Transforming growth factor beta 1, 2, and 3 (TGF-β1, TGF-β2, TGF-β3)

Transforming growth factor beta 1, 2, and 3 (TGF-β1, TGF-β2, and TGF-β3) are secreted dimeric polypeptide cytokines and the principal mammalian isoforms of the TGF-β subfamily. They are synthesized as large precursor proteins, including a latency-associated peptide (LAP) and a mature region, and require proteolytic cleavage and extracellular activation to function. Mature TGF-β isoforms operate through a canonical pathway in which they bind dimeric type II TGF-β receptors that recruit and phosphorylate type I receptors, both of which are transmembrane serine/threonine kinase receptors. Activated receptors phosphorylate SMAD2/3 proteins, which then associate with SMAD4 and translocate to the nucleus to regulate gene transcription. TGF-βs play crucial roles in regulation of cell growth, differentiation, immune suppression, maintenance of tissue homeostasis, and extracellular matrix production. Dysregulation is linked to cancer, fibrosis, autoimmune, and degenerative diseases. Multiple therapeutics target TGF-β, but due to its broad homeostatic roles, inhibition can cause significant safety concerns including immunosuppression and impaired tissue repair[1][2][3][4][5][6][7][9].

Other names

TGF-beta 1, 2, 3TGFβ1, TGFβ2, TGFβ3TGFB1, TGFB2, TGFB3Pro-TGF beta 1 (for inactive TGF-β1)LAP/TGF beta 1 (for latent TGF-β1)

Inhibition of TGF-β ligand binding to its receptors Antibody-mediated neutralization of TGF-β ligand Inhibition of TGF-β receptor kinase activity Interference with SMAD signaling (downstream signal transduction)