anti-Histidyl-tRNA Synthetase (HARS) Antibodies

Human Histidyl-tRNA Synthetase (HARS) interaction partners

1. the first biochemical analysis of Charcot-Marie-Tooth-associated HARS mutations and underscores how loss of the primary aminoacylation function can contribute to disease pathology.

2. This study suggests that the human HisRS genes, while descending from a common ancestor with dual function for both types of tRNA(His), have acquired highly specialized tRNA recognition properties through evolution.

3. Despite the similar kinetics, differential scanning fluorimetry revealed that Y454S is less thermally stable than Wild Type HARS, and cells from Y454S patients grown at elevated temperatures demonstrate diminished levels of protein synthesis compared to those of Wild Type cells. The thermal sensitivity associated with the Y454S mutation represents a biochemical basis for understanding Usher Syndrome Type IIIB.

4. Loss of function mutations in histidyl-tRNA synthetase cause a spectrum of inherited peripheral neuropathies

5. Data suggest that by comparing human and trypanosomatid histidyl-tRNA synthetases (HisRS) may provide opportunities for developing specific inhibitors of Trypanosoma brucei HisRS.

6. Secreted histidyl-tRNA synthetase splice variants elaborate major epitopes for autoantibodies in inflammatory myositis.

7. Data indicate that higher anti-Jo1 levels were associated with disease severity in antisynthetase syndrome (ASS) patients.

8. Non-Jo-1 anti-synAb positive patients have decreased survival compared with Jo-1 patients.

9. Findings suggest that histidyl-tRNA synthetase (HARS) is associated with axonal peripheral neuropathy.

10. The crystal structure of a novel splice variant of a tRNA synthetase lacking the entire catalytic domain.

11. Although anti-Jo1 positive patients with antisynthetase syndrome share features of patients with anti-PL7/PL12 antibody, they exhibit many differences regarding clinical phenotype and long-term outcome.

12. Study identified sequence variants in the known disease-causing genes SLC6A3 and FLVCR1, and present evidence to strongly support the pathogenicity of variants identified in TUBGCP6, BRAT1, SNIP1, CRADD, and HARS.

13. genomic organization of the HARS locus and mapping of transcripts originating from a bi-directional promoter controlling the differential expression of these gene

14. Demonstrating histidyl-tRNA synthetase (Jo-1)-specific T cell responses represents a key step in establishing the hypothesis that Jo-1 drives T cell-mediated autoimmunity in Jo-1+ polymyositis.

15. the TSG101 interaction with HRS is a crucial step in endocytic down-regulation of mitogenic signaling and this interaction may have a role in linking the functions of early and late endosomes

16. A proteolytically sensitive conformation of HisRS exists in the lung, the target tissue associated with this autoantibody response.

17. clinical and prognostic profiles of 45 patients displaying anti-histidyl-tRNA synthetase autoantibodies were determined

Mouse (Murine) Histidyl-tRNA Synthetase (HARS) interaction partners

1. AA 60-90 of HRS were absolutely required for in vitro as well as in vivo signaling via MyD88-dependent TLR pathways to case myositis.