| First Author | Kurnellas MP | Year | 2014 |
| Journal | J Exp Med | Volume | 211 |
| Issue | 9 | Pages | 1847-56 |
| PubMed ID | 25073790 | Mgi Jnum | J:218116 |
| Mgi Id | MGI:5616688 | Doi | 10.1084/jem.20140107 |
| Citation | Kurnellas MP, et al. (2014) Mechanisms of action of therapeutic amyloidogenic hexapeptides in amelioration of inflammatory brain disease. J Exp Med 211(9):1847-56 |
| abstractText | Amyloid fibrils composed of peptides as short as six amino acids are effective therapeutics for experimental autoimmune encephalomyelitis (EAE). Immunosuppression arises from at least two pathways: (1) expression of type 1 IFN by pDCs, which were induced by neutrophil extracellular traps arising from the endocytosis of the fibrils; and (2) the reduced expression of IFN-gamma, TNF, and IL-6. The two independent pathways stimulated by the fibrils can act in concert to be immunosuppressive in Th1 indications, or in opposition, resulting in inflammation when Th17 T lymphocytes are predominant. The generation of type 1 IFN can be minimized by using polar, nonionizable, amyloidogenic peptides, which are effective in both Th1 and Th17 polarized EAE. |
