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Eradication of Myrosinase-Tethered Cancer Cells by Allyl Isothiocyanate Derived from Enzymatic Hydrolysis of Sinigrin
Sinigrin is present in significant amounts in cruciferous vegetables. Epidemiological studies suggest that the consumption of such vegetables decreases the risk of cancer, and the effect is attributed mainly to allyl isothiocyanate (AITC), a hydrolysis product of sinigrin catalyzed by myrosinase. An...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778717/ https://www.ncbi.nlm.nih.gov/pubmed/35057038 http://dx.doi.org/10.3390/pharmaceutics14010144 |
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author | Tarar, Ammar Alyami, Esmael M. Peng, Ching-An |
author_facet | Tarar, Ammar Alyami, Esmael M. Peng, Ching-An |
author_sort | Tarar, Ammar |
collection | PubMed |
description | Sinigrin is present in significant amounts in cruciferous vegetables. Epidemiological studies suggest that the consumption of such vegetables decreases the risk of cancer, and the effect is attributed mainly to allyl isothiocyanate (AITC), a hydrolysis product of sinigrin catalyzed by myrosinase. Anticancer activity of AITC has been previously investigated for several cancer models, but less attention was paid to delivering AITC on the target site. In this study, the gene sequences of core streptavidin (coreSA) and myrosinase (MYR) were cloned in a pET-30a(+) plasmid and transformed into BL21(DE3) E. coli competent cells. The MYR-coreSA chimeric protein was expressed and purified using immobilized metal affinity chromatography and further characterized by gel electrophoresis, Western blot, and enzyme activity assay. The purified MYR-coreSA chimeric protein was tethered on the outer membrane of biotinylated adenocarcinoma A549 cells and then treated with various concentrations of sinigrin. Our results showed that 20 µM of sinigrin inhibited the growth of A549 cells tethered with myrosinase by ~60% in 48 h. Furthermore, the levels of treated cells undertaken apoptosis were determined by Caspase-3/7 activation and Annexin-V. In summary, sinigrin harnessed like a prodrug catalyzed by myrosinase to the production of AITC, which induced cell apoptosis and arrested the growth of lung cancer cells. |
format | Online Article Text |
id | pubmed-8778717 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87787172022-01-22 Eradication of Myrosinase-Tethered Cancer Cells by Allyl Isothiocyanate Derived from Enzymatic Hydrolysis of Sinigrin Tarar, Ammar Alyami, Esmael M. Peng, Ching-An Pharmaceutics Article Sinigrin is present in significant amounts in cruciferous vegetables. Epidemiological studies suggest that the consumption of such vegetables decreases the risk of cancer, and the effect is attributed mainly to allyl isothiocyanate (AITC), a hydrolysis product of sinigrin catalyzed by myrosinase. Anticancer activity of AITC has been previously investigated for several cancer models, but less attention was paid to delivering AITC on the target site. In this study, the gene sequences of core streptavidin (coreSA) and myrosinase (MYR) were cloned in a pET-30a(+) plasmid and transformed into BL21(DE3) E. coli competent cells. The MYR-coreSA chimeric protein was expressed and purified using immobilized metal affinity chromatography and further characterized by gel electrophoresis, Western blot, and enzyme activity assay. The purified MYR-coreSA chimeric protein was tethered on the outer membrane of biotinylated adenocarcinoma A549 cells and then treated with various concentrations of sinigrin. Our results showed that 20 µM of sinigrin inhibited the growth of A549 cells tethered with myrosinase by ~60% in 48 h. Furthermore, the levels of treated cells undertaken apoptosis were determined by Caspase-3/7 activation and Annexin-V. In summary, sinigrin harnessed like a prodrug catalyzed by myrosinase to the production of AITC, which induced cell apoptosis and arrested the growth of lung cancer cells. MDPI 2022-01-07 /pmc/articles/PMC8778717/ /pubmed/35057038 http://dx.doi.org/10.3390/pharmaceutics14010144 Text en © 2022 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 | Article Tarar, Ammar Alyami, Esmael M. Peng, Ching-An Eradication of Myrosinase-Tethered Cancer Cells by Allyl Isothiocyanate Derived from Enzymatic Hydrolysis of Sinigrin |
title | Eradication of Myrosinase-Tethered Cancer Cells by Allyl Isothiocyanate Derived from Enzymatic Hydrolysis of Sinigrin |
title_full | Eradication of Myrosinase-Tethered Cancer Cells by Allyl Isothiocyanate Derived from Enzymatic Hydrolysis of Sinigrin |
title_fullStr | Eradication of Myrosinase-Tethered Cancer Cells by Allyl Isothiocyanate Derived from Enzymatic Hydrolysis of Sinigrin |
title_full_unstemmed | Eradication of Myrosinase-Tethered Cancer Cells by Allyl Isothiocyanate Derived from Enzymatic Hydrolysis of Sinigrin |
title_short | Eradication of Myrosinase-Tethered Cancer Cells by Allyl Isothiocyanate Derived from Enzymatic Hydrolysis of Sinigrin |
title_sort | eradication of myrosinase-tethered cancer cells by allyl isothiocyanate derived from enzymatic hydrolysis of sinigrin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778717/ https://www.ncbi.nlm.nih.gov/pubmed/35057038 http://dx.doi.org/10.3390/pharmaceutics14010144 |
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