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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(2)O(2), 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 mecha...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8618108/ https://www.ncbi.nlm.nih.gov/pubmed/34832852 http://dx.doi.org/10.3390/ph14111070 |
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author | Lukasheva, Elena V. Babayeva, Gulalek Karshieva, Saida Sh. Zhdanov, Dmitry D. Pokrovsky, Vadim S. |
author_facet | Lukasheva, Elena V. Babayeva, Gulalek Karshieva, Saida Sh. Zhdanov, Dmitry D. Pokrovsky, Vadim S. |
author_sort | Lukasheva, Elena V. |
collection | PubMed |
description | L-lysine α-oxidase (LO), one of L-amino acid oxidases, deaminates L-lysine with the yield of H(2)O(2), 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(2)O(2), 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 | Online Article Text |
id | pubmed-8618108 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86181082021-11-27 L-Lysine α-Oxidase: Enzyme with Anticancer Properties Lukasheva, Elena V. Babayeva, Gulalek Karshieva, Saida Sh. Zhdanov, Dmitry D. Pokrovsky, Vadim S. Pharmaceuticals (Basel) Review L-lysine α-oxidase (LO), one of L-amino acid oxidases, deaminates L-lysine with the yield of H(2)O(2), 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(2)O(2), 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. MDPI 2021-10-22 /pmc/articles/PMC8618108/ /pubmed/34832852 http://dx.doi.org/10.3390/ph14111070 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Lukasheva, Elena V. Babayeva, Gulalek Karshieva, Saida Sh. Zhdanov, Dmitry D. Pokrovsky, Vadim S. L-Lysine α-Oxidase: Enzyme with Anticancer Properties |
title | 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_short | L-Lysine α-Oxidase: Enzyme with Anticancer Properties |
title_sort | l-lysine α-oxidase: enzyme with anticancer properties |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8618108/ https://www.ncbi.nlm.nih.gov/pubmed/34832852 http://dx.doi.org/10.3390/ph14111070 |
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