Inositolphosphoglycans and diacylglycerol are possible mediators in the glycogenic effect of GLP-1(7-36)amide in BC3H-1 myocytes

A potent glycogenic effect of GLP‐1(7‐36)amide has been found in rat hepatocytes and skeletal muscle, and specific receptors for this peptide, which do not seem to be associated with the adenylate cyclase—cAMP system, have been detected in these tissue membranes. On the other hand, inositolphosphoglycan molecules (IPGs) have been implicated as second messengers of the action of insulin. In this work, we have found, in differentiated BC3H‐1 myocytes, specific binding of [125I]GLP‐1(7‐36)amide, and a stimulatory effect of the peptide on glycogen synthesis, confirming the findings in rat skeletal muscle. Also, GLP‐1(7‐36)amide modulates the cell content of radiolabelled glycosylphosphatidylinositols (GPIs) and increases the production of diacylglycerol (DAG), in the same manner as insulin acts, indicating hydrolysis of GPIs and an immediate and short‐lived generation of IPGs. Thus, IPGs and DAG could be mediators in the glycogenic action of GLP‐1(7‐36)amide in skeletal muscle.