Explore: Insulin Receptors

The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of receptor tyrosine kinase

influences on insulin release by beta cells, because insulin release is inhibited by α2-adrenergic receptors and stimulated by β2-adrenergic receptors. The net

insulin receptor, it can also complement for the effects of insulin. Receptors for IGF-1 are found in vascular smooth muscle, while typical receptors

to respond normally to the hormone insulin or downregulate insulin receptors in response to hyperinsulinemia. Insulin is a hormone that facilitates the

ligands (insulin, IGF-1 and IGF-2), two tyrosine kinase receptors (insulin receptor and IGF-1R receptor) and six ligand binding proteins (IGFBP 1–6). Together

concentrations, the number of surface receptors for insulin is gradually reduced by the accelerated rate of receptor internalization and degradation brought

phosphorylation of the insulin receptors or IGF-1 receptors, upon extracellular ligand binding, induces the cytoplasmic binding of IRS-1 to these receptors, through

needed] Insulin sensitization: Increased sensitivity of insulin receptors on cells leading to decreased insulin resistance, and higher effects of insulin on

α-subunits act as insulin receptors and the insulin molecule acts as a ligand. Together, they form a receptor-ligand complex. Binding of insulin to the α-subunit

formed against insulin receptors, called insulin receptor antibodies. The antibodies attach to insulin receptors and prevent insulin breakdown, or degradation