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-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.

Fibrillin-1 and fibrillin-2 are large cysteine-rich glycoproteins that serve two key physiological functions: as supporting structures that impart tissue integrity and as regulators of signaling events that instruct cell performance. The structural ...

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 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.

The FBN1 gene provides instructions for making a large protein called fibrillin-1. This protein is transported out of cells into the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells.

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.

Fibrillin is an essential glycoprotein that plays a crucial role in the formation of elastic fibers, providing tissue elasticity and stability to the elastic fibers. It includes three isoforms: fibrillin-1, fibrillin-2, and fibrillin-3, each with specific functions in elastic fiber formation and tissue regulation.

2000年12月20日 · Fibrillin-1 has a striking modular organisation which is dominated by multiple tandem repeats of the calcium binding epidermal growth factor-like (cbEGF) domain. This review focuses on recent studies which have investigated the structural and functional role of calcium binding to cbEGF domains in fibrillin-1 and 10-12 nm microfibrils.

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.