<unk>  (, leukocyte<unk> , ELANE, ELA2,<unk>  2,<unk> utrophil, elaszym, serine<unk> , subtype human leukocyte<unk>  (HLE)) is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity.<unk>  is secreted by<unk> utrophils during inflammation, and destroys bacteria and host tissue. It also localizes to<unk> utrophil extracellular traps <unk> Ts), via its high affinity for DNA, an unusual property for serine proteases. As with other serine proteinases it contains a charge relay system composed of the catalytic triad of histidine, aspartate, and serine residues that are dispersed throughout the primary sequence of the polypeptide but that are brought together in the three dimensional conformation of the folded protein. The gene encoding<unk> , ELA2, consists of five exons.<unk>  is closely related to other cytotoxic immune serine proteases, such as the granzymes and cathepsin G. It is more distantly related to the digestive CELA1. The<unk> utrophil form of<unk>  () is 218 amino acids long, with two asparagine-linked carbohydrate chains (see glycosylation). It is present in azurophil granules in the<unk> utrophil cytoplasm. There appear to be two forms of<unk> , termed IIa and IIb.
Neutrophil elastase
Fibrinolysin
Alpha defensin
Beta defensin
Complement component 5a
Complement component 3
Complement component 4
Intrinsic factor