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All three TGFβ1, TGFβ2 and TGFβ3. are synthesized as precursor molecules containing a propeptide region in addition to the TGF-β homodimer. [10] After it is synthesized, the TGF-β homodimer interact with a Latency Associated Peptide (LAP)[a protein derived from the N-terminal region of the TGF beta gene product] forming a complex called Small Latent Complex (SLC).
Because MMP-2 and MMP-9 can activate TGF-β through proteolytic degradation of the latent TGF beta complex, [31] αV containing integrins activate TGF-β1 by creating a close connection between the latent TGF-β complex and MMPs. Integrins αVβ6 and αVβ3 are suggested to simultaneously bind the latent TGF-β1 complex and proteinases ...
The secretion and activation of TGF-betas is regulated by their association with latency-associated proteins and with latent TGF-beta binding proteins. The product of this gene targets latent complexes of transforming growth factor beta to the extracellular matrix, where the latent cytokine is subsequently activated by several different mechanisms.
The latent TGF-beta binding proteins (LTBP) are a family of carrier proteins. [ 1 ] [ 2 ] LTBP is a family of secreted multidomain proteins that were originally identified by their association with the latent form of transforming growth factors .
68 Ga-Trivehexin targets (i.e., binds to) the cell surface receptor αvβ6-integrin, a heterodimeric transmembrane cell adhesion receptor whose primary natural ligand is latency associated peptide (LAP) in its complex with transforming growth factor beta 1 (TGF-β1). [2] Binding of αvβ6-integrin to LAP releases and thus, activates TGF-β1.
Proteins from the TGF-beta superfamily are only active as homo- or heterodimer; the two chains being linked by a single disulfide bond. From X-ray studies of TGF-beta-2, [7] it is known that all the other cysteines are involved in intrachain disulfide bonds. As shown in the following schematic representation, there are four disulfide bonds in ...
Latent-transforming growth factor beta-binding protein 2 is a protein that in humans is encoded by the LTBP2 gene. [5] [6]The protein encoded by this gene belongs to the family of latent transforming growth factor (TGF)-beta binding proteins (LTBP), which are extracellular matrix proteins with multi-domain structure.
The principal function of αvβ6 is the activation of cytokine transforming growth factor-b1 (TGF-β1). [19] [29] Latent-TGF-β1 is bound to the extracellular matrix, covered by its pro-peptide latency associated peptide (LAP). [29] αvβ6 binds LAP, and through cytoskeletal force releases TGF-β1. [30]