Erwinia asparaginase for acute lymphoblastic leukemia in children with hypersensitivity to E coli-derived asparaginase

With related Commentary

Erwinia chrysanthemi, an asparaginase derived from the bacterium E chrysanthemi, was recently approved by the Food and Drug Administration as a component of multiagent chemotherapy in patients with acute lymphoblastic leukemia (ALL) who have developed hypersensitivity to Escherichia coli (E coli)-derived asparaginase and pegaspargase.¹ Hypersensitivity to E coli-derived asparaginase may occur in up to 30% of patients² with ALL, a common childhood cancer. Leukemic cells are not able to synthesize the amino acid asparagine, which is required for protein metabolism and survival, because of a lack of asparagine synthetase activity. Erwinia-derived asparaginase reduces circulating levels of asparagine by catalyzing the deamidation of asparagine to aspartic acid and ammonia. The reduction of circulating asparagine results in cytotoxicity specific for leukemic cells by depriving them of their source of the amino acid.

*For PDFs of the full report and accompanying Commentary, click on the links to the left of this introduction.

With related Commentary

Erwinia chrysanthemi, an asparaginase derived from the bacterium E chrysanthemi, was recently approved by the Food and Drug Administration as a component of multiagent chemotherapy in patients with acute lymphoblastic leukemia (ALL) who have developed hypersensitivity to Escherichia coli (E coli)-derived asparaginase and pegaspargase.¹ Hypersensitivity to E coli-derived asparaginase may occur in up to 30% of patients² with ALL, a common childhood cancer. Leukemic cells are not able to synthesize the amino acid asparagine, which is required for protein metabolism and survival, because of a lack of asparagine synthetase activity. Erwinia-derived asparaginase reduces circulating levels of asparagine by catalyzing the deamidation of asparagine to aspartic acid and ammonia. The reduction of circulating asparagine results in cytotoxicity specific for leukemic cells by depriving them of their source of the amino acid.

*For PDFs of the full report and accompanying Commentary, click on the links to the left of this introduction.

With related Commentary

Erwinia chrysanthemi, an asparaginase derived from the bacterium E chrysanthemi, was recently approved by the Food and Drug Administration as a component of multiagent chemotherapy in patients with acute lymphoblastic leukemia (ALL) who have developed hypersensitivity to Escherichia coli (E coli)-derived asparaginase and pegaspargase.¹ Hypersensitivity to E coli-derived asparaginase may occur in up to 30% of patients² with ALL, a common childhood cancer. Leukemic cells are not able to synthesize the amino acid asparagine, which is required for protein metabolism and survival, because of a lack of asparagine synthetase activity. Erwinia-derived asparaginase reduces circulating levels of asparagine by catalyzing the deamidation of asparagine to aspartic acid and ammonia. The reduction of circulating asparagine results in cytotoxicity specific for leukemic cells by depriving them of their source of the amino acid.

*For PDFs of the full report and accompanying Commentary, click on the links to the left of this introduction.