Interaction with colon cancer cells hyperactivates TGF-beta signaling in cancer-associated fibroblasts.
Authors: Hawinkels L, Paauwe M, Verspaget H, Wiercinska E, van der Zon J, van der Ploeg K, Koelink P, Lindeman J, Mesker W, ten Dijke P, Sier C
Oncogene, 2014;33(1):97-107.
Species: Human
Sample Type: Cell Culture Supernates

Glioblastoma-secreted factors induce IGFBP7 and angiogenesis by modulating Smad-2-dependent TGF-beta signaling.
Authors: Pen A, Moreno MJ, Durocher Y, Deb-Rinker P, Stanimirovic DB
Oncogene, 2008;27(54):6834-44.
Species: Human
Sample Type: Cell Culture Supernates

Opposite regulation of transforming growth factors-beta2 and -beta3 expression in the human endometrium.
Authors: Gaide Chevronnay HP, Cornet PB, Delvaux D, Lemoine P, Courtoy PJ, Henriet P, Marbaix E
Endocrinology, 2007;149(3):1015-25.
Species: Human
Sample Type: Tissue Homogenates

Transforming growth factor-beta1 suppresses airway hyperresponsiveness in allergic airway disease.
Authors: Alcorn JF, Rinaldi LM, Jaffe EF, van Loon M, Bates JH, Janssen-Heininger YM, Irvin CG
Am. J. Respir. Crit. Care Med., 2007;176(10):974-82.
Species: Mouse
Sample Type: BALF

Activation of transforming growth factor-beta by the integrin alphavbeta8 delays epithelial wound closure.
Authors: Neurohr C, Nishimura SL, Sheppard D
Am. J. Respir. Cell Mol. Biol., 2006;35(2):252-9.
Species: Human
Sample Type: Cell Culture Supernates

The selective estrogen receptor modulator arzoxifene and the rexinoid LG100268 cooperate to promote transforming growth factor beta-dependent apoptosis in breast cancer.
Authors: Rendi MH, Suh N, Lamph WW, Krajewski S, Reed JC, Heyman RA, Berchuck A, Liby K, Risingsong R, Royce DB, Williams CR, Sporn MB
Cancer Res., 2004;64(10):3566-71.
Species: Rat
Sample Type: Cell Culture Supernates

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.