ELANE
ELANE (elastase, neutrophil expressed) encodes neutrophil elastase, a serine protease of the peptidase S1 family that degrades proteins inside neutrophil azurophil granules and in the extracellular matrix. It is also known as NE, HNE, HLE, PMN-E and ELA2. Browse Assay Genie's current range of ELANE research reagents below, or read on for the biology behind the target.
ELANE is a member of the elastase subfamily of serine proteases, which hydrolyse many proteins in addition to elastin. The encoded preproprotein is proteolytically processed to generate the active protease. Once activated, neutrophil elastase hydrolyses proteins within specialised neutrophil lysosomes called azurophil granules, and also acts on proteins of the extracellular matrix. UniProt records its localisation to the phagosome, lysosome, cytolytic granule and nucleus.
In host defence, neutrophil elastase degrades the outer membrane protein A (OmpA) of E. coli and the virulence factors of bacteria such as Shigella, Salmonella and Yersinia. Some bacteria counter this activity: the Staphylococcus aureus serine protease inhibitors Eap, EapH1 and EapH2 reversibly inhibit the enzyme and impair microbicidal activity in neutrophils. Through proteolysis of collagen-IV and elastin, the enzyme may also contribute to degenerative and inflammatory diseases.
The ELANE gene belongs to the peptidase S1 family and sits in a gene cluster on chromosome 19. Humans have six elastase genes, which encode structurally similar proteins. HGNC places it among the granule associated serine proteases of immune defence, the complement system regulators and receptors, and the elastases. The previous name was elastase 2, neutrophil (symbol ELA2). Mutations in the gene are associated with cyclic neutropenia and severe congenital neutropenia (SCN), which makes it a central gene in neutrophil disorder research. The mouse ortholog is Elane.
Neutrophil elastase acts within azurophil granules and phagosomes, making it a key protease for studying neutrophil effector function.
Proteolysis of collagen-IV and elastin by the enzyme may contribute to degenerative and inflammatory diseases.
Mutations in ELANE are associated with cyclic neutropenia and severe congenital neutropenia, so the gene is central to these disorders.
The enzyme degrades E. coli OmpA and virulence factors of Shigella, Salmonella and Yersinia, and is inhibited by S. aureus Eap proteins.
ELANE encodes neutrophil elastase, a serine protease activated from a preproprotein. It hydrolyses proteins within neutrophil azurophil granules and extracellular matrix proteins, including collagen-IV and elastin, and degrades bacterial proteins such as E. coli OmpA and virulence factors of Shigella, Salmonella and Yersinia.
ELANE is also called neutrophil elastase, NE, HNE (human neutrophil elastase), HLE, PMN-E and ELA2. HGNC lists the previous name as elastase 2, neutrophil. The enzyme carries the EC number 3.4.21.37 and belongs to the elastase subfamily of the peptidase S1 family.
Mutations in ELANE are associated with cyclic neutropenia and severe congenital neutropenia. The enzyme may also contribute to degenerative and inflammatory diseases. The mouse ortholog is Elane; check the datasheet of any product for its validated reactivity.
Other elastases, granule serine proteases and neutrophil and inflammation markers with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P08246; product specifications from Assay Genie datasheets.