Lenograstim is another rHuG-CSF and is the result of expression in mammalian cells (17). Although the gene is the same as that expressed in E. coli to produce filgrastim, this mammalian expression system does not require the extra methionine and hence possesses a 174-amino acid peptide core. In addition, the single 0-linked carbohydrate chain typical of the endogenous molecule (at Thr133) is found in this form of G-CSF. The function of the carbohydrate is unclear, although several hypotheses have been proposed, including inhibition of proteolytic degradation and aggregation and increased serum half-life (19-21), Cys17 being the apparent target in protein degeneration (22). Although the activity of glycosylated rHuG-CSF has been shown to be greater than that of the nonglycosylated form in vitro (23-26), the activity of the material in vivo is similar to the bacterially synthesized form in all respects (5,27,28) (with the exception of a single drug company-sponsored study ). So how, or indeed whether, the additional carbohydrate plays a role in vivo remains unclear.
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