Suppression of myoblast fusion by concanavalin A: possible involvement of membrane fluidity.

Experimental evidence is presented which is consistent with the involvement of membrane fluidity during myoblast fusion. Treatment of pretrypsinized myoblasts with tetrameric Con A, but not with the dimeric succinyl derivate, inhibits fusion. Inhibition is reversed by treatment with alpha-methyl-D-mannoside or subsequent trypsinization. No inhibition is observed when the lectin is incubated with cells at 4 degrees C unless the incubation is followed by treatment with glycogen, a multivalent Con A cross-linking agent. This effect of glycogen is reversed by subsequent treatment with alpha-amylase. Direct observation of Con A-binding site topography by transmission electron microscopy of membrane replicas of cells labelled with Con A and haemocyanin reveals that inhibition of fusion correlates with a clustered distribution of Con A-binding sites, whereas normal fusion correlates with a dispersed distribution.