Fibronectin Fragments / RGD Peptides
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Introduction of Fibronectin Fragments
Fibronectin (FN) exists in stroma, cell surface, plasma and other body fluids. It is a large multi-domain glycoprotein that interacts with a variety of macromolecules, including cytoskeleton and extracellular matrix components, circulating components of the blood coagulation, fibrinolysis, acute phase and complement systems, and cell surface receptors of a variety of cells. Including fibroblasts, neurons, phagocytes and bacteria. FN also interacts with itself and binds to several small molecules, such as ganglioside and sugar. As one of the major cell adhesion molecules, FN plays a key role in many important physiological processes, such as embryogenesis, wound healing, hemostasis and thrombosis. The changes, degradation and combination of fibronectin expression are closely related to a large number of pathological occurrence, including cancer and fibrosis.
Introduction of RGD (Arg-Gly-Asp)
It is a conserved and common basic component in the structure of many extracellular matrix (ECM) proteins and plasma proteins. It is also the basic unit of cell recognition system. RGD peptide, as the recognition site of the interaction between integrin and its ligands, mediates the adhesion between cells and extracellular matrix and cells, and has the function of signal transduction, thus mediating many important life activities. In 1984, Pierschbacher and Ruodluherci first identified RGD as a specific binding site of fibronectin (FN) to its receptor.
Mode of Action
FN is generally secreted in the form of dimer, and the molecular weight of each monomer is 220-250 kDa. It is mainly synthesized by fibroblasts, endothelial cells, chondrocytes, glial cells and muscle cells, and distributed around. Organ transplantation stimulates a series of immune cascade reactions, and FN acts as an activator in the activation of T cells. All FN are encoded by the same gene, and different translation products are produced by different tissue-specific cleavage of post-transcriptional mRNA. Multiple domains on FN can bind to collagen, fibrin, heparin and specific cell membrane receptors. Among them, the well-known binding domain is the Arg-Gly-Asp sequence (RGD), which regulates cell adhesion after integrin recognition. FN is involved in many physiological functions in vivo, such as adsorption and migration between cells, cytoskeleton assembly, tyrosine phosphorylation and tumor metastasis.
Function of Fibronectin Fragments/RGD Peptides
- As a biochemical reagent, it provides a basis for cell culture and industrial application of bioengineering.
- It is used in the diagnosis and treatment of many diseases (such as wound repair and healing, cancer diagnosis and treatment, etc.).
- Affect cell adhesion, migration or tumor metastasis, embryonic development, growth and differentiation.
References
- Guillem-Marti, J., Gelabert, M., Heras-Parets, A., Pegueroles, M., Ginebra, M. P., & Manero, J. M. (2019). RGD mutation of the heparin binding II fragment of fibronectin for guiding mesenchymal stem cell behavior on titanium surfaces. ACS applied materials & interfaces, 11(4), 3666-3678.
- Chuang, W. J., & Chang, Y. S. (2018). U.S. Patent No. 9,969,791. Washington, DC: U.S. Patent and Trademark Office.
