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• W1965515057 endingPage "3508" @default.
• W1965515057 startingPage "3499" @default.
• W1965515057 abstract "The number of therapeutic proteins has increased dramatically over the past years and most of the therapeutic proteins in the market today are glycoproteins. Usually, recombinant glycoproteins are produced in mammalian cell lines, such as Chinese-hamster-ovary-cells to obtain mammalian-type of glycosylation. The terminal monosaccharide of N-linked complex glycans is typically occupied by sialic acid. Presence of this sialic acid affects absorption, serum half-life, and clearance from the serum, as well as the physical, chemical and immunogenic properties of the respective glycoprotein. From a manufacturing perspective, the degree of sialylation is crucial since sialylation varies the function of the product. In addition, insufficient or inconsistent sialylation is also a major problem for the process consistency. Sialylation of over-expressed glycoproteins in all mammalian cell lines commonly used in biotechnology for the production of therapeutic glycoproteins is incomplete and there is a need for strategies leading to homogenous, naturally sialylated glycoproteins. This review will shortly summarize the biosynthesis of sialic acids and describe some recent strategies to increase or modify sialylation of specific therapeutic glycoproteins." @default.
• W1965515057 created "2016-06-24" @default.
• W1965515057 creator A5044707922 @default.
• W1965515057 creator A5047994109 @default.
• W1965515057 creator A5067577751 @default.
• W1965515057 date "2009-10-01" @default.
• W1965515057 modified "2023-09-24" @default.
• W1965515057 title "Increasing the sialylation of therapeutic glycoproteins: The potential of the sialic acid biosynthetic pathway" @default.
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• W1965515057 doi "https://doi.org/10.1002/jps.21684" @default.
• W1965515057 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19199295" @default.
• W1965515057 hasPublicationYear "2009" @default.
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