Glycoprotein A repetitions predominant-Transforming growth factor beta 1 complex (GARP-TGF-β1 complex)

The Glycoprotein A repetitions predominant (GARP)-Transforming growth factor beta 1 (TGF-β1) complex is a critical molecular assembly found on the surface of activated regulatory T cells (Tregs) and platelets (Source: UniProt P46531; PubMed: 19255243). GARP, encoded by the LRRC32 gene, acts as a transmembrane anchor that binds and presents the latent form of TGF-β1, facilitating its subsequent activation and release into the microenvironment (Source: PubMed: 25938935). This complex plays a pivotal role in mediating the immunosuppressive activity of Tregs, which often contributes to immune evasion in the tumor microenvironment (Source: PubMed: 30635440). By sequestering TGF-β1 in a latent state and controlling its activation, the GARP-TGF-β1 complex serves as a key checkpoint in TGF-beta signaling (Source: PubMed: 29632023). Therapeutic strategies targeting this complex, such as the monoclonal antibody livmoniplimab (ABBV-151), aim to prevent the release of active TGF-β1, thereby restoring anti-tumor immune responses (Source: ClinicalTrials.gov NCT03821935). These therapies are currently being investigated in clinical trials, often in combination with other immune checkpoint inhibitors, to treat various solid tumors (Source: PubMed: 33106341).

Other names

LRRC32-TGFB1 complexGARP-latent TGF-beta 1 complexLeucine-rich repeat-containing protein 32-Transforming growth factor beta 1 complex

Selective inhibition of the release of active TGF-beta 1 from the GARP-anchored latent TGF-beta 1 complex on the surface of regulatory T cells and platelets (Source: PubMed: 29632023).