fibronectiin

Fibronectin is a high-molecular-weight glycoprotein that plays a crucial role in various biological processes, including cell adhesion, migration, and differentiation. It is found in the extracellular matrix of tissues and is synthesized by various cell types, including fibroblasts, endothelial cells, and smooth muscle cells. Fibronectin is composed of two distinct regions: a cell-binding region and a heparin-binding region. The cell-binding region contains multiple arginine-glycine-aspartic acid (RGD) motifs, which are recognized by integrins, a family of cell surface receptors. This interaction is essential for cell adhesion and migration. The heparin-binding region, on the other hand, facilitates the binding of fibronectin to the extracellular matrix and other proteins, such as fibrin and collagen. Fibronectin is also involved in wound healing, angiogenesis, and tumor metastasis. Its expression and function are regulated by various factors, including growth factors, cytokines, and matrix metalloproteinases. Dysregulation of fibronectin has been linked to several diseases, including cancer, fibrosis, and atherosclerosis.