High impact information on Arts1

• Those peptides are generated by proteolysis, which begins in the cytoplasm and continues in the endoplasmic reticulum by the unique aminopeptidase ERAAP [1].
• Furthermore, ERAAP-deficient cells presented many unstable and structurally unique peptide-MHC complexes, which elicited potent CD8(+) T cell and B cell responses [1].
• The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules [2].
• We addressed these issues by generating mice lacking the endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP) [2].
• Puromycin-insensitive leucyl-specific aminopeptidase (PILSAP) plays an important role in angiogenesis by regulating the proliferation and migration of endothelial cells (ECs) [3].

Biological context of Arts1

• Mouse PILSAP gene contained 19 exons and located in the chromosome 13C1-C2 [4].

Anatomical context of Arts1

• A mouse orthologue of puromycin-insensitive leucyl-specific aminopeptidase is expressed in endothelial cells and plays an important role in angiogenesis [5].
• Thus, trimming of antigenic peptides by ERAAP in the endoplasmic reticulum is essential for the generation of the normal repertoire of processed peptides [2].
• Puromycin insensitive leucyl-specific aminopeptidase (PILSAP) is required for the development of vascular as well as hematopoietic system in embryoid bodies [6].

Other interactions of Arts1

• AML1/Runx1/PEBP2alphaB increased PILSAP mRNA in mouse ECs, whereas dominant interfering chimerical PEBP2beta-MYH11 decreased it [4].
• The similar results were obtained in EBs treated with leucinethiol, a specific inhibitor of leucine aminopeptidase or siRNA for PILSAP [6].
• These results indicate that the expression of PILSAP in mouse ECs is regulated, at least in part, by PEBP2 [4].

References