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, 39 (12), 3315-22

Membrane Protein GARP Is a Receptor for Latent TGF-beta on the Surface of Activated Human Treg

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Membrane Protein GARP Is a Receptor for Latent TGF-beta on the Surface of Activated Human Treg

Julie Stockis et al. Eur J Immunol.

Abstract

Human Treg and Th clones secrete the latent form of TGF-beta, in which the mature TGF-beta protein is bound to the latency-associated peptide (LAP), and is thereby prevented from binding to the TGF-beta receptor. We previously showed that upon TCR stimulation, human Treg clones but not Th clones produce active TGF-beta and bear LAP on their surface. Here, we show that latent TGF-beta, i.e. both LAP and mature TGF-beta, binds to glycoprotein A repetitions predominant (GARP), a transmembrane protein containing leucine rich repeats, which is present on the surface of stimulated Treg clones but not on Th clones. Membrane localization of latent TGF-beta mediated by binding to GARP may be necessary for the ability of Treg to activate TGF-beta upon TCR stimulation. However, it is not sufficient as lentiviral-mediated expression of GARP in human Th cells induces binding of latent TGF-beta to the cell surface, but does not result in the production of active TGF-beta upon stimulation of these Th cells.

Comment in

  • The Tregs' World According to GARP
    M Battaglia et al. Eur J Immunol 39 (12), 3296-300. PMID 19904770.
    Naturally occurring CD4+CD25(high) regulatory T cells (nTreg) are essential for maintaining tolerance. FOXP3 has been established as a molecular marker of nTreg; however, …

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