Cutting Edge: Active TGF-β1 Released from GARP/TGF-β1 Complexes on the Surface of Stimulated Human B Lymphocytes Increases Class-Switch Recombination and Production of IgA
- Resource Type
- Authors
- Julie Stockis; Olivier Dedobbeleer; Sophie Lucas; Bas van der Woning; Pierre Coulie
- Source
- Journal of Immunology, Vol. 199, no. 2, p. 391-396 (2017)
The Journal of Immunology
- Subject
- 0301 basic medicine
Immunoglobulin A
Cell type
medicine.medical_treatment
Immunology
Plasma protein binding
Biology
Lymphocyte Activation
T-Lymphocytes, Regulatory
Transforming Growth Factor beta1
03 medical and health sciences
0302 clinical medicine
Immune system
medicine
Humans
Immunology and Allergy
Recombination, Genetic
B-Lymphocytes
Membrane Proteins
Immunoglobulin Class Switching
3. Good health
Cell biology
030104 developmental biology
Cytokine
Oligodeoxyribonucleotides
Membrane protein
Immunoglobulin class switching
030220 oncology & carcinogenesis
biology.protein
Cytokines
Cutting Edge
Protein Binding
Transforming growth factor
- Language
Production of active TGF-β is regulated at a posttranslational level and implies release of the mature cytokine dimer from the inactive, latent TGF-β precursor. There are several cell-type specific mechanisms of TGF-β activation. We identified a new mechanism operating on the surface of human regulatory T cells and involving membrane protein GARP, which binds latent TGF-β1. The paracrine activity of regulatory T cell–derived TGF-β1 contributes to immunosuppression and can be inhibited with anti-GARP Abs. Whether other immune cell types use surface GARP to activate latent TGF-β1 was not known. We show in this study that stimulated, human B lymphocytes produce active TGF-β1 from surface GARP/latent TGF-β1 complexes with isotype switching to IgA production.