Abstract
The dynamics of a glycosylated potassium channel, Kv3.1, are altered by biochemical engineering of the N-acyl side chain of sialic acids.
Author(s): Charles WilsonThe sialic acid of complex N-glycans can be biochemically engineered by substituting the physiological precursor N-acetylmannosamine with non-natural N-acylmannosamines. The Kv3. 1 glycoprotein, a neuronal voltage-gated potassium channel, contains sialic acid. Western blots of the Kv3. 1 glycoprotein isolated from transfected B35 neuroblastoma cells incubated with N-acylmannosamines verified sialylated N-glycans attached to the Kv3. 1 glycoprotein. Outward ionic currents of Kv3. 1 transfected B35 cells treated with Npentanoylmannosamine or N-propanoylmannosamine had slower activation and inactivation rates than those of untreated cells. Therefore, the N-acyl side chain of sialic acid is intimately connected with the activation and inactivation rates of this glycosylated potassium channel.