entegrin

Entegrin is not a widely recognized term as a distinct biological entity in standard databases. In many cases it is encountered as a misspelling or variant of integrin, a large family of cell adhesion receptors. If encountered, it is generally prudent to interpret it as references to the integrin family.

Integrins are transmembrane heterodimeric receptors that mediate adhesion between cells and the extracellular matrix (ECM) or between cells themselves. In humans, 18 alpha subunits and 8 beta subunits combine to form 24 known integrins. They recognize a variety of ECM proteins, including fibronectin, laminin, and collagen, and also participate in cell–cell contacts.

The integrin molecule has a large extracellular domain that binds ligands, a single transmembrane segment, and a short cytoplasmic tail. Activation can occur via inside-out signaling, increasing ligand affinity, or outside-in signaling, where ligand binding triggers intracellular signaling cascades. Cytoplasmic tails interact with adaptor proteins such as talin and kindlin, linking integrins to the actin cytoskeleton and recruiting signaling molecules like FAK and Src. This signaling coordinates processes such as migration, survival, and proliferation, and is modulated by divalent cations, particularly Mg2+ and Ca2+.

Biological roles for integrins are diverse, including development, immune cell trafficking, hemostasis, wound healing, and angiogenesis. They also contribute to disease processes such as cancer metastasis, fibrosis, and inflammatory conditions. Clinically, integrin function is a target for therapy; several antagonists and antibodies against specific integrins have been developed, notably inhibitors of platelet integrin αIIbβ3 used in acute cardiovascular settings, as well as agents targeting other integrins in various diseases.