integrinereceptoren

Integrinereceptoren are a family of cell surface receptors that play a crucial role in cell adhesion, migration, and signaling. They are heterodimeric proteins composed of an alpha (α) and a beta (β) subunit, each of which is a member of a distinct subfamily. The α subunits are non-covalently associated with β subunits, which are themselves dimers. This combination allows integrins to interact with various extracellular matrix (ECM) proteins and other cell surface molecules, facilitating cell-cell and cell-ECM interactions.

Integrins are classified into several subfamilies based on their β subunits. The most well-known subfamilies include the β1, β2, and β3 subfamilies. Each subfamily has distinct functions and ligand specificities. For example, integrins containing the β1 subunit, such as α1β1 and α2β1, are involved in the adhesion of cells to the ECM, particularly collagen. Integrins with the β2 subunit, like αLβ2 and αMβ2, are involved in leukocyte trafficking and immune responses. Integrins with the β3 subunit, such as αIIbβ3 and α5β1, are critical for platelet aggregation and angiogenesis, respectively.

Integrin activation involves conformational changes that expose cryptic binding sites, allowing them to interact with their ligands. This activation can be induced by various stimuli, including mechanical forces, growth factors, and cytokines. Once activated, integrins can transmit signals into the cell, influencing gene expression, cell proliferation, and differentiation.

Integrinereceptoren are implicated in numerous physiological and pathological processes, including wound healing, inflammation, cancer metastasis, and tissue remodeling. Dysregulation of integrin function has been linked to various diseases, such as atherosclerosis, fibrosis, and cancer. Therefore, integrins are important targets for therapeutic interventions aimed at modulating cell adhesion and signaling.