
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).
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