|TGF‑ beta 2 Inhibition of IL‑4-dependent Cell Proliferation and Neutralization by TGF‑ beta 2/1.2 Antibody. Porcine TGF‑ beta 2 (Catalog # 102-B2) inhibits Recombinant Mouse IL‑4 (Catalog # 404-ML) induced proliferation in the HT‑2 mouse T cell line in a dose-dependent manner (orange line). Inhibition of Recombinant Mouse IL‑4 (7.5 ng/mL) activity elicited by Porcine TGF‑ beta 2 (1 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-TGF‑ beta 2/1.2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-302-NA). The ND50 is typically 0.01‑0.03 µg/mL.|
Transforming Growth Factor Beta 1, 2, and 3 (TGF-beta 1, TGF-beta 2, and TGF-beta 3) are highly pleiotropic cytokines that virtually all cell types secrete. TGF-beta molecules are proposed to act as cellular switches that regulate processes such as immune function, proliferation, and epithelial-mesenchymal transition. Targeted deletions of these genes in mice show that each TGF-beta isoform has some non-redundant functions: TGF-beta 1 is involved in hematopoiesis and endothelial differentiation; TGF-beta 2 affects development of cardiac, lung, craniofacial, limb, eye, ear, and urogenital systems; and TGF-beta 3 influences palatogenesis and pulmonary development. The full range of in vitro biological activities of TGF-beta 5 has not yet been explored. However, TGF-beta 1, TGF-beta 2, TGF-beta 3, and TGF-beta 5 have been found to be largely interchangeable in an inhibitory bioassay, and it is anticipated that TGF-beta 5 will show a spectrum of activities similar to the other TGF-beta family members. To date, the production of TGF-beta 5 has only been demonstrated in Xenopus.
TGF-beta ligands are initially synthesized as precursor proteins that undergo proteolytic cleavage. The mature segments form active ligand dimers via a disulfide-rich core consisting of the characteristic 'cysteine knot'. TGF-beta signaling begins with binding to a complex of the accessory receptor betaglycan (also known as TGF-beta RIII) and a type II serine/threonine kinase receptor termed TGF-beta RII. This receptor then phosphorylates and activates a type I serine/threonine kinase receptor, either ALK-1 or TGF-beta RI (also called ALK-5). The activated type I receptor phosphorylates and activates Smad proteins that regulate transcription. Use of other signaling pathways that are Smad-independent allows for distinct actions observed in response to TGF-beta in different contexts.
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