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In vitro evaluation of anti-epidermoid cancer activity of Acanthus ebracteatus protein hydrolysate and their effects on apoptosis and cellular proteins

Acanthus ebracteatus Vahl. is commonly consumed with the aim of curing cancer, inflammatory conditions and skin diseases in traditional Thai medicine. It is known to contain various phytochemicals; however, very little is known about the effects of A. ebracteatus protein hydrolysate on cancer cells,...

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Autores principales: Khamwut, Ariya, Jevapatarakul, Damita, Reamtong, Onrapak, T-Thienprasert, Nattanan Panjaworayan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: D.A. Spandidos 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6704294/
https://www.ncbi.nlm.nih.gov/pubmed/31452790
http://dx.doi.org/10.3892/ol.2019.10647
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author Khamwut, Ariya
Jevapatarakul, Damita
Reamtong, Onrapak
T-Thienprasert, Nattanan Panjaworayan
author_facet Khamwut, Ariya
Jevapatarakul, Damita
Reamtong, Onrapak
T-Thienprasert, Nattanan Panjaworayan
author_sort Khamwut, Ariya
collection PubMed
description Acanthus ebracteatus Vahl. is commonly consumed with the aim of curing cancer, inflammatory conditions and skin diseases in traditional Thai medicine. It is known to contain various phytochemicals; however, very little is known about the effects of A. ebracteatus protein hydrolysate on cancer cells, including its molecular mechanisms. The present study therefore investigated the anti-cancer activity of A. ebracteatus protein hydrolysates against epidermoid cancer of the skin cell line A431. Their effects on the apoptosis pathway and expression of proteins involved in the regulation of apoptosis, cell proliferation or cell cycle were also investigated. Crude extract of protein hydrolysate, partially purified peptides and purified peptides extracted from the aerial part of A. ebracteatus were administered to the A431 cells. The cytotoxicity effects were then determined using an MTT assay. As a result, A. ebracteatus protein hydrolysate significantly inhibited A431 cells with half inhibitory concentration equals to 425.9 ng protein/ml. By performing Annexin V assay, the partially purified peptides of A. ebracteatus were demonstrated to enhance the apoptosis pathway. Furthermore, western blot analysis revealed that the partially purified peptides of A. ebracteatus increased protein expression levels of RelA (p65) and Cyclin D1 proteins. However, A. ebracteatus did not increase the expression levels of p53-serine 15 phosphorylation (Ser15P).
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spelling pubmed-67042942019-08-26 In vitro evaluation of anti-epidermoid cancer activity of Acanthus ebracteatus protein hydrolysate and their effects on apoptosis and cellular proteins Khamwut, Ariya Jevapatarakul, Damita Reamtong, Onrapak T-Thienprasert, Nattanan Panjaworayan Oncol Lett Articles Acanthus ebracteatus Vahl. is commonly consumed with the aim of curing cancer, inflammatory conditions and skin diseases in traditional Thai medicine. It is known to contain various phytochemicals; however, very little is known about the effects of A. ebracteatus protein hydrolysate on cancer cells, including its molecular mechanisms. The present study therefore investigated the anti-cancer activity of A. ebracteatus protein hydrolysates against epidermoid cancer of the skin cell line A431. Their effects on the apoptosis pathway and expression of proteins involved in the regulation of apoptosis, cell proliferation or cell cycle were also investigated. Crude extract of protein hydrolysate, partially purified peptides and purified peptides extracted from the aerial part of A. ebracteatus were administered to the A431 cells. The cytotoxicity effects were then determined using an MTT assay. As a result, A. ebracteatus protein hydrolysate significantly inhibited A431 cells with half inhibitory concentration equals to 425.9 ng protein/ml. By performing Annexin V assay, the partially purified peptides of A. ebracteatus were demonstrated to enhance the apoptosis pathway. Furthermore, western blot analysis revealed that the partially purified peptides of A. ebracteatus increased protein expression levels of RelA (p65) and Cyclin D1 proteins. However, A. ebracteatus did not increase the expression levels of p53-serine 15 phosphorylation (Ser15P). D.A. Spandidos 2019-09 2019-07-22 /pmc/articles/PMC6704294/ /pubmed/31452790 http://dx.doi.org/10.3892/ol.2019.10647 Text en Copyright: © Khamwut et al. This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
spellingShingle Articles
Khamwut, Ariya
Jevapatarakul, Damita
Reamtong, Onrapak
T-Thienprasert, Nattanan Panjaworayan
In vitro evaluation of anti-epidermoid cancer activity of Acanthus ebracteatus protein hydrolysate and their effects on apoptosis and cellular proteins
title In vitro evaluation of anti-epidermoid cancer activity of Acanthus ebracteatus protein hydrolysate and their effects on apoptosis and cellular proteins
title_full In vitro evaluation of anti-epidermoid cancer activity of Acanthus ebracteatus protein hydrolysate and their effects on apoptosis and cellular proteins
title_fullStr In vitro evaluation of anti-epidermoid cancer activity of Acanthus ebracteatus protein hydrolysate and their effects on apoptosis and cellular proteins
title_full_unstemmed In vitro evaluation of anti-epidermoid cancer activity of Acanthus ebracteatus protein hydrolysate and their effects on apoptosis and cellular proteins
title_short In vitro evaluation of anti-epidermoid cancer activity of Acanthus ebracteatus protein hydrolysate and their effects on apoptosis and cellular proteins
title_sort in vitro evaluation of anti-epidermoid cancer activity of acanthus ebracteatus protein hydrolysate and their effects on apoptosis and cellular proteins
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6704294/
https://www.ncbi.nlm.nih.gov/pubmed/31452790
http://dx.doi.org/10.3892/ol.2019.10647
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