Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid

Paulina Czaplewska; Aleksandra Bogucka; Katarzyna Macur; Magda Rybicka; Michał Rychłowski; Marta J Fiołka

doi:10.3389/fmolb.2023.1128320

Proteomic response of A549 lung cancer cell line to protein-polysaccharide complex Venetin-1 isolated from earthworm coelomic fluid

Front Mol Biosci. 2023 Jun 8:10:1128320. doi: 10.3389/fmolb.2023.1128320. eCollection 2023.

Authors

Paulina Czaplewska¹, Aleksandra Bogucka^{1

2}, Katarzyna Macur¹, Magda Rybicka¹, Michał Rychłowski¹, Marta J Fiołka³

Affiliations

¹ Intercollegiate Faculty of Biotechnology, The University of Gdansk, Gdańsk, Poland.
² Institute of Biochemistry, Justus Liebig University of Giessen, Giessen, Germany.
³ Department of Immunobiology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland.

Abstract

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.

Keywords: coelomic fluid; earthworms; protein-polysaccharide complex; proteomics; swath.