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J. Biol. Chem., Vol. 266, Issue 13, 8115-8121, May, 1991

Insulin stimulates the generation of two putative insulin mediators, inositol-glycan and diacylglycerol in BC3H-1 myocytes

S Suzuki, K Sugawara, Y Satoh and T Toyota
Third Department of Internal Medicine, Tohoku University School of Medicine, Sendai, Japan.

Recent evidence suggests that insulin induces hydrolysis of phosphatidylinositol-glycan (PI-G) and releases inositol-glycan (IG) and diacylglycerol (DAG). These two mediators are speculated to mediate different insulin actions. In this study, we examined metabolic labeling of PI-G in BC3H-1 myocytes with known precursors of PI-G. PI-G was metabolically labeled with [3H]myo-inositol, [3H]glucosamine, [3H]galactose, [3H]glycerol, and [3H]myristic acid. The treatment of 3H- labeled PI-G with phosphatidylinositol-specific phospholipase C liberated [3H]myo-inositol, [3H]glucosamine, or [3H]galactosamine- labeled IgGs, and [3H]glycerol or [3H]myristic acid-labeled DAG. In BC3H-1 myocytes, insulin induced phosphodiesteratic hydrolysis of PI-G and stimulated generation of IGs and DAG. Released IGs were labeled with [3H]myo-inositol, [3H]glucosamine, and [3H]galactose. Released DAG was labeled with [3H] glycerol and [3H]myristic acid. The IG had a dose- dependent insulin-like activity on glucose oxidation and lipogenesis without affecting glucose transport in rat adipocytes. Insulin increased 3H radioactivities of IG and insulin-mimicking activities of IG. These results provided further evidence that hydrolysis of PI-G and generation of IGs and DAG might be early steps in some insulin actions.
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