treatment.
• Pancreatic cationic elastase (irPE) is a key enzyme implicated in pancreatitis pathogenesis.

Purpose of the Study:

• To investigate the molecular forms and inhibitor complexes of immunoreactive cationic pancreatic elastase (irPE) in patients with severe acute pancreatitis.
• To determine the presence and activity of free and bound pancreatic elastase in serum and peritoneal exudates.

Main Methods:

• Analysis of serum and peritoneal exudate samples from 8 patients with severe acute pancreatitis.
• Immunoreactive assays to detect pancreatic elastase (irPE).
• Assessment of inhibitor complexes (alpha-1-proteinase-inhibitor and alpha-2-macroglobulin) and elastase-like activity.

Main Results:

• Immunoreactive cationic pancreatic elastase (irPE) was predominantly found complexed with alpha-1-proteinase-inhibitor (alpha 1PI) in serum and peritoneal exudates.
• Minor quantities of irPE existed as free proenzyme.
• Alpha-2-macroglobulin (alpha 2M)-bound elastase-like activity was detected in exudates, indicating active elastase binding.
• No free elastolytic activity was found in the exudates.

Conclusions:

• Pancreatic cationic elastase is released, at least partially as active enzyme, during severe acute pancreatitis.
• The released active elastase is rapidly complexed with inhibitors, primarily alpha-1-proteinase-inhibitor (alpha 1PI).
• The absence of free elastolytic activity suggests effective inhibition in the affected compartments.