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Results 1 - 9 of 9
EC Number
General Information
Commentary
Reference
malfunction
Saccharomyces cerevisiae cells deficient in Lap4 absorb almost 3fold as much cadmium as the wild type strain
physiological function
exposure of human peripheral blood mononuclear cells to isoform ERAP1 polymorphic variant proteins as well as ERAP1 overexpression increases inflammatory cytokine and chemokine production, and enhances immune cell activation. ERAP1 is able to activate innate immunity via multiple pathways, including the NOD-like receptor NLRP3 inflammasome. These responses vary if autoimmune disease-associated variants of ERAP1 are examined in the assay systems. Blocking ERAP1 cellular internalization augments IL-1beta production
physiological function
in both HeLa-B27 and C1R-B27 cells, the proportion of 9-mer HLA-B27-bound peptides is decreased by isoform ERAP1 silencing, whereas the percentages of longer peptides, 11-13 mer, are increased. Following ERAP1 silencing, C-terminally extended peptides are readily identified. These are better able to bind to HLA–B27 than N-terminally extended peptides lacking an arginine at position 2. In both HeLa-B27 cells and mouse fibroblasts expressing HLA-B27, the absence of ERAP1 reduces peptide recognition by HLA-B27-restricted immunodominant viral HLA–B27 epitope KK10-specific cytotoxic T-lymphocytes. Presence of an ankylosing spondylitis-protective variant of ERAP1, K528R, as compared to wild-type ERAP1, reduces the peptide recognition by KK10 cytotoxic T lymphocytes following transfection with extended KK10 minigenes
physiological function
in the presence of aminopeptidase inhibitor amastatin, nitric oxide synthesis in activated RAW264.7 cells is significantly decreased. Subsequently, significant reduction of nitric oxide synthesis is observed in aminopeptidase ERAP1 knockdown cells compared with wild-type cells. This reduction is rescued by exogenously added ERAP1. When peritoneal macrophages prepared from ERAP1 knockout mouse are employed, reduction of nitric oxide synthesis in knockout mouse macrophages is also attributable to ERAP1. In the presence of amastatin, further reduction is observed in knockout mouse-derived macrophages
physiological function
intracellular ERAP1 induces angiogenesis through endothelial integrin activation, while the secreted form of the enzyme suppresses angiogenesis through angiotensin II inactivation. ERAP1 participates in the innate immune response by increasing the production of cytokine receptors. ERAP1 is associated with the MHC class I antigen processing and presentation pathway
physiological function
Lap4 is involved in glutathione degradation, under cadmium stress, Lap4 and gamma-glutamyl transferase work together to assure an efficient glutathione turnover stored in the vacuole
physiological function
mice lacking isoform ERAP1 exhibit exaggerated innate immune responses early during pathogen recognition, as characterized by increased activation of splenic and hepatic natural killer and natural killer T-cells and enhanced production of proinflammatory cytokines such as IL12 and MCP1. ERAP1 is playing a critical role in natural killer cell development and function. ERAP1-KO mice show higher frequencies of terminally matured natural killer cells, as well as higher frequencies of licensed natural killer cells expressing the Ly49C and Ly49I receptors which positively correlates with an enhanced natural killer cell activation and IFNc production by ERAP1-KO mice challenged with pro-inflammatory stimuli. During pathogen recognition, ERAP1 regulates IL12 production by CD11c+ dendritic cells specifically
physiological function
precursors of MHC class I–presented peptides are trimmed to mature epitopes
physiological function
secreted from RAW-264.7 cells after costimulation with lipopolysaccharide and interferon-gamma
Results 1 - 9 of 9