IGF-1 Signaling describes the complex intracellular cascade initiated by the binding of Insulin-like Growth Factor 1 (IGF-1) to its specific cell surface receptor, the IGF-1R. This pathway is a critical mediator of the effects of Growth Hormone (GH), primarily promoting cell proliferation, inhibiting apoptosis, and driving systemic growth, particularly in muscle and bone tissue. Proper regulation of this signaling is essential for metabolic health, tissue repair, and the overall maintenance of lean body mass throughout the lifespan.
Origin
The term combines the abbreviation for Insulin-like Growth Factor 1 with “signaling,” referring to the transmission of a biological message within the cell. IGF-1 was named for its structural homology to proinsulin and its ability to stimulate cell growth, a function originally attributed to “sulfation factor.” Its discovery and subsequent characterization in the mid-20th century clarified the mechanism by which growth hormone exerts its anabolic effects.
Mechanism
The binding of IGF-1 to the transmembrane tyrosine kinase receptor (IGF-1R) causes receptor dimerization and autophosphorylation of its intracellular domain. This phosphorylation event recruits and activates a series of intracellular adaptor proteins, most notably the Insulin Receptor Substrate (IRS) proteins. The signal is then transduced primarily through the PI3K/Akt pathway, which promotes glucose uptake and protein synthesis, or the MAPK pathway, which drives cellular proliferation and differentiation.
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