| Autor: |
Raquel Caminha Dantas, Ludmilla Freire Caetano, Ariany Lima Sousa Torres, Matheus Soares Alves, Emanuelly Thays Muniz Figueiredo Silva, Louhanna Pinheiro Rodrigues Teixeira, Daniel Câmara Teixeira, Renato de Azevedo Moreira, Marcela Helena Gambim Fonseca, Saul Gaudêncio Neto, Leonardo Tondello Martins, Gilvan Pessoa Furtado, Kaio Cesar Simiano Tavares |
| Jazyk: |
angličtina |
| Rok vydání: |
2019 |
| Předmět: |
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| Zdroj: |
BMC Research Notes, Vol 12, Iss 1, Pp 1-6 (2019) |
| Druh dokumentu: |
article |
| ISSN: |
1756-0500 |
| DOI: |
10.1186/s13104-019-4836-5 |
| Popis: |
Abstract 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: |
Directory of Open Access Journals |
| Externí odkaz: |
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