“…Both, hydrocortisone and predinisolone, were shown to improve sialylation [73,74]. Higher concentrations of these glucocorticoids compared to DEX were required to increase sialic acid content to the same extent [73].…”
Section: Hydrocortisone and Predinisolonementioning
confidence: 99%
“…Glutamate [52] Replacing glutamine with glutamate improves galactosylation and complement-dependent cytotoxicity Glutamine [74] Adaptation of a cell line to glutamine-free growth improves the antennarity of N-linked glycoforms Glycine [76] Glycine supplementation improves glycosylation by increasing sialic acid content of glycoforms Proline [75] Proline supplementation increases sialylation in hyperosmotic cell culture Proline [76] Proline supplementation improves glycosylation by increasing sialic acid content of glycoforms Threonine [76] Threonine supplementation improves glycosylation by increasing sialic acid content of glycoforms…”
Section: Amino Acid Reference Effect On Glycosylationmentioning
“…Both, hydrocortisone and predinisolone, were shown to improve sialylation [73,74]. Higher concentrations of these glucocorticoids compared to DEX were required to increase sialic acid content to the same extent [73].…”
Section: Hydrocortisone and Predinisolonementioning
confidence: 99%
“…Glutamate [52] Replacing glutamine with glutamate improves galactosylation and complement-dependent cytotoxicity Glutamine [74] Adaptation of a cell line to glutamine-free growth improves the antennarity of N-linked glycoforms Glycine [76] Glycine supplementation improves glycosylation by increasing sialic acid content of glycoforms Proline [75] Proline supplementation increases sialylation in hyperosmotic cell culture Proline [76] Proline supplementation improves glycosylation by increasing sialic acid content of glycoforms Threonine [76] Threonine supplementation improves glycosylation by increasing sialic acid content of glycoforms…”
Section: Amino Acid Reference Effect On Glycosylationmentioning
“…Hence, the presence of cell-proliferation regulation-associated cell signaling and structural proteins could be linked with the preparation of cells for higher rate of proliferation in the upcoming log-phase. Cells in lag phase have been reported to high intercellular stress level compared to cells in log, stationary and death-phase [35]. The stress proteins present in the microvesicles could be expected to be associated with regulation of intracellular stress in lag-phase of culture.…”
Section: Functional Analysis Of Microvesicular Proteinsmentioning
“…Mucin-type O-glycosylation in mammalian cells typically varies in the frequency of site occupancy and display a mixture of different structures [82]. In human cells, the generation of homogeneous mucin-type O-glycans is hampered by the large repertoire of competing glycosyltransferases ( Figure 5A and B).…”
Section: What Are the Targets For O-glycanengineering?mentioning
Glyco-engineering of expression platforms is increasingly recognized as an important strategy to improve biopharmaceuticals. A better understanding and control of the factors leading to glycan heterogeneity will allow simplified production of recombinant glycoprotein therapeutics with less variation in terms of glycosylation. Further technological advances will have a major impact on manufacturing processes and may provide a completely new class of glycoprotein therapeutics with customized functions.
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