Neutrophil Elastase 2 (ELA2 as the official gene symbol); Leukocyte elastase; Serine elastase; Polymorphonuclear leukocyte elastase; Granulocyte elastase

NE; is a single-chain glycoprotein with 218 amino acid residues and belongs to a member of the chymotrypsin superfamily of  serine protease, which includes chymotrypsin, trypsin, and elastase. With three residues in the active site, His⁴¹-Asp⁸⁸-Ser¹⁷³ comprises a “charge-relay” system to carry out hydrolysis. All serine proteases have their own internal inhibitors to prevent any overdose effects of cell lysis. A natural inhibitor of NE is α₁-antitrypsin (α₁AT). The major physiological function of NE is host-defense, i.e., to degrade foreign microorganisms or organic molecules that were phagocytosed by neutrophils. NE also degrades a variety of substrates including elastin, the most important of all, and other  extracellular matrix proteins ( collagen,  proteoglycan,  fibronectin, and  cadherins),  platelet...