Expression of a recombinant bacterial l-asparaginase in human cells
| Autor: | L. T. Martins, Renato de Azevedo Moreira, Gilvan Pessoa Furtado, Saul Gaudencio Neto, Ludmilla Freire Caetano, Matheus Soares Alves, Daniel Câmara Teixeira, Emanuelly Thays Muniz Figueiredo Silva, Ariany Lima Sousa Torres, Marcela Helena Gambim Fonseca, Louhanna Pinheiro Rodrigues Teixeira, Raquel Caminha Dantas, Kaio César Simiano Tavares |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Antigenicity Glycosylation lcsh:Medicine Context (language use) Acute lymphoblastic leukemia medicine.disease_cause General Biochemistry Genetics and Molecular Biology Epitope law.invention 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine law medicine Escherichia coli Hypersensitivity Asparaginase Humans Cloning Molecular lcsh:Science (General) lcsh:QH301-705.5 chemistry.chemical_classification Chemistry lcsh:R Temperature General Medicine Hydrogen-Ion Concentration In vitro Recombinant Proteins Research Note l-Asparaginase 030104 developmental biology Enzyme HEK293 Cells Biochemistry lcsh:Biology (General) 030220 oncology & carcinogenesis Recombinant DNA lcsh:Q1-390 |
| Zdroj: | BMC Research Notes, Vol 12, Iss 1, Pp 1-6 (2019) BMC Research Notes |
| ISSN: | 1756-0500 |
| Popis: | Objective l-Asparaginase (ASNase) is an enzyme used in the treatment of acute lymphoblastic leukemia (ALL). As the therapeutic ASNases has bacterial origin, severe side effects are associated with its use, among them hypersensitivity and inactivation of the enzyme. In this context, the objective of this work was to produce a recombinant ASNase of bacterial origin in human cells in order to determine the presence and consequences of potential post-translational modifications on the enzyme. Results Recombinant ASNase was expressed in human cells with a molecular weight of 60 kDa, larger than in Escherichia coli, which is 35 kDa. N-glycosylation analysis demonstrated that the increased molecular weight resulted from the addition of glycans to the protein by mammalian cells. The glycosylated ASNase presented in vitro activity at physiological pH and temperature. Given that glycosylation can act to reduce antigenicity by masking protein epitopes, our data may contribute to the development of an alternative ASNase in the treatment of ALL in patients who demonstrate side effects to currently marketed enzymes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
| Nepřihlášeným uživatelům se plný text nezobrazuje | K zobrazení výsledku je třeba se přihlásit. |