TGFβ receptors are single pass serine/threonine kinase receptors. They exist in several different isoforms that can be homo- or heterodimeric. The number of characterized ligands in the TGFβ superfamily far exceeds the number of known receptors, suggesting the promiscuity that exists between the ligand and receptor interactions.
TGF (Transforming Growth Factor) are involved in paracrine signalling and can be found in many different tissue types, including brain, heart, kidney, liver, and testes. Over-expression of TGF can induce renal fibrosis, causing kidney disease, as well as diabetes, and ultimately end-stage renal disease (ESRD). Recent developments have found that, using certain types of protein antagonists against TGFβ receptors, can halt and in some cases reverse the effects of renal fibrosis.
Three TGF-β receptor types can be distinguished by their structural and functional properties. Receptor types I and II have similar ligand-binding affinities and can be distinguished from each other only by peptide mapping. Both receptor types I and II have a high affinity for TGF-β1 and low affinity for TGF-β2. TGF-β receptor type III has a high affinity for both TGF-β1 and -β2 and in addition TGF-β1.2.
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