Fibrillin-2 (FBN2)

Fibrillin-2 is a large extracellular matrix glycoprotein encoded by the FBN2 gene and is critical for microfibril formation, which provides elasticity and structural integrity to various tissues such as skin, ligaments, and blood vessels. Fibrillin-2 interacts with elastin and other matrix proteins to direct the assembly of elastic fibers, especially during embryonic development. It also plays an important regulatory role by binding and sequestering growth factors—including transforming growth factor-beta and certain BMPs and GDFs—thus controlling their bioavailability and signaling. Mutations in FBN2 cause congenital contractural arachnodactyly, a disorder marked by joint contractures, long slender fingers, and connective tissue anomalies. Unlike fibrillin-1 (FBN1), which is implicated in Marfan syndrome and cardiovascular complications, FBN2 mutations primarily result in musculoskeletal abnormalities without significant cardiovascular or ocular involvement. Fibrillin-2 has no direct pharmacological antagonists or drugs targeting it, and its clinical relevance is largely as a biomarker for diagnosis of related connective tissue disorders rather than as a therapeutic target.

Other names

Fibrillin-2PlacensinFBN2DA9Fibrillin 5CCAFBN2_HUMANFibrillin 2 (congenital contractural arachnodactyly)

Not applicable (no drugs or small molecules known to specifically target fibrillin-2 in current clinical use; interactions are primarily structural and regulatory within the extracellular matrix)