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Engineered asparaginase from Erwinia chrysanthemi enhances asparagine hydrolase activity and diminishes enzyme immunoreactivity - a new promise to treat acute lymphoblastic leukemia
Journal of Chemical Technology and Biotechnology ( IF 2.8 ) Pub Date : 2021-09-25 , DOI: 10.1002/jctb.6933
Iris Munhoz Costa 1 , Débora Custódio Moura 1 , Guilherme Meira Lima 1 , Adalberto Pessoa 1 , Camila Oresco dos Santos 2 , Marcos Antônio Oliveira 3 , Gisele Monteiro 1
Affiliation  

The treatment of acute lymphoblastic leukemia (ALL) uses the biopharmaceutical l-asparaginase (ASNase) as the main medication. This drug, from bacterial origin (Escherichia coli or Erwinia chrysanthemi), depletes l-asparagine (Asn) and secondarily l-glutamine (Gln – GLNase activity) from the bloodstream, leading leukemic cells to die by deprivation of Asn. The use of ASNase is limited by the high incidence of adverse effects, which collectively can specifically impair quality of life of patients. Its high toxicity caused by the product of the hydrolysis of amino acids and the formation of anti-ASNase antibodies often required treatment interruption, thus reducing the chances of cure and increasing the rates of disease relapse.

中文翻译:

来自菊花的工程化天冬酰胺酶可增强天冬酰胺水解酶活性并降低酶免疫反应性——治疗急性淋巴细胞白血病的新希望

急性淋巴细胞白血病(ALL)的治疗中使用的生物制药-asparaginase(ASNase)为主要药物。这种药物,来自细菌来源(大肠杆菌菊花欧文氏菌),消耗l-天冬酰胺 (Asn) 和次要l-谷氨酰胺(Gln – GLNase 活性)来自血流,导致白血病细胞因缺乏 Asn 而死亡。ASNase 的使用受到不良反应发生率高的限制,这些不良反应共同会特别损害患者的生活质量。其由氨基酸水解产物和抗 ASNase 抗体形成引起的高毒性通常需要中断治疗,从而降低治愈机会并增加疾病复发率。
更新日期:2021-12-03
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