fibronectiinin

Fibronectin is a glycoprotein that is present in the extracellular matrix of connective tissue in vertebrates. It plays a critical role in cell adhesion and migration, and is involved in various physiological processes, including wound healing and blood clotting.

Fibronectin has a molecular weight of approximately 400 kilodaltons, and is composed of two types of subunits: A and B. The A subunit contains a collagen-binding domain, while the B subunit contains a heparin-binding domain. These domains allow fibronectin to interact with other molecules, such as collagen and integrins, which are involved in cell adhesion and signaling.

Fibronectin is produced by various cell types, including fibroblasts, endothelial cells, and smooth muscle cells. It is secreted into the extracellular matrix, where it forms a network of fibers that provide structural support and play a role in cell adhesion and migration. Fibronectin has also been shown to be involved in various pathological processes, including cancer, fibrosis, and vascular disease.

Fibronectin is highly conserved across species, and has similar structure and function in humans, mice, and other mammals. It has also been identified in some invertebrates, such as insects and amphibians, where it appears to play similar roles in development and tissue repair.

Studies of fibronectin have implications for our understanding of various diseases, including cancer and cardiovascular disease. Furthermore, the structure and function of fibronectin have been used as models for the design of novel biomaterials and therapeutic agents.