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Biochemical engineering of the N ‐acyl side chain of sialic acids alters the kinetics of a glycosylated potassium channel Kv3.1
Author(s) -
Hall M. Kristen,
Reutter Werner,
Lindhorst Thisbe,
Schwalbe Ruth A.
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.09.021
Subject(s) - sialic acid , chemistry , potassium channel , transfection , voltage gated potassium channel , glycoprotein , biochemistry , potassium , glycan , kinetics , microbiology and biotechnology , biophysics , biology , gene , organic chemistry , physics , quantum mechanics
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.