Search results for "asparaginase"
showing 4 items of 4 documents
L-asparaginase inhibits invasive and angiogenic activity and induces autophagy in ovarian cancer
2012
Recent work identified L-asparaginase (L-ASP) as a putative therapeutic target for ovarian cancer. We suggest that L-ASP, a dysregulator of glycosylation, would interrupt the local microenvironment, affecting the ovarian cancer cell-endothelial cell interaction and thus angiogenesis without cytotoxic effects. Ovarian cancer cell lines and human microvascular endothelial cells (HMVEC) were exposed to L-ASP at physiologically attainable concentrations and subjected to analyses of endothelial tube formation, invasion, adhesion and the assessment of sialylated proteins involved in matrix-associated and heterotypic cell adhesion. Marked reduction in HMVEC tube formation in vitro, HMVEC and ovari…
Unique Microbial Catabolic Pathway for the Human Core N-Glycan Constituent Fucosyl-α-1,6-N-Acetylglucosamine-Asparagine
2020
The survival of commensal bacteria in the human gut partially depends on their ability to metabolize host-derived molecules. The use of the glycosidic moiety of N-glycoproteins by bacteria has been reported, but the role of N-glycopeptides or glycoamino acids as the substrates for bacterial growth has not been evaluated. We have identified in Lactobacillus casei strain BL23 a gene cluster (alf-2) involved in the catabolism of the glycoamino acid fucosyl-α-1,6-N-GlcNAc-Asn (6′FN-Asn), a constituent of the core-fucosylated structures of mammalian N-glycoproteins. The cluster consists of the genes alfHC, encoding a major facilitator superfamily (MFS) permease and the α-l-fucosidase AlfC, and t…
Characteristics and outcome of adult patients with acute promyelocytic leukemia and increased body mass index treated with the PETHEMA Protocols
2020
PETHEMA, HOVON, PALG, GATLA cooperative groups.
Stabilization of anti-leukemic enzyme l-asparaginase by immobilization on polysaccharide levan
2001
Abstract Biologically active fructose polymer levan from Zymomonas mobilis of different molecular mass (75 and 2000 kDa) was covalently coupled to anti-leukemic enzyme Erwinia carotovora l -asparaginase. The method used for the immobilization of the enzyme involved periodate oxidation of the polysaccharide, followed by reductive alkylation. A gentle periodate oxidation of levan (oxidation degree ≤24%) resulted in the highest residual enzyme activity (≥55%). The K m(app.) of glycoconjugates was higher than the K m of native l -asparaginase. The conjugation of l -asparaginase widened the optimum pH range of the enzyme. The electrophoretic mobility in polyacrylamide gel of glycoconjugates obta…