Journal
FEBS LETTERS
Volume 581, Issue 22, Pages 4195-4198Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.07.060
Keywords
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosaminekinase; N-acetylmannosamine; sialuria; recombinant glycoprotein
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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. (c) 2007 Published by, Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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