Endoplasmic Reticulum Aminopeptidase 1 Proteins (ERAP1)

Cow (Bovine) Endoplasmic Reticulum Aminopeptidase 1 (ERAP1) interaction partners

1. ERAP1 and PDE8A were downregulated in vaccinated cattle that were protected from experimental M. bovis challenge. Remarkably, both genes encode proteins that have been negatively associated with immune protection against Bovine Tuberculosis.

Human Endoplasmic Reticulum Aminopeptidase 1 (ERAP1) interaction partners

1. This study revealed a close relationship between the transcriptional induction of the ERAP1 gene by interferon-gamma and the alternative splicing.

2. Increased aminopeptidase expression governed by altered transcript dynamics at both ERAP1 and ERAP2 is a key mechanism driving the degree to which these enzymes contribute to immune-mediated disease.

3. There was a significant association between ERAP1 polymorphisms (rs30187 and rs27037) and increased risk of Ankylosing Spondylitis susceptibility.

4. ERAP1 gene rs26653 polymorphism may increase the risk of psoriasis vulgaris in Chinese Han population

5. this study shows the association of ERAP1 single nucleotide polymorphism and its haplotypes with psoriasis vulgaris, and its dependence on the presence or absence of the HLA-C*06:02 allele and age at disease onset

6. ERAP1 and ERAP2 heterodimers have a role in mediating the processing pathway of MHC class I antigens

7. these results indicated that the ERAP gene may play a critical role in Hepatitis C virus chronicity in Chinese Han population

8. this study demonstrates associations of ERAP1 coding variants and domain specific interaction with HLA-C *06 in the early onset psoriasis patients of India

9. To decrease the enzymatic activity of ERAP1.

10. Data demonstrate that HCMV miR-UL112-5p targets ERAP1, thereby inhibiting the processing and presentation of the HCMV pp65495-503 peptide to specific CTLs.

11. these results present the first direct evidence that human disease-associated ERAP1 variants can greatly alter survival, as well as antigen presentation, T-cell repertoire and NK cell responses in vivo in mice

12. The ERAP1 association with ankylosing spondylitis is predominantly attributable to common ERAP1 haplotypes and haplotype combinations.

13. these study reports an association of the ERAP1 SNP rs30187 with the HLA-C*07 allele in inflammatory bowel disease in the Spanish population

14. Study suggests that ERAP1 rs27044 polymorphism may be related to ankylosing spondylitis susceptibility in Chinese Han population.

15. Segregating according to HLAB27 status did not alter the lack of association. rs30187 SNP in ERAP1 does not confer risk of developing ERA or AS in the Asian Indian population.

16. ERAP1 and ERAP2 have significant and distinct effects on the HLA-B*27 peptidome, suggesting that both enzymes largely act as separate entities in vivo. This may explain their different patterns of association with AS.

17. This review focuses on the ambivalent role of HLA-B27 in autoimmunity and viral protection correlating its functions to the quantitative and qualitative effects of ERAP1 and ERAP2 polymorphisms on their enzymatic activity.

18. The ERAP1 gene polymorphism might be a risk factor in the pathogenesis of ankylosing spondylitis and inflammatory bowel disease. In contrast, IL-23R gene polymorphisms may serve a protective role in ankylosing spondylitis and inflammatory bowel disease.

19. Our results suggest that normal levels of ERAP1 reduce the accumulation of aberrant and disulfide-linked forms of HLA-B27 in monocytes, and thus help to maintain the integrity of cell surface HLA-B27 complexes.

20. The alterations in the nature and affinity of HLA-B*51.peptide complexes probably affect T-cell and natural killer cell recognition, providing a sound basis for the joint association of ERAP1 and HLA-B*51 with Behcet's disease.

Mouse (Murine) Endoplasmic Reticulum Aminopeptidase 1 (ERAP1) interaction partners

1. The ERAP1 behaves similar to acute-phase proteins, which are secreted into the blood in response to infectious/inflammatory stimuli and are involved in enhancing NO synthesis as a host defense mechanism.

2. data provide the first evidence that ERAP1 associated with exosomes plays important roles in inflammatory processes via activation of macrophages.

3. we have shown that the loss of ERAAP leads to shifts in the nature and lengths of peptides presented by MHC I molecules on the cell surface

4. results suggest that several aminopeptidases play important roles in the maximum synthesis of NO in activated macrophages in a substrate peptide-dependent manner and ERAP1 is one of the aminopeptidases involved in the NO synthesis

5. Data show that endoplasmic reticulum protein 44 (ERp44) forms a mixed disulfide bond with aminopeptidase ERAP1 and controls the release of ERAP1 in a redox-dependent manner to control blood pressure.

6. This study clarifies ERAP1's role in shaping immunodominance through creation and destruction of peptides in vivo and demonstrates the functional significance of ERAP1 in modulating T-cell killing based upon this role.

7. These results suggest that secretion of ERAP1 is mediated by toll-like receptors via induction of intermediate cytokines

8. ERAP1 directly alters peptide binding and presentation by HLA-B27, thus demonstrating a potential pathogenic mechanism in ankylosing spondylitis.

9. Absence of Tpn or ERAAP independently altered the peptide repertoire by causing loss as well as gain of new pMHC I. ERAAP defined the characteristic amino termini of canonical MHC I peptides.

10. MHC class Ib-restricted cytolytic effector cells specifically eliminated ERAAP-deficient cells in vitro and in vivo.

11. endoplasmic reticulum aminopeptidase 1 is involved in the activation of macrophages induced by lipopolysaccharide and interferon-gamma

12. ERAAP silencing results in MHC-I peptide-loading defects eliciting rejection of the murine T-cell lymphoma RMA in syngeneic mice

13. The characteristic peptide length, as well as composition, of class I histocompatibility peptide cargo is determined not only by the class-I peptide-binding groove, but also by ERAAP proteolysis in the endoplasmic reticulum.

14. identification of ERAAP, the aminopeptidase associated with antigen processing in the endoplasmic reticulum (ERAAP)

15. Data show that loss of endoplasmic reticulum aminopeptidase 1 (ERAP1) in the antigen-processing pathway results in a marked shift in the hierarchy of immunodominance in viral infections.

16. Although PILSAP may not function in the initial generation of Flk-1 positive mesodermal precursors, it does play a role in growth of vascular, hematopoietic, and muscular lineage population from those precursors.

17. PILSAP affects RhoA activation and that influences the proper function of endothelial cells

18. ERAAP, in concert with major histocompatibility complex class I molecules, regulates the quality of processed peptides presented on the cell surface.