The lack of insulin mimetic or antagonistic effects of methyl-alpha-D-Mannoside in iso-osmolar solutions.

Transduction of insulin binding into metabolic control in isolated rat adipocytes apparently requires intact cell surface carbohydrate. The ability of certain lectins and some glycosides to mimic and/or inhibit the actions of insulin had been cited as evidence supporting the hypothesis that a concanavalin A-like binding site on fat cells is crucial to this function. Such a binding site could explain the stimulation by methyl-alpha-D-mannoside of glucose oxidation or its ability to antagonize the effect of insulin on lipolysis. The present study corroborated these effects of methyl-alpha-D-mannoside in hyperosmolar medium, but shows that the effects vanish when osmolarity is maintained within physiological limits. Osmolarity alone could not explain all of the complex effect observed, but it can be concluded that earlier data suggesting methyl-alpha-D-mannoside mimics or antagonizes the actions of insulin cannot be used to support the above hypothesis.