Bio Background |
The endoplasmic reticulum (ER) aminopeptidase 1 (ERAP1), a member of the peptidase M1 family, plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides (1, 2). It is also designated as adipocyte-derived leucine aminopeptidase (A-LAP), puromycin-insensitive leucine-specific aminopeptidase (PILS-AP) and aminopeptidase regulator of TNFR1 shedding (ARTS-1) (3). ERAP1 is localized to the lumen of the ER and induced by interferon. It may be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (3, 4). |
Bio References |
Hattori A, Kitatani K, Matsumoto H, et al. Characterization of recombinant human adipocytederived leucine aminopeptidase expressed in Chinese hamster ovary cells. J. Biochem. 2000; 128:755-62.Saric T, Chang SC, Hattori A, et al. An IFN-gamma induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat. Immunol. 2002; 3:1169-76.Cui X, Hawari F, Alsaaty S, et al. Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding. J. Clin. Invest. 2002; 110:515-26.Akada T, Yamazaki T, Miyashita H, et al. Puromycin insensitive leucyl-specific aminopeptidase (PILSAP) is involved in the activation of endothelial integrins. J. Cell Physiol. 2002; 193: 253-62. |