Transforming growth factor-beta receptor III (TGF-beta RIII) is one of three receptors for the secreted growth factor TGF-beta. Unlike type I and type II TGF-beta receptors, TGF-beta RIII does not participate directly in the propagation of intracellular signaling in response to TGF-beta binding (1). TGF-beta RIII typically functions as a coreceptor for TGF-beta by binding the ligand with high affinity in order to regulate signaling. TGF-beta RIII contains a large glycosylated extracellular domain and a small intracellular domain. The extracellular domain can bind ligand and enhance TGF-beta signaling. The receptor can also inhibit signaling by binding to and sequestering ligand (1). One study measured the effect of secreted TGF-beta RIII on sequestration of TGF-beta (2). They performed ELISA with TGF-beta RIII antibody to measure the amount of the secreted protein. Their data demonstrated the ability of TGF-beta RIII to inhibit tumor cell growth by sequestering signaling molecules (2). The small intracellular domain, although previously thought to have no signaling activity, has been shown to bind to the cytoskeleton and regulate its organization during cell migration (3). Research from the Blobe lab at Duke University performed immunoprecipitation with TGF-beta RIII antibody to demonstrate these cytoskeletal interactions (3). Together, these functions of the TGF-beta receptor are important for cardiovascular development and the migration of cancer cells (1,3). TGF-beta RIII antibodies have been used to investigate the expression and localization of TGF-beta receptor in different cell types and to elucidate its biological functions. In addition to these applications, TGF-beta RIII antibodies have been used as tools to manipulate TGF-beta in cell culture (4). Rosado et al. added varying concentrations TGF-beta RIII antibodies to their cell culture system to examine the response of chondrocytes to TGF-beta signaling (4).
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