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Enhanced sialylation of EPO by overexpression of UDP‐GlcNAc 2‐epimerase/ManAc kinase containing a sialuria mutation in CHO cells
Author(s) -
Bork Kaya,
Reutter Werner,
Weidemann Wenke,
Horstkorte Rüdiger
Publication year - 2007
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.2007.07.060
Subject(s) - sialic acid , chinese hamster ovary cell , glycoprotein , enzyme , biochemistry , mutation , erythropoietin , recombinant dna , kinase , chemistry , function (biology) , n acetylneuraminic acid , microbiology and biotechnology , biology , gene , receptor , genetics
Sialylation (e.g. expression of sialic acid) plays a crucial role for function and stability of most glycoproteins. The key enzyme for the biosynthesis of sialic acid is the UDP‐ N ‐acetylglucosamine 2‐epimerase/ N ‐acetylmannosamine‐kinase (GNE). Mutations in the binding site of the feedback inhibitor CMP‐sialic acid of the GNE leads to sialuria, a disease in which patients produce sialic acid in gram scale. Here, we report on the use in biotechnology of sialuria‐mutated GNE. Expression of the sialuria‐mutated GNE in CHO‐cells leads to increased sialylation of recombinant expressed erythropoietin (EPO). Our data show that sialuria‐mutated‐GNE over‐expressing cells are the perfect platform to express highly sialylated therapeutic proteins, such as EPO.