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When AMP binds to the subunit, it allosterically activates the complex, making it a more susceptible substrate for phosphorylation at the threonine 172 site, which is more easily phosphorylated in the activation loop of the subunit by the primary upstream AMPK kinase LKB1
Summary of laboratory model and mechanistic signaling observations Data from documented laboratory peptide signaling studies Documented interactions in GH secretagogue research models Peak elevation in research models Teichman et al., 2006 Reduced time to peak GH pulse Bowers et al., 1991 Physiologic rhythm maintenance Teichman et al., 2006 Verified in laboratory settings Raun et al., 1998 GH secretagogue research suggests pathway activity that supports protein synthesis and lipid oxidation modeling
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