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Overview
Human Transforming Growth Factor-β1 (TGF-β1) is a pleiotropic cytokine produced primarily by platelets and bone, and in smaller amounts by most nucleated cell types and tumors. TGF-β1 is involved in tissue remodeling, wound repair, development and hematopoiesis. TGF-β1 is stimulatory for cells of mesenchymal origin and inhibitory for cells of epithelial or neuroectodermal origin. It is also a switch factor for IgA. Human TGF-β1 is synthesized as a dimeric inactive precursor of 390 amino acid residues, which is cleaved to an active dimer of 112 residues disulphide-linked peptides. The mature protein has a molecular mass of 25 kDa. TGF-β1 binds to three types of receptors. Type I and Type II TGF-β1 receptors encode serine/threonine kinases and mediate signal transduction events via autophosphorylation.