Human neutrophil and pancreatic elastase (HNE/PE)

Human neutrophil and pancreatic elastase refers to a pair of distinct serine proteases that share the ability to hydrolyze elastin and are often discussed together in the context of protease-antiprotease balance [1.2.1, 1.3.2]. Human neutrophil elastase (HNE), encoded by the ELANE gene, is a major component of neutrophil granules and plays a vital role in the innate immune response by degrading pathogens and extracellular matrix proteins [1.3.5]. However, its excessive activity is linked to tissue destruction in inflammatory conditions such as chronic obstructive pulmonary disease (COPD), cystic fibrosis, and acute respiratory distress syndrome (ARDS) [1.2.3, 1.3.2]. Pancreatic elastase (PE), primarily the CELA3 isoforms, is synthesized by pancreatic acinar cells and functions in the small intestine to facilitate protein digestion [1.3.4]. While HNE is a primary therapeutic target for inhibitors like sivelestat and alvelestat, PE is widely used as a clinical biomarker; low fecal elastase-1 levels indicate exocrine pancreatic insufficiency [1.3.1, 1.3.4]. Both enzymes are regulated by endogenous inhibitors like alpha-1 antitrypsin, and an imbalance between these proteases and their inhibitors is a hallmark of various degenerative and inflammatory pathologies [1.2.1, 1.2.3].

Other names

Neutrophil elastasePancreatic elastaseELANECELA3Leukocyte elastaseElastase 1Elastase 2Polymorphonuclear leukocyte elastase

Inhibition of serine protease activity, thereby preventing the degradation of elastin and other extracellular matrix proteins.