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Cross talk among TGF-βand integrins





The growth factor TGF-β are fundamental to prenatal development and the postnatal growth, remodeling, and maintenance of various tissues and organs. TGF-β is secreted in a latent complex consisting of three proteins: TGF-β, an inhibitor know as latency-associated protein, LAP, which is derived from the TGF-β propeptide and an ECM-binding protein which is one of the latent TGF-β binding proteins, also know as LTBPs. LTBPs interact with fibrillins and other extracellular matrix (ECM) components and thus function to localize latent TGF-β in the ECM. LAP contains an integrin-binding site (RGD), and several RGD-binding integrins are able to activate latent TGF-β through binding this site.

Integrins are crucially important because they are the main receptor proteins that cells use to both bind to and respond to the ECM. An integrin molecule is composed of two noncovalently associated transmembrane glycoprotein subunits called α and β. Because the same integrin molecule in different cell types can have different ligand-binding specificities, it seems that additional cell-type-specific factors can interact with integrins to modulate their binding activity.

ELISA(enzyme-linked immunosorbent assay) is a method for detecting the concentration of some kind antigen or antibody,such as TGF-βand integrins, using the characteristic of specific binding between antigen-antibody.The method is suitable for determination of cell culture supernatant, serum, plasma,tissue fluid, and urine samples. Meretciel provide quality ELISA kits for R&D,can use to study the Cross talk among TGF-βand integrins.

Humans and mice with fibrillin gene mutations, and mutant mice defective in integrin-mediated activators show the critical role of ECM and integrins in regulating TGF-β signaling. More and more evidence indicates that there is wide crosstalk between integrins and TGF-β signalling. TGF-β affects integrin-mediated cell adhesion and migration by regulating the expression of integrins, their ligands and integrin-associated proteins. On the other hand, several integrins directly control TGF-β activation. Furthermore, a number of integrins can interfere with TGF-β signalling in different ways, including the physical association of integrins with TGF-β receptors,the regulation of the expression of TGF-β signalling pathway components and the modulation of downstream effectors. 

After all,TGF-β–integrin signalling is implicated in normal physiology, as well as in a variety of pathological processes including cancer,systemic sclerosis, idiopathic pulmonary fibrosis and chronic obstructive pulmonary disease. Thus, integrins could provide attractive therapeutic targets to interfere with TGF-β signalling in these processes.

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