PMID: 429330Apr 25, 1979Paper

Carbohydrate inhibitors of concanavalin A that inhibit binding of insulin-sepharose to fat cells and antagonize and mimic insulin's bioactivity. A possible role for membrane carbohydrate in insulin's action.

The Journal of Biological Chemistry
H M Katzen

Abstract

A consistent pattern of insulin-like properties is expressed by a variety of glycoside inhibitors of concanavalin A (Con A), and is suggestive of a common mechanism of action to explain these effects. Various exogenously added glycoside derivatives inhibit the binding of insulin-Sepharose beads to insulin receptors on isolated intact rat fat cells with a specificity resembling that for Con A-Sepharose binding to these cells. A more limited number of glycosides tested were also found to inhibit the binding of 125I-insulin, although some enhancement of binding that preceded the inhibition was observed for some of these saccharides. The glycosides also antagonize insulin-stimulated glucose utilization by the cells, but in some cases also mimic the hormone by stimulating glucose utilization. A few glycosides mimic insulin without appearing to antagonize its bioactivity. Radiolabeled glycoside inhibitors fail to bind to insulin in equilibrium dialysis experiments although they readily bind to Con A, indicating that the glycosides act directly on the cell rather than on the insulin molecule. The latter observation is consistent with the ability of those glycosides that act like insulin to do so independent of the hormone. In view of ...Continue Reading

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