RENATA DAMIANI
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Resumo IPEN-doc 24397 Carbohydrate composition and site-occupancy determination in pituitary and recombinant preparations of human thyrotropin2017 - BARTOLINI, PAOLO; RIBELA, MARIA T.C.P.; DAMIANI, RENATA; SILVA, FELIPE D.; LIMA, ELIANA R.; OLIVEIRA, JOAO E.; PERONI, CIBELE N.; TORJESEN, PETER A.; SOARES, CARLOS R.Human thyrotropin (hTSH) is a glycoprotein with three potential glycosylation sites: two in the -subunit and one in the -subunit. Carbohydrate site-occupancy is frequently neglected in glycoprotein characterization, even if related to folding, trafficking, initiation of inflammation, host defence and congenital disorders of glycosylation (CDG). For the first-time N-glycoprofiling analysis was applied to site-occupancy determination of two native pituitary hTSH, in comparison with three CHO-derived preparations of hTSH, a widely used biopharmaceutical. A single methodology provided: (i) average N-glycan mass; (ii) mass fraction of each monosaccharide and of sulfate; (iii) percent carbohydrate. The results indicate that occupancy (65–87%) and carbohydrate mass (12–19%) can be 34–57% higher in recombinant hormones. The average glycan mass is 24% lower in pituitary hTSH and contains ∼3-fold fewer moles of galactose (P < 0.005) and sialic acid (P < 0.01). The number of moles of fucose per mole of hTSH was found 2.5-fold higher in the pituitary preparations. One of these native preparations, presenting the smallest glycan mass, lowest occupancy, GalNAc, sulfate, Gal and sialic acid contents, also presented the lowest in vivo bioactivity and circulatory half-life. This methodology, extremely important for comparing a recombinant biopharmaceutical to its native equivalent, can be applied to any physiologically or clinical relevant glycoprotein.Artigo IPEN-doc 22995 N-Glycoprofiling analysis for carbohydrate composition and site-occupancy determination in a poly-glycosylated protein: human thyrotropin of different origins2017 - RIBELA, MARIA T.C.P.; DAMIANI, RENATA; SILVA, FELIPE D.; LIMA, ELIANA R.; OLIVEIRA, JOAO E.; PERONI, CIBELE N.; TORJESEN, PETER A.; SOARES, CARLOS R.; BARTOLINI, PAOLOHuman thyrotropin (hTSH) is a glycoprotein with three potential glycosylation sites: two in the -subunit and one in the -subunit. These sites are not always occupied and occupancy is frequently neglected in glycoprotein characterization, even though it is related to folding, trafficking, initiation of inflammation and host defense, as well as congenital disorders of glycosylation (CDG). For the first time N-glycoprofiling analysis was applied to the site-occupancy determination of two native pituitary hTSH, in comparison with three recombinant preparations of hTSH, a widely used biopharmaceutical. A single methodology provided the: (i) average N-glycan mass; (ii) mass fraction of each monosaccharide and of sulfate; and (iii) percent carbohydrate. The results indicate that the occupancy (65%–87%) and carbohydrate mass (12%–19%) can be up to 34%–57% higher in recombinant hormones. The average glycan mass is 24% lower in pituitary hTSH and contains ~3-fold fewer moles of galactose (p < 0.005) and sialic acid (p < 0.01). One of the two native preparations, which had the smallest glycan mass together with the lowest occupancy and GalNAc, sulfate, Gal and sialic acid contents, also presented the lowest in vivo bioactivity and circulatory half-life. The methodology described, comparing a recombinant biopharmaceutical to its native equivalent, can be applied to any physiologically or clinical relevant glycoprotein.Resumo IPEN-doc 11433 Comparative studies of pituitary (NIDDK, USA) and recombinant (Thyrogen and IPEN) human thyroid stimulating hormone (hTSH) for what concerns cabohydrate structures and charge heterogeneity2006 - OLIVEIRA, J.E.; LOUREIRO, R.F.; CARVALHO, C.M.; DAMIANI, R.; BARTOLINI, P.; RIBELA, M.T.C.P.Resumo IPEN-doc 16160 Charge isomer distribution of different pituitary and recombinant human thyrotropin (hTSH) preparations2010 - DAMIANI, R.; OLIVEIRA, J.E.; ALMEIDA, B.E.; BARTOLINI, P.; RIBELA, M.T.C.P.Resumo IPEN-doc 18702 Sodium butyrate greatly enhances human thyrotropin (hTSH) synthesis by serum-free CHO cell culture with alterations of the carbohydrate moiety2012 - DAMIANI, R.; OLIVEIRA, J.E.; ALMEIDA, B.E.; BARTOLINI, P.; RIBELA, M.T.C.P.