ELANE - elastase, neutrophil expressed
Entrez Gene Name: elastase, neutrophil expressed
Entrez GeneID: Human(1991)
, Mouse(50701), Rat(299606)
, Mouse(50701), Rat(299606) Synonyms: Ela2, ELANE, ELASTASE, NEUTROPHIL, F430011M15Rik, GE, HLE, HNE, LEUKOCYTE ELASTASE, NE, NEUTROPHIL ELASTASE, PMN-E
Gene Summary
- Human (1991): Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins. The product of this gene hydrolyzes proteins within specialized neutrophil lysosomes, called azurophil granules, as well as proteins of the extracellular matrix following the protein's release from activated neutrophils. The enzyme may play a role in degenerative and inflammatory diseases by its proteolysis of collagen-IV and elastin of the extracellular matrix. This protein degrades the outer membrane protein A (OmpA) of E. coli as well as the virulence factors of such bacteria as Shigella, Salmonella and Yersinia. Mutations in this gene are associated with cyclic neutropenia and severe congenital neutropenia (SCN). This gene is clustered with other serine protease gene family members, azurocidin 1 and proteinase 3 genes, at chromosome 19pter. All 3 genes are expressed coordinately and their protein products are packaged together into azurophil granules during neutrophil differentiation. [provided by RefSeq]
Molecular Functions | Biological Process | Cellular Components | Protein Domains | Subcellular Locations | Pathways | Literature References | IPA Extras
Cell Regulation
Biological Process
cellular calcium ion homeostasis, leukocyte migration, negative regulation of chemokine biosynthetic process, negative regulation of chemotaxis, negative regulation of inflammatory response, negative regulation of interleukin-8 biosynthetic process, phagocytosis, positive regulation of interleukin-8 biosynthetic process, positive regulation of MAP kinase activity, positive regulation of smooth muscle cell proliferation, protein catabolic process, proteolysis, proteolysis involved in cellular protein catabolic process, response to UV
Literature References
- 12018205Weinrauch Y, Drujan D, Shapiro SD, Weiss J, Zychlinsky A. Neutrophil elastase targets virulence factors of enterobacteria.Nature 2002 May 2;417(6884):91-4
- 17384412Campbell EJ, Owen CA. The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G.J Biol Chem 2007 May 11;282(19):14645-54
- 16301669Carroll TP, Greene CM, Taggart CC, Bowie AG, O'neill SJ, McElvaney NG. Viral Inhibition of IL-1- and Neutrophil Elastase-Induced Inflammatory Responses in Bronchial Epithelial Cells.J Immunol 2005 Dec 01;175(11):7594-601 View 594 categorized literature findings and their references in IPA
Molecular Functions
bacterial binding, catalytic activity, cytokine binding, hydrolase activity, peptidase activity, protein binding, serine-type endopeptidase activity, serine-type peptidase activity
