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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hall MK,Reutter W,Lindhorst T,Schwalbe RA

doi

10.1016/j.febslet.2011.09.021

subject

Has Abstract

pub_date

2011-10-20 00:00:00

pages

3322-7

issue

20

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(11)00700-9

journal_volume

585

pub_type

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