Human neutrophil elastase and pancreatic elastase (HNE and PE)

Human neutrophil elastase (HNE) and pancreatic elastase (PE) are serine proteases that play pivotal roles in tissue homeostasis and the inflammatory response [2, 12]. HNE, encoded by the ELANE gene, is primarily found in the azurophilic granules of neutrophils and is released to degrade extracellular matrix proteins such as elastin and collagen, while also contributing to the destruction of engulfed pathogens [12, 13]. Pancreatic elastases, including members of the chymotrypsin-like elastase (CELA) family, are traditionally known for their role in protein digestion in the gut, but specific isoforms like CELA1 are also expressed in the lung where they contribute to strain-mediated matrix remodeling [6, 15]. An imbalance between these proteolytic enzymes and their endogenous inhibitors, most notably alpha-1 antitrypsin, is a central driver of tissue destruction in chronic obstructive pulmonary disease (COPD), emphysema, and acute respiratory distress syndrome (ARDS) [13, 19]. Therapeutic interventions include the use of selective inhibitors like sivelestat for acute lung injury and alvelestat for alpha-1 antitrypsin deficiency, as well as augmentation therapy with purified alpha-1 antitrypsin to restore the protease-antiprotease balance [1, 19, 21].

Other names

PMN elastaseLeukocyte elastaseELANECELA1CELA2ACELA3ACELA3BMedullasinElastase-2

Competitive inhibition of the serine protease active site, preventing the degradation of elastin and other extracellular matrix proteins [1, 12].