Fibrillin is a glycoprotein, which is essential for the formation of elastic fibers found in connective tissue. [2] Fibrillin is secreted into the extracellular matrix by fibroblasts and becomes incorporated into the insoluble microfibrils, which appear to provide a scaffold for deposition of elastin. [3]

Fibrillin is an important connective tissue protein in the capsule of the ocular lens, arteries, lung, skin and the dura mater. Fibrillin mutations can result in disease manifestations in each of these tissues. More than 600 mutations have been identified in fibrillin 15, …

Fibrillin-1 (FBN1) is a large, cysteine-rich, calcium binding extracellular matrix glycoprotein encoded by FBN1 gene. It serves as a structural component of microfibrils and provides force-bearing mechanical support in elastic and nonelastic connective tissue.

Fibrillin-1 is the major structural component of the 10 nm-diameter microfibrils that confer key physical and mechanical properties to virtually every tissue, alone and together with elastin in the elastic fibers.

Fibrillins form the structural framework of a unique and essential class of extracellular microfibrils that endow dynamic connective tissues with long-range elasticity. Their biological importance is emphasized by the linkage of fibrillin mutations ...

Fibrillin-1 is a protein that in humans is encoded by the FBN1 gene, located on chromosome 15. [5][6] It is a large, extracellular matrix glycoprotein that serves as a structural component of 10–12 nm calcium-binding microfibrils.

Fibrillins 1 and 2 are the main constituents of the extracellular microfibrils responsible for the biomechanical properties of most tissues and organs.

Fibrillin is a very large molecule whose primary structure is now known from the cloning and sequencing of 10 kb of cDNA. Immunohistochemical results suggest that one of the functions of fibrillin molecules is to contribute to the structure of the microfibril.

Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and non-elastic extracellular matrices, and are known to interact with several binding partners including tropoelastin and integrins. Here, we study the evolution of fibrillin proteins.

Fibrillin (FBN)-1 is a calcium-binding protein that assembles to form 10–12 nm microfibrils in the extracellular matrix (ECM) of elastic and non-elastic tissues. The human gene FBN-1 spans >230 kb (1) on chromosome 15q15-21.1 (2) and is highly fragmented into 65 exons.