Pankreaselastase

Pankreaselastase, known in English as pancreatic elastase, is a digestive serine protease produced by the pancreatic acinar cells. It is secreted into the small intestine as proelastase and activated by trypsin in the duodenum. The enzyme cleaves elastin, a major structural protein in connective tissue, contributing to protein digestion alongside other pancreatic proteases.

Pancreatic elastase-1 (PE-1) is commonly measured in stool as a non-invasive marker of pancreatic exocrine function. The fecal elastase-1 test uses an immunoassay to quantify elastase-1 in stool; values are relatively stable during intestinal transit because the enzyme resists degradation. Normal fecal elastase-1 levels are typically above roughly 200 micrograms per gram of stool. Reduced levels indicate pancreatic exocrine insufficiency, which can result from chronic pancreatitis, cystic fibrosis, or pancreatic duct obstruction. The test is less reliable for mild insufficiency and is not routinely used to diagnose acute pancreatitis. It may be influenced by very watery stools or low stool mass.

Replacement therapy with pancreatic enzymes does not directly increase measured elastase-1 in stool, since the assay detects endogenous elastase-1.