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 H2 O2, 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 H2 O2, 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. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Authors
Lukasheva E.V. 1 , Babayeva G. 1, 2 , Karshieva S.Sh.2 , Zhdanov D.D. 3 , Pokrovsky V.S. 1, 2, 4
Journal
Publisher
MDPI AG
Number of issue
11
Language
English
Status
Published
Number
1070
Volume
14
Year
2021
Organizations
  • 1 Department of Biochemistry, Peoples’ Friendship University of Russia (RUDN University), Miklukho—Maklaya Street 6, Moscow, 117198, Russian Federation
  • 2 Laboratory of Combined Treatment, N.N. Blokhin Cancer Research Center, Kashirskoe Shosse 24, Moscow, 115478, Russian Federation
  • 3 Institute of Biomedical Chemistry, Pogodinskaya Street 10/8, Moscow, 119121, Russian Federation
  • 4 Center of Genetics and Life Sciences, Sirius University of Science and Technology, Federal Territory Sirius, 1 Olimpiisky Prospect, Sochi, 354340, Russian Federation
Keywords
Anticancer enzymes; Colon cancer treatment; L-amino acid oxidase; L-lysine; L-lysine α-oxidase; Tumor therapy
Date of creation
16.12.2021
Date of change
25.05.2023
Short link
https://repository.rudn.ru/en/records/article/record/76538/
Share

Other records