Referenced in: none

Automatically associated channels: Kv3.1 , Slo1

Title: Biochemical engineering of the N-acyl side chain of sialic acids alters the kinetics of a glycosylated potassium channel Kv3.1.

Authors: M Kristen Hall, Werner Reutter, Thisbe Lindhorst, Ruth A Schwalbe

Journal, date & volume: FEBS Lett., 2011 Oct 20 , 585, 3322-7

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/21945320

Abstract
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 N-pentanoylmannosamine 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.