GARP–latent transforming growth factor beta 1 complex

The **GARP–latent transforming growth factor beta 1 complex** is a cell-surface protein complex predominantly found on regulatory T cells (Treg) and platelets, consisting of GARP (glycoprotein A repetitions predominant, also known as LRRC32) covalently or noncovalently linked to latent TGF-β1 (transforming growth factor-beta 1) via disulfide bonds[2][4]. GARP acts as a cell surface receptor and chaperone for latent TGF-β1, presenting it in an inactive form and regulating its activation at the plasma membrane. Activation of TGF-β1 from this complex typically requires interaction with αV integrins (notably αVβ8), facilitating local release of active TGF-β1, which suppresses immune responses in the tumor microenvironment and contributes to immune tolerance[1][2][3][4]. Monoclonal antibodies can bind and stabilize this complex, preventing TGF-β1 activation and providing a novel target for cancer immunotherapy by inhibiting regulatory T cell-mediated immunosuppression.

Other names

GARP:TGF-β1 complexLRRC32:latent TGF-β1 complexGlycoprotein A repetitions predominant–latent TGF-beta 1 complexGARP–proTGFβ1 complex

Antibodies preventing activation/release of active TGF-β1 from the GARP–latent TGF-β1 complex, thus inhibiting Treg immunosuppression Modulation of downstream TGF-β1 signaling