Endoplasmic reticulum aminopeptidases: Biology and pathogenic potential

Nat Rev Rheumatol. 2010 Aug;6(8):461-7. doi: 10.1038/nrrheum.2010.85. Epub 2010 Jun 8.

Abstract

Endoplasmic reticulum aminopeptidase 1 (ERAP1) and the closely related ERAP2 are involved in the final trimming of peptides within the endoplasmic reticulum for presentation by major histocompatibility complex (MHC) class I molecules. ERAP1 was found to be associated with ankylosing spondylitis (AS) in a genome-wide association study of nonsynonymous single nucleotide polymorphisms, and this association has been confirmed in several studies. An ERAP1/ERAP2 haplotype has also been reported to be associated with familial AS. ERAP1 and ERAP2 could carry out several potential roles in the pathogenesis of AS. ERAP1-deficient mice show a considerable alteration in the level and repertoire of peptides presented by MHC class I molecules. Furthermore, ERAP1 has been shown to be involved in shedding cytokine receptors. Both of these functions require further analysis to better understand the exact role of ERAP1 in AS.

Publication types

  • Review

MeSH terms

  • Aminopeptidases / genetics
  • Aminopeptidases / metabolism*
  • Animals
  • Endoplasmic Reticulum / enzymology*
  • Genetic Predisposition to Disease
  • HLA-B27 Antigen / genetics
  • Haplotypes
  • Histocompatibility Antigens Class I / metabolism
  • Humans
  • Mice
  • Mice, Knockout
  • Minor Histocompatibility Antigens
  • Polymorphism, Single Nucleotide
  • Spondylitis, Ankylosing / genetics
  • Spondylitis, Ankylosing / metabolism

Substances

  • HLA-B27 Antigen
  • Histocompatibility Antigens Class I
  • Minor Histocompatibility Antigens
  • Aminopeptidases
  • ERAP1 protein, human
  • ERAP2 protein, human