| First Author | Edwards JP | Year | 2014 |
| Journal | J Immunol | Volume | 193 |
| Issue | 6 | Pages | 2843-9 |
| PubMed ID | 25127859 | Mgi Jnum | J:244456 |
| Mgi Id | MGI:5913235 | Doi | 10.4049/jimmunol.1401102 |
| Citation | Edwards JP, et al. (2014) Release of active TGF-beta1 from the latent TGF-beta1/GARP complex on T regulatory cells is mediated by integrin beta8. J Immunol 193(6):2843-9 |
| abstractText | Activated T regulatory cells (Tregs) express latent TGF-beta1 on their cell surface bound to GARP. Although integrins have been implicated in mediating the release of active TGF-beta1 from the complex of latent TGF-beta1 and latent TGF-beta1 binding protein, their role in processing latent TGF-beta1 from the latent TGF-beta1/GARP complex is unclear. Mouse CD4(+)Foxp3(+) Treg, but not CD4(+)Foxp3(-) T cells, expressed integrin beta8 (Itgb8) as detected by quantitative RT-PCR. Itgb8 expression was a marker of thymically derived (t)Treg, because it could not be detected on Foxp3(+)Helios(-) Tregs or on Foxp3(+) T cells induced in vitro. Tregs from Itgb8 conditional knockouts exhibited normal suppressor function in vitro and in vivo in a model of colitis but failed to provide TGF-beta1 to drive Th17 or induced Treg differentiation in vitro. In addition, Itgb8 knockout Tregs expressed higher levels of latent TGF-beta1 on their cell surface consistent with defective processing. Thus, integrin alphavbeta8 is a marker of tTregs and functions in a cell intrinsic manner in mediating the processing of latent TGF-beta1 from the latent TGF-beta1/GARP complex on the surface of tTregs. |
