Fibulin-2
Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene. It is a member of the fibulin family of extracellular matrix glycoproteins, which have roles in cellular functions such as adhesion and migration.
Structure[edit | edit source]
Fibulin-2 is a large glycoprotein with a molecular mass of approximately 200 kDa. It is composed of three types of repeating modules: an EGF-like module, a fibronectin type III module, and a unique C-terminal module. The EGF-like modules are responsible for the protein's ability to bind to other proteins and to calcium ions, while the fibronectin type III modules are thought to mediate interactions with cell surface receptors.
Function[edit | edit source]
Fibulin-2 is involved in a variety of cellular processes, including cell adhesion, migration, and angiogenesis. It is thought to play a role in the assembly and stabilization of elastic fibers, which are important components of the extracellular matrix. Fibulin-2 can interact with other extracellular matrix proteins, such as fibronectin, laminin, and collagen, and can also bind to cell surface receptors, such as integrins.
Clinical significance[edit | edit source]
Mutations in the FBLN2 gene have been associated with a variety of diseases, including age-related macular degeneration, cancer, and certain types of congenital heart disease. In cancer, fibulin-2 has been found to be overexpressed in certain types of tumors, suggesting that it may play a role in tumor progression.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD