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• W4361235415 abstract "<div>Abstract<p>Acute lymphoblastic leukemia (ALL) is the most common type of pediatric cancer, although about 4 of every 10 cases occur in adults. The enzyme drug l-asparaginase serves as a cornerstone of ALL therapy and exploits the asparagine dependency of ALL cells. In addition to hydrolyzing the amino acid l-asparagine, all FDA-approved l-asparaginases also have significant l-glutaminase coactivity. Since several reports suggest that l-glutamine depletion correlates with many of the side effects of these drugs, enzyme variants with reduced l-glutaminase coactivity might be clinically beneficial if their antileukemic activity would be preserved. Here we show that novel low l-glutaminase variants developed on the backbone of the FDA-approved <i>Erwinia chrysanthemi</i> l-asparaginase were highly efficacious against both T- and B-cell ALL, while displaying reduced acute toxicity features. These results support the development of a new generation of safer l-asparaginases without l-glutaminase activity for the treatment of human ALL.</p><p><b>Significance:</b> A new l-asparaginase–based therapy is less toxic compared with FDA-approved high l-glutaminase enzymes <i>Cancer Res; 78(6); 1549–60. ©2018 AACR</i>.</p></div>" @default.
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• W4361235415 date "2023-03-31" @default.
• W4361235415 modified "2023-10-18" @default.
• W4361235415 title "Data from A Novel l-Asparaginase with low l-Glutaminase Coactivity Is Highly Efficacious against Both T- and B-cell Acute Lymphoblastic Leukemias <i>In Vivo</i>" @default.
• W4361235415 doi "https://doi.org/10.1158/0008-5472.c.6509787" @default.
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