IGF-1 LR3 Muscle Growth refers to the anabolic effect of the modified peptide Insulin-like Growth Factor-1 Long R3 (IGF-1 LR3) on skeletal muscle tissue, primarily promoting hypertrophy and hyperplasia. IGF-1 LR3 is an analog of the naturally occurring IGF-1, engineered to have a significantly extended half-life and reduced binding affinity for the Insulin-like Growth Factor Binding Proteins (IGFBPs). This modification enhances its bioavailability and sustained signaling to the muscle cells. While studied in research contexts for its potent anabolic properties, its use in non-clinical settings for muscle enhancement is often associated with regulatory and safety concerns.
Origin
This specific peptide analog was developed in the field of molecular endocrinology and biotechnology, aimed at creating a research tool with enhanced stability and potency compared to native IGF-1. The ‘LR3’ designation refers to the addition of an arginine (R) at position 3 and a 13 amino acid extension (Long) at the N-terminus of the IGF-1 molecule. Its application to muscle growth stems directly from the known physiological role of endogenous IGF-1 in mediating the anabolic effects of growth hormone. The non-clinical interest in this molecule is driven by its prolonged biological activity.
Mechanism
The primary mechanism involves IGF-1 LR3 binding to the IGF-1 Receptor (IGF-1R) on the surface of muscle cells, initiating an intracellular signaling cascade, most notably through the PI3K/Akt/mTOR pathway. Activation of this pathway stimulates protein synthesis and inhibits protein degradation, leading to muscle cell hypertrophy. Furthermore, it is believed to promote muscle cell hyperplasia by stimulating the differentiation and fusion of satellite cells into new muscle fibers. The reduced binding to IGFBPs ensures that a greater fraction of the peptide remains unbound and biologically active over a longer duration, sustaining the anabolic signal.
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