Acute lymphoblastic leukaemia is currently treated with bacterial L-asparaginase; however, its side effects raise the need for the development of improved and efficient novel enzymes. Previously, we obtained low anti-asparaginase antibody production and high serum enzyme half-life in mice treated with the P40S/S206C mutant; however, its specific activity was significantly reduced. Thus, our aim was to test single mutants, S206C and P40S, through in vitro and in vivo assays.
View Article and Find Full Text PDFAsparagine is a non-essential amino acid crucial for protein biosynthesis and function, and therefore cell maintenance and growth. Furthermore, this amino acid has an important role in regulating several metabolic pathways, such as tricarboxylic acid cycle and the urea cycle. When compared to normal cells, tumor cells typically present a higher demand for asparagine, making it a compelling target for therapy.
View Article and Find Full Text PDFSeptins are dynamic filament-forming proteins that are recognized as important components of the cytoskeleton and are involved in numerous functions inside the cells, such as cytokinesis, exocytosis, and ciliogenesis and even in defense against pathogenic bacteria. Despite being highly conserved in eukaryotes, there is scarce literature on the role of septins in organisms other than humans and yeast. Therefore, septins from Schistosoma mansoni represent an interesting model to study an unexplored branch of this protein family.
View Article and Find Full Text PDFSeptins are GTP-binding proteins that are highly conserved among eukaryotes and which are usually membrane-associated. They have been linked to several critical cellular functions such as exocytosis and ciliogenesis, but little mechanistic detail is known. Their assembly into filaments and membrane binding properties are incompletely understood and that is specially so for non-human septins where such information would offer therapeutic potential.
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