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Transforming growth factor beta 1 and 3 are two isoforms of the TGF-β family of secreted cytokines and growth factors, sharing approximately 70–80% sequence homology and signaling through the same receptor system. Both are synthesized as precursor proteins processed to produce mature, active dimers. TGF-β1 and TGF-β3 regulate a wide range of biological processes, including cell proliferation, migration, differentiation, extracellular matrix deposition, immunomodulation, and apoptosis. These isoforms play critical roles in development, wound healing, tissue homeostasis, and disease, particularly in cancer, fibrosis, and inflammatory disorders. Though similar, TGF-β1 and TGF-β3 have distinct regulatory roles, especially in tissue-specific contexts such as bone repair and embryogenesis[1][2][3][4][5][6]. Therapeutic targeting of TGF-β1 or TGF-β3 is an area of active research, with several clinical candidates aimed at modulating their pathological activity. Structurally, TGF-β isoforms form dimeric cystine knot proteins, bind cell surface type I and type II receptors, and initiate downstream SMAD-dependent and SMAD-independent signaling cascades[2][5]. Their activity is tightly regulated by latency-associated peptides and extracellular binding proteins, with activation often triggered by proteolytic, integrin, or microenvironmental cues[3][4]. Note: For structured downstream use, treat “Transforming growth factor beta 1” and “Transforming growth factor beta 3” as separate canonical targets; grouping them is non-standard.
Neutralization of ligand function (antibody); Inhibition of receptor kinase activity (small molecule inhibitor); Blockade of downstream signaling (SMAD inhibition)
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