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Review
. 2013 Sep;154(3):219-28.
doi: 10.1093/jb/mvt066. Epub 2013 Aug 14.

Endoplasmic reticulum aminopeptidases: biochemistry, physiology and pathology

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Review

Endoplasmic reticulum aminopeptidases: biochemistry, physiology and pathology

Akira Hattori et al. J Biochem. 2013 Sep.

Abstract

The human endoplasmic reticulum aminopeptidase (ERAP) 1 and 2 proteins were initially identified as homologues of human placental leucine aminopeptidase/insulin-regulated aminopeptidase. They are categorized as a unique class of proteases based on their subcellular localization on the luminal side of the endoplasmic reticulum. ERAPs play an important role in the N-terminal processing of the antigenic precursors that are presented on the major histocompatibility complex (MHC) class I molecules. ERAPs are also implicated in the regulation of a wide variety of physiological phenomena and pathogenic conditions. In this review, the current knowledge on ERAPs is summarized.

Keywords: aminopeptidase; ankylosis spondylitis; antigen presentation; autoimmune diseases; endoplasmic reticulum.

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