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Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid
Earthworms’ celomic fluid has long attracted scientists’ interest due to their toxic properties. It has been shown that the elimination of coelomic fluid cytotoxicity to normal human cells was crucial for the generation of the non-toxic Venetin-1 protein-polysaccharide complex, which exhibits select...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10292018/ https://www.ncbi.nlm.nih.gov/pubmed/37377864 http://dx.doi.org/10.3389/fmolb.2023.1128320 |
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author | Czaplewska, Paulina Bogucka, Aleksandra Macur, Katarzyna Rybicka, Magda Rychłowski, Michał Fiołka, Marta J. |
author_facet | Czaplewska, Paulina Bogucka, Aleksandra Macur, Katarzyna Rybicka, Magda Rychłowski, Michał Fiołka, Marta J. |
author_sort | Czaplewska, Paulina |
collection | PubMed |
description | Earthworms’ celomic fluid has long attracted scientists’ interest due to their toxic properties. It has been shown that the elimination of coelomic fluid cytotoxicity to normal human cells was crucial for the generation of the non-toxic Venetin-1 protein-polysaccharide complex, which exhibits selective activity against Candida albicans cells as well as A549 non-small cell lung cancer cells. To find the molecular mechanisms behind the anti-cancer properties of the preparation, this research investigated the proteome response of A549 cells to the presence of Venetin-1. The sequential window acquisition of all theoretical mass spectra (SWATH-MS) methodology was used for the analysis, which allows for a relative quantitative analysis to be carried out without radiolabelling. The results showed that the formulation did not induce significant proteome responses in normal BEAS-2B cells. In the case of the tumour line, 31 proteins were up regulated, and 18 proteins down regulated. Proteins with increased expression in neoplastic cells are mainly associated with the mitochondrion, membrane transport and the endoplasmic reticulum. In the case of altered proteins, Venetin-1 interferes with proteins that stabilise the structures, i.e., keratin, glycolysis/gluconeogenesis and metabolic processes. |
format | Online Article Text |
id | pubmed-10292018 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-102920182023-06-27 Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid Czaplewska, Paulina Bogucka, Aleksandra Macur, Katarzyna Rybicka, Magda Rychłowski, Michał Fiołka, Marta J. Front Mol Biosci Molecular Biosciences Earthworms’ celomic fluid has long attracted scientists’ interest due to their toxic properties. It has been shown that the elimination of coelomic fluid cytotoxicity to normal human cells was crucial for the generation of the non-toxic Venetin-1 protein-polysaccharide complex, which exhibits selective activity against Candida albicans cells as well as A549 non-small cell lung cancer cells. To find the molecular mechanisms behind the anti-cancer properties of the preparation, this research investigated the proteome response of A549 cells to the presence of Venetin-1. The sequential window acquisition of all theoretical mass spectra (SWATH-MS) methodology was used for the analysis, which allows for a relative quantitative analysis to be carried out without radiolabelling. The results showed that the formulation did not induce significant proteome responses in normal BEAS-2B cells. In the case of the tumour line, 31 proteins were up regulated, and 18 proteins down regulated. Proteins with increased expression in neoplastic cells are mainly associated with the mitochondrion, membrane transport and the endoplasmic reticulum. In the case of altered proteins, Venetin-1 interferes with proteins that stabilise the structures, i.e., keratin, glycolysis/gluconeogenesis and metabolic processes. Frontiers Media S.A. 2023-06-08 /pmc/articles/PMC10292018/ /pubmed/37377864 http://dx.doi.org/10.3389/fmolb.2023.1128320 Text en Copyright © 2023 Czaplewska, Bogucka, Macur, Rybicka, Rychłowski and Fiołka. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Czaplewska, Paulina Bogucka, Aleksandra Macur, Katarzyna Rybicka, Magda Rychłowski, Michał Fiołka, Marta J. Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid |
title | Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid |
title_full | Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid |
title_fullStr | Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid |
title_full_unstemmed | Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid |
title_short | Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid |
title_sort | proteomic response of a549 lung cancer cell line to protein-polysaccharide complex venetin-1 isolated from earthworm coelomic fluid |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10292018/ https://www.ncbi.nlm.nih.gov/pubmed/37377864 http://dx.doi.org/10.3389/fmolb.2023.1128320 |
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