Insulinlika

Insulinlika is a term used in biology to describe molecules that resemble insulin in structure or function. It is often applied to hormones and peptide ligands within the insulin/IGF family, as well as to insulin-like peptides found in invertebrates. In humans and other vertebrates, the principal insulin-like peptides are insulin, insulin-like growth factor 1 (IGF-1), and IGF-2. They are produced as larger precursor molecules and processed into mature peptides that are held together by disulfide bonds between A and B chains.

These molecules exert their effects by binding to cell surface receptors, mainly the insulin receptor (IR) and the IGF-1 receptor (IGF1R). Some ligands can activate both receptors or form hybrid IR/IGF1R receptors, with varying affinities. Signaling cascades commonly involved include the PI3K-Akt pathway, which promotes glucose uptake, glycogen synthesis, and protein translation, and the MAPK pathway, which influences cell growth and differentiation.

Physiological roles of insulinlika peptides are diverse. Insulin governs systemic glucose homeostasis and lipid metabolism; IGF-1 and IGF-2 support growth, development, and anabolic processes. In other species, insulin-like peptides regulate metabolism, reproduction, and lifespan, reflecting the broad importance of insulin-like signaling in biology.

Clinical relevance and research: disruptions or alterations in insulin-like signaling are linked to metabolic diseases such as type 2 diabetes and insulin resistance; dysregulated IGF signaling can contribute to cancer and overgrowth syndromes. Therapeutically, insulin and insulin analogs are used to treat diabetes, while IGF signaling components are targets of cancer therapies and metabolic research. In model organisms, insulin-like peptides illuminate roles in aging, nutrient sensing, and development.