L-Lysine α-Oxidase: Enzyme with Anticancer Properties

L-lysine α-oxidase (LO), one of L-amino acid oxidases, deaminates L-lysine with the yield of H<sub>2</sub>O<sub>2</sub>, ammonia, and α-keto-ε-aminocaproate. Multiple in vitro and in vivo studies have reported cytotoxic, antitumor, antimetastatic, and antitumor activity of LO...

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Autores principales: Elena V. Lukasheva, Gulalek Babayeva, Saida Sh. Karshieva, Dmitry D. Zhdanov, Vadim S. Pokrovsky
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Publicado: MDPI AG 2021
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Acceso en línea:https://doaj.org/article/bdfdb068d6764ddab93558ebef56e2ac
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spelling oai:doaj.org-article:bdfdb068d6764ddab93558ebef56e2ac2021-11-25T18:39:05ZL-Lysine α-Oxidase: Enzyme with Anticancer Properties10.3390/ph141110701424-8247https://doaj.org/article/bdfdb068d6764ddab93558ebef56e2ac2021-10-01T00:00:00Zhttps://www.mdpi.com/1424-8247/14/11/1070https://doaj.org/toc/1424-8247L-lysine α-oxidase (LO), one of L-amino acid oxidases, deaminates L-lysine with the yield of H<sub>2</sub>O<sub>2</sub>, ammonia, and α-keto-ε-aminocaproate. Multiple in vitro and in vivo studies have reported cytotoxic, antitumor, antimetastatic, and antitumor activity of LO. Unlike asparaginase, LO has a dual mechanism of action: depletion of L-lysine and formation of H<sub>2</sub>O<sub>2</sub>, both targeting tumor growth. Prominent results were obtained on murine and human tumor models, including human colon cancer xenografts HCT 116, LS174T, and T47D with maximum T/C 12, 37, and 36%, respectively. The data obtained from human cancer xenografts in immunodeficient mice confirm the potential of LO as an agent for colon cancer treatment. In this review, we discuss recently discovered molecular mechanisms of biological action and the potential of LO as anticancer enzyme.Elena V. LukashevaGulalek BabayevaSaida Sh. KarshievaDmitry D. ZhdanovVadim S. PokrovskyMDPI AGarticleanticancer enzymestumor therapyL-amino acid oxidaseL-lysine α-oxidaseL-lysinecolon cancer treatmentMedicineRPharmacy and materia medicaRS1-441ENPharmaceuticals, Vol 14, Iss 1070, p 1070 (2021)
institution DOAJ
collection DOAJ
language EN
topic anticancer enzymes
tumor therapy
L-amino acid oxidase
L-lysine α-oxidase
L-lysine
colon cancer treatment
Medicine
R
Pharmacy and materia medica
RS1-441
spellingShingle anticancer enzymes
tumor therapy
L-amino acid oxidase
L-lysine α-oxidase
L-lysine
colon cancer treatment
Medicine
R
Pharmacy and materia medica
RS1-441
Elena V. Lukasheva
Gulalek Babayeva
Saida Sh. Karshieva
Dmitry D. Zhdanov
Vadim S. Pokrovsky
L-Lysine α-Oxidase: Enzyme with Anticancer Properties
description L-lysine α-oxidase (LO), one of L-amino acid oxidases, deaminates L-lysine with the yield of H<sub>2</sub>O<sub>2</sub>, ammonia, and α-keto-ε-aminocaproate. Multiple in vitro and in vivo studies have reported cytotoxic, antitumor, antimetastatic, and antitumor activity of LO. Unlike asparaginase, LO has a dual mechanism of action: depletion of L-lysine and formation of H<sub>2</sub>O<sub>2</sub>, both targeting tumor growth. Prominent results were obtained on murine and human tumor models, including human colon cancer xenografts HCT 116, LS174T, and T47D with maximum T/C 12, 37, and 36%, respectively. The data obtained from human cancer xenografts in immunodeficient mice confirm the potential of LO as an agent for colon cancer treatment. In this review, we discuss recently discovered molecular mechanisms of biological action and the potential of LO as anticancer enzyme.
format article
author Elena V. Lukasheva
Gulalek Babayeva
Saida Sh. Karshieva
Dmitry D. Zhdanov
Vadim S. Pokrovsky
author_facet Elena V. Lukasheva
Gulalek Babayeva
Saida Sh. Karshieva
Dmitry D. Zhdanov
Vadim S. Pokrovsky
author_sort Elena V. Lukasheva
title L-Lysine α-Oxidase: Enzyme with Anticancer Properties
title_short L-Lysine α-Oxidase: Enzyme with Anticancer Properties
title_full L-Lysine α-Oxidase: Enzyme with Anticancer Properties
title_fullStr L-Lysine α-Oxidase: Enzyme with Anticancer Properties
title_full_unstemmed L-Lysine α-Oxidase: Enzyme with Anticancer Properties
title_sort l-lysine α-oxidase: enzyme with anticancer properties
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/bdfdb068d6764ddab93558ebef56e2ac
work_keys_str_mv AT elenavlukasheva llysineaoxidaseenzymewithanticancerproperties
AT gulalekbabayeva llysineaoxidaseenzymewithanticancerproperties
AT saidashkarshieva llysineaoxidaseenzymewithanticancerproperties
AT dmitrydzhdanov llysineaoxidaseenzymewithanticancerproperties
AT vadimspokrovsky llysineaoxidaseenzymewithanticancerproperties
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