RENATA DAMIANI
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Resumo IPEN-doc 20256 Effects of butyrate and manganese on productivity, sialylation, N-glycosylation site occupancy and biological properties of CHO-derived thyrotropin2014 - DAMIANI, RENATA; OLIVEIRA, JOAO E.; ALMEIDA, BEATRIZ E.; SANT'ANA, PATRICIA M.; DALMORA, SERGIO L.; BARTOLINI, PAOLO; RIBELA, MARIA T.C.P.Artigo IPEN-doc 20113 Reversed-phase performance liquid chromatography as an alternative to animal bioassay for human thyrotropin potency determination2014 - ALMEIDA, B.E.; DAMIANI, R.; OLIVEIRA, J.E.; DALMORA, S.L.; TORJESEN, P.A.; BARTOLINI, P.; RIBELA, M.T.C.P.Artigo IPEN-doc 13175 Influence of a reduced COsub(2) environment on the secretion yield potency and N-glycan structures of recombinant thyrotropin from CHO cells2008 - OLIVEIRA, JOAO E.; DAMIANI, RENATA; VORAUER-UHL, KAROLA; BARTOLINI, PAOLO; RIBELA, MARIA T.C.P.Artigo IPEN-doc 14267 Stable expression of a human-like sialylated recombinant thyrotropin in a Chinese hamster ovary cell line expressing α2,6-sialyltransferase2009 - DAMIANI, RENATA; OLIVEIRA, JOAO E.; VORAUER-UHL, KAROLA; PERONI, CIBELE N.; VIANNA, ELIZABETH G.; BARTOLINI, PAOLO; RIBELA, MARIA T.C.P.A CHO cell line, previously genetically modified by the introduction of rat α2,6-sialyltransferase cDNA, generated for the first time a human-like sialylated recombinant hTSH (hlsr-hTSH) more similar to the native hormone, with 61% of α2,3- and 39% of α2,6-linked sialic acid residues. The best clone, when submitted to gene amplification with up to 8 μM methotrexate, presented a secretion level of ∼2 μg hTSH/106 cells/day, useful for product purification and characterization. The relative molecular masses (Mr) of the heterodimer and of the α- and β-subunits of purified hlsr-hTSH, determined by MALDI-TOF mass spectrometry, and the relative hydrophobicities, determined by RP-HPLC, were not remarkably different from those presented by two r-hTSH preparations secreted by normal CHO cells. Some differences were observed, though, in N-glycan composition, with more tri- and much more tetra-sialylated structures in hlsr-hTSH. When analyzed via an in vivo bioassay based on hTSH-induced T4 release in mice, hlsr-hTSH was shown to be equipotent (p > 0.05) with the commercial preparation of r-hTSH (Thyrogen), and 1.6-fold more potent than native hTSH (p < 0.001).