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 Wilson

The 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.


Share this       

Select your language of interest to view the total content in your interested language

Table of Contents

Google Scholar citation report
Citations : 11

received 11 citations as per Google Scholar report

Flyer
Global Tech Summit puqiiipuqiii