Integrin

Integrins are protein molecules that are present in all animal cells except red blood cells. They are permanently anchored in the cell membrane and cross the cell membrane. They belong to the most transmembrane proteins.

Integrins connect with other cells and with the extracellular matrix. Furthermore, they are important for the signal transmission between cells and their environment. They are also referred to as adhesion molecules. At least three other proteins play in cell - cell and cell - matrix interaction and communication play an important role - the cadherins, CAMs ( cell adhesion molecules ) and selectins.

Has The extracellular protein domain of these transmembrane proteins binding sites with the RGD recognition feature such as fibronectin in fibroblasts or "non- RGD proteins " such as intercellular adhesion molecules ( ICAMs ), collagens and laminin ( in epithelial cells).

Integrins are glycoproteins. Of structurally they are heterodimers, that is composed of two glycoprotein chains interconnected. In humans, can be constructed from the previously known 18 alpha and 8 beta subunits of 24 different integrins in other studies it is assumed that 19 alpha and 8 beta subunits that form 25 integrin heterodimers.

Integrins play an important role in many processes within the body. Example, you can bind viruses, allow the directed migration of white blood cells in inflammatory foci or convey certain steps of blood coagulation.

The change in binding between integrins and binding molecules it has become an important goal of developing new drugs. Other possible applications are, inter alia, in inflammatory diseases and in oncology. Natalizumab, an inhibitor of binding between the occurring on white blood cell integrin α4β1 ( VLA-4 = engl. " Very late antigen- 4 ") with VCAM- 1 (Eng. " vascular cell adhesion molecule 1 ") and fibronectin, has been used to as a drug treatment of relapsing forms of multiple sclerosis admitted.