CARLOS ROBERTO JORGE SOARES

CARLOS ROBERTO JORGE SOARES

(Fonte: Lattes)

Resumo

Graduado em Farmácia e Bioquímica pela Universidade de São Paulo (1989), realizou Mestrado (1995) e Doutorado (2000) em Tecnologia Nuclear - Aplicações pela Universidade de São Paulo. Atualmente é pesquisador do Instituto de Pesquisas Energéticas (IPEN-CNEN/SP) e professor de pós-graduação vinculado à Universidade de São Paulo. Com experiência em biotecnologia na expressão de proteínas recombinantes por bactéria e por células de mamífero. Atua principalmente no seguinte tema: síntese, purificação, caracterização e aplicações de hormônios recombinantes. Atualmente é Gerente do Centro de Biotecnologia do IPEN. (Texto extraído do Currículo Lattes em 08 out. 2021)

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Expression of glycosylated human prolactin in HEK293 cells and related N‑glycan composition analysis
2019 - SILVA, FELIPE D.; OLIVEIRA, JOÃO E.; FREIRE, RENAN P.; SUZUKI, MIRIAM F.; SOARES, CARLOS R.; BARTOLINI, PAOLO
Prolactin (PRL) is a hormone produced by the pituitary gland with innumerable functions, such as lactation, reproduction, osmotic and immune regulation. The present work describes the synthesis of hPRL in human embryonic kidney (HEK293) cells, transiently transfected with the pcDNA-3.4-TOPO® vector carrying the hPRL cDNA. A concentration of ~ 20 mg/L, including glycosylated (G-hPRL) and non-glycosylated (NG-hPRL) human prolactin, was obtained, with ~ 19% of G-hPRL, which is higher than that observed in CHO-derived hPRL (~ 10%) and falling within the wide range of 5–30% reported for pituitary-derived hPRL. N-Glycoprofiling analysis of G-hPRL provided: (i) identification of each N-glycan structure and relative intensity; (ii) average N-glycan mass; (iii) molecular mass of the whole glycoprotein and relative carbohydrate mass fraction; (iv) mass fraction of each monosaccharide. The data obtained were compared to pituitary- and CHO-derived G-hPRL. The whole MM of HEK-derived G-hPRL, determined via MALDI–TOF-MS, was 25,123 Da, which is 0.88% higher than pit- and 0.61% higher than CHO-derived G-hPRL. The main difference with the latter was due to sialylation, which was ~ sevenfold lower, but slightly higher than that observed in native G-hPRL. The “in vitro” bioactivity of HEK-G-hPRL was ~ fourfold lower than that of native G-hPRL, with which it had in common also the number of N-glycan structures.