Anticancer enzyme L-lysine α-oxidase: Properties and application perspectives

Fungal L-lysine α-oxidase (1.4.3.14) (LO) from Trichoderma harzianum Rifai presents an oxidoreductase with a firmly attached coenzyme - FAD. This stable enzyme catalyzes an oxidative deamination of L-lysine yielding hydrogen peroxide, ammonia, and α-keto acid. LO exhibits antitumor activity toward 5 of 12 tested transplantable tumors. The sensitive tumors were ascitic hepatoma 22 (T/C = 201%, CR = 66%); mammary adenocarcinoma Ca-755 (TGI = 96%); melanoma B-16 (TGI = 81%); AKATOL (TGI = 75%); RSHM 5 (TGI = 79%). LO therapeutic activity was observed within a wide range of doses, 35-350 U/kg, by intraperitoneal daily injections for 5 d. Contrary to Escherichia coli L-asparaginase, LO demonstrates its antitumor activity by the low therapeutic doses in vivo within a wide range of optimal doses and through another antitumor spectrum. Fisher lymphadenosis L-5178y highly sensitive toward L-asparaginase appeared to be LO resistant. The possible mechanisms of LO antitumor activity through the key biochemical processes are discussed.

Авторы
Treshalina H.M.1 , Lukasheva E.V. 2 , Sedakova L.A.1 , Firsova G.A.1 , Guerassimova G.K.1 , Gogichaeva N.V. 2 , Berezov T.T. 2
Редакторы
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Сборник материалов конференции
Издательство
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Номер выпуска
1-3
Язык
Английский
Страницы
267-273
Статус
Опубликовано
Подразделение
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Ссылка
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DOI
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Номер
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Том
88
Год
2000
Организации
  • 1 Blokhin Cancer Research Center, Russian Academy of Medical Sciences, Moscow, Russian Federation
  • 2 Department of Biochemistry, Russian Peoples' Friendship University, Moscow, Russian Federation
Ключевые слова
Anticancer testing in vivo; Antitumor enzyme therapy; L-amino acid oxidase; L-lysine α-oxidase; Schedule of L-lysine α-oxidase anticancer therapy
Дата создания
19.10.2018
Дата изменения
19.10.2018
Постоянная ссылка
https://repository.rudn.ru/ru/records/article/record/424/