Pancreatic elastase (PE)

Pancreatic elastase is a serine endopeptidase produced by pancreatic acinar cells and released into the small intestine as an inactive zymogen before activation by trypsin[1][2][7]. It plays a critical role in digestion by cleaving peptide bonds after small neutral amino acids such as alanine, showing specific activity towards elastin and other matrix proteins[1][2]. Pancreatic elastase is a compact globular protein comprised of a single chain (240 amino acids in human/porcine forms), containing a catalytic triad typical of serine proteases[1][2]. Fecal pancreatic elastase-1 is a widely used, non-invasive biomarker for assessing exocrine pancreatic function, particularly in identifying exocrine insufficiency due to chronic pancreatitis, cystic fibrosis, pancreatic carcinoma, and other disorders, with measurement via standardized ELISA in stool[7]. The enzyme is essential for proper nutrient absorption; its deficiency leads to maldigestion and malabsorption syndromes, requiring therapeutic enzyme replacement[4][7]. While commonly called "pancreatic elastase," various highly homologous isoforms and nomenclature confusion have existed; the diagnostically relevant human isoform is chymotrypsin-like elastase family member 3B (CELA3B), but the term still refers broadly to the digestive enzyme measured in feces[1].

Other names

elastase-1pancreatopeptidaseserine elastaseELA1chymotrypsin-like elastase family, member 1 (CELA1)elastase (generic, refers also to other elastases)

Enzymatic cleavage of dietary proteins; in therapy, exogenous enzymes compensate for endogenous deficiency