Integrins and Extracellular Matrix

Cell adhesion plays a major role in cell communication and regulation and is of fundamental importance in the development and maintenance of tissues. Cell-extracellular matrix (ECM) interactions have global implications in many disease states through processes such as angiogenesis, apoptosis, and inflammation and are critical for normal and tumor cell signal transduction pathways. Knowledge of the molecular mechanisms involved in these interactions will facilitate the development of novel therapeutic molecules to benefit patients diagnosed with diseases such as arthritis and cancer.

The extracellular matrix is a complex structural and functional network of proteins and proteoglycans that can interact simultaneously with multiple cell surface receptors. The majority of these proteins are glycosylated, including a wide variety of collagens, laminins, fibronectin, and elastins. ECM proteins can influence cellular function through a complex feedback mechanism. A class of cell surface proteins known as integrins mediates the adhesion of cells to ECM proteins and endothelial surfaces. These receptors anchor cells to the ECM leading to the transduction of signaling events that regulate cell survival, proliferation, and migration. Functional integrins are heterodimeric molecules, containing one alpha and one beta transmembrane glycoprotein subunit that are non-covalently bound together. Different integrin combinations may recognize a single ECM ligand, while others bind several different ECM proteins.

More than 18a and 8b subunits with numerous splice variant isoforms have been identified in mammals, with a and b subunits combining in some 22 pairings to form receptors for ECM proteins. The b subunit contains the main binding site, the specificity of which is modified by a metal binding to an a subunit. Certain integrins can also bind to soluble ligands or to counter-receptors on adjacent cells, such as the intracellular adhesion molecules (ICAMs) resulting in aggregation of cells. The most common ECM ligands for integrin binding are fibronectin, laminin, and collagen. Integrins seem to bind using a population approach. Each integrin-ligand binding is of low affinity and thus has relatively weak adhering strength. Larger local concentrations of integrin bindings yield proportionately stronger adhesions (called focal contacts), thus allowing many different areas on the cell membrane independent control over local binding or detachment. Integrin binding also induces extracellular signaling. Millipore is a market leader in antibodies, proteins and assays for the identification, localization and blocking of cellular adhesion mechanisms.

ECM Proteins

For detailed information on Millipore’s extensive line of ECM products, please refer to the Microporous Membrane-based Cell Culture and the Pathway Tools chapters of this handbook.

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