Thursday, January 16, 2014
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Cell culture and mouse
studies identified mutants of Escherichia coli l-asparaginase II (EcA)
that could help treat ALL. EcA depletes l-asparagine,
which is required for protein synthesis in ALL cells but has a short
half-life and induces immunogenicity. In cultured ALL cells and leukemic
blast cells from patients with ALL, several mutants of EcA induced cell cycle
arrest and apoptosis with greater potency than EcA and did not affect
peripheral blood monocytes. Antibody-mediated inactivation of EcA limits the
effectiveness of repeated treatment. In mice and in sera from patients
treated with wild-type EcA, mutant EcA showed less cross-reactivity with
neutralizing antibodies than wild-type EcA. Next steps include additional
experiments in clinical samples.
Hakko Kirin Co. Ltd. markets Leunase, which contains l-asparaginase obtained from a
genetically modified E. coli strain and is used to treat ALL and other
Pharmaceuticals plc markets Erwinaze, an Erwinia
chrysanthemi-derived asparaginase, to treat ALL in patients who developed
hypersensitivity to E. coli-derived asparaginase.
Jazz Pharmaceuticals and Alize
Pharma S.A.S. have a pegylated l-asparaginase from E. chrysanthemi in Phase I
trials for ALL.
Published online Jan. 16, 2014
Patent application filed;
available for licensing
Mehta, R.K. et al. J.
Biol. Chem.; published online Dec. 2, 2013;
Contact: Avinash Sonawane, KIIT University, Bhubaneswar,
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