title: Biochemical engineering of the N-acyl side chain of sialic acids alters the kinetics of a glycosylated potassium channel Kv3.1.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, Greenville, NC 27834, USA.
authors.forename: M Kristen
authors.initials: MK
authors.lastname: Hall
authors.forename: Werner
authors.initials: W
authors.lastname: Reutter
authors.forename: Thisbe
authors.initials: T
authors.lastname: Lindhorst
authors.forename: Ruth A
authors.initials: RA
authors.lastname: Schwalbe
mesh_terms: D045744:Cell Line, Tumor; D006031:Glycosylation; D006595:Hexosamines / Q000378:metabolism / Q000494:pharmacology*; D006801:Humans; D017136:Ion Transport / Q000235:genetics; D060847:Metabolic Engineering; D019158:N-Acetylneuraminic Acid / Q000235:genetics / Q000378:metabolism*; D051670:Shaw Potassium Channels / Q000235:genetics / Q000378:metabolism*
chemical_list: D006595:Hexosamines; C489597:KCNC1 protein, human; D051670:Shaw Potassium Channels; D019158:N-Acetylneuraminic Acid