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In vitro antitumor activity of Latcripin-15 regulator of chromosome condensation 1 domain protein

Cancer is one of the most significant health problems worldwide and thus the development of novel therapeutic agents with fewer side effects is required. The present study investigated the in vitro anticancer effects of a newly isolated fungal protein. In this study, Latcripin-15 (LP-15) regulator o...

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Autores principales: Tian, Li, Wang, Xiaoli, Li, Xingyun, Liu, Ben, Zhang, Wei, Cao, Jing, Ning, Anhong, Huang, Min, Zhong, Mintao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: D.A. Spandidos 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5103913/
https://www.ncbi.nlm.nih.gov/pubmed/27899975
http://dx.doi.org/10.3892/ol.2016.5106
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author Tian, Li
Wang, Xiaoli
Li, Xingyun
Liu, Ben
Zhang, Wei
Cao, Jing
Ning, Anhong
Huang, Min
Zhong, Mintao
author_facet Tian, Li
Wang, Xiaoli
Li, Xingyun
Liu, Ben
Zhang, Wei
Cao, Jing
Ning, Anhong
Huang, Min
Zhong, Mintao
author_sort Tian, Li
collection PubMed
description Cancer is one of the most significant health problems worldwide and thus the development of novel therapeutic agents with fewer side effects is required. The present study investigated the in vitro anticancer effects of a newly isolated fungal protein. In this study, Latcripin-15 (LP-15) regulator of chromosome condensation 1 (RCC1) domain protein, which is obtained from the Lentinula edodes C(91-3) fungal strain, was identified, cloned, expressed, purified and re-folded to assess the in vitro antitumor activity of the protein. LP-15 RCC1 full-length cDNA was isolated from Lentinula edodes using 3′ and 5′-rapid amplification of cDNA ends and then cloned, expressed, purified and re-folded in vitro. In addition, the effects of the isolated LP-15 RCC1 protein's functional domain on the viability and apoptosis of human lung cancer A549 cells were assessed by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay, transmission electron microscopy, flow cytometry and Hoechst 33258 staining. The LP-15 RCC1 functional domain protein was successfully expressed, purified and re-folded in vitro. Treatment with the LP-15 RCC1 functional domain protein significantly reduced tumor cell viability and induced apoptosis in A549 cells. The results of the present study indicate that the LP-15 RCC1 functional domain requires further investigation as a novel therapeutic agent for cancer therapy.
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spelling pubmed-51039132016-11-29 In vitro antitumor activity of Latcripin-15 regulator of chromosome condensation 1 domain protein Tian, Li Wang, Xiaoli Li, Xingyun Liu, Ben Zhang, Wei Cao, Jing Ning, Anhong Huang, Min Zhong, Mintao Oncol Lett Articles Cancer is one of the most significant health problems worldwide and thus the development of novel therapeutic agents with fewer side effects is required. The present study investigated the in vitro anticancer effects of a newly isolated fungal protein. In this study, Latcripin-15 (LP-15) regulator of chromosome condensation 1 (RCC1) domain protein, which is obtained from the Lentinula edodes C(91-3) fungal strain, was identified, cloned, expressed, purified and re-folded to assess the in vitro antitumor activity of the protein. LP-15 RCC1 full-length cDNA was isolated from Lentinula edodes using 3′ and 5′-rapid amplification of cDNA ends and then cloned, expressed, purified and re-folded in vitro. In addition, the effects of the isolated LP-15 RCC1 protein's functional domain on the viability and apoptosis of human lung cancer A549 cells were assessed by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay, transmission electron microscopy, flow cytometry and Hoechst 33258 staining. The LP-15 RCC1 functional domain protein was successfully expressed, purified and re-folded in vitro. Treatment with the LP-15 RCC1 functional domain protein significantly reduced tumor cell viability and induced apoptosis in A549 cells. The results of the present study indicate that the LP-15 RCC1 functional domain requires further investigation as a novel therapeutic agent for cancer therapy. D.A. Spandidos 2016-11 2016-09-08 /pmc/articles/PMC5103913/ /pubmed/27899975 http://dx.doi.org/10.3892/ol.2016.5106 Text en Copyright: © Tian 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
Tian, Li
Wang, Xiaoli
Li, Xingyun
Liu, Ben
Zhang, Wei
Cao, Jing
Ning, Anhong
Huang, Min
Zhong, Mintao
In vitro antitumor activity of Latcripin-15 regulator of chromosome condensation 1 domain protein
title In vitro antitumor activity of Latcripin-15 regulator of chromosome condensation 1 domain protein
title_full In vitro antitumor activity of Latcripin-15 regulator of chromosome condensation 1 domain protein
title_fullStr In vitro antitumor activity of Latcripin-15 regulator of chromosome condensation 1 domain protein
title_full_unstemmed In vitro antitumor activity of Latcripin-15 regulator of chromosome condensation 1 domain protein
title_short In vitro antitumor activity of Latcripin-15 regulator of chromosome condensation 1 domain protein
title_sort in vitro antitumor activity of latcripin-15 regulator of chromosome condensation 1 domain protein
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5103913/
https://www.ncbi.nlm.nih.gov/pubmed/27899975
http://dx.doi.org/10.3892/ol.2016.5106
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