Next Article in Journal
Purification and Characterization of Recombinant Botulinum Neurotoxin Serotype FA, Also Known as Serotype H
Previous Article in Journal
A Genomic and Proteomic Approach to Identify and Quantify the Expressed Bacillus thuringiensis Proteins in the Supernatant and Parasporal Crystal
Article Menu
Issue 5 (May) cover image

Export Article

Open AccessArticle
Toxins 2018, 10(5), 194; https://doi.org/10.3390/toxins10050194

Proteomic Investigation to Identify Anticancer Targets of Nemopilema nomurai Jellyfish Venom in Human Hepatocarcinoma HepG2 Cells

1
College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea
2
Marine Environmental Research and Information Laboratory, Gunpo 15850, Korea
3
South Sea Environmental Research Center, Korea Institute of Ocean Science and Technology (KIOST), Geoje 53201, Korea
4
Faculty of Marine Environmental Science, University of Science and technology (UST), Geoje 53201, Korea
5
Institutes of Agriculture and Life Science, Gyeongsang National University, Jinju 52828, Korea
6
Institute of Animal Medicine, Gyeongsang National University, Jinju 52828, Korea
*
Author to whom correspondence should be addressed.
Received: 4 March 2018 / Revised: 24 April 2018 / Accepted: 27 April 2018 / Published: 10 May 2018
(This article belongs to the Special Issue Evolution and Molecular Biology of Marine Biotoxins)
Full-Text   |   PDF [4408 KB, uploaded 11 May 2018]   |  

Abstract

Nemopilema nomurai is a giant jellyfish that blooms in East Asian seas. Recently, N. nomurai venom (NnV) was characterized from a toxicological and pharmacological point of view. A mild dose of NnV inhibits the growth of various kinds of cancer cells, mainly hepatic cancer cells. The present study aims to identify the potential therapeutic targets and mechanism of NnV in the growth inhibition of cancer cells. Human hepatocellular carcinoma (HepG2) cells were treated with NnV, and its proteome was analyzed using two-dimensional gel electrophoresis, followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI/TOF/MS). The quantity of twenty four proteins in NnV-treated HepG2 cells varied compared to non-treated control cells. Among them, the amounts of fourteen proteins decreased and ten proteins showed elevated levels. We also found that the amounts of several cancer biomarkers and oncoproteins, which usually increase in various types of cancer cells, decreased after NnV treatment. The representative proteins included proliferating cell nuclear antigen (PCNA), glucose-regulated protein 78 (GRP78), glucose-6-phosphate dehydrogenase (G6PD), elongation factor 1γ (EF1γ), nucleolar and spindle-associated protein (NuSAP), and activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1). Western blotting also confirmed altered levels of PCNA, GRP78, and G6PD in NnV-treated HepG2 cells. In summary, the proteomic approach explains the mode of action of NnV as an anticancer agent. Further characterization of NnV may help to unveil novel therapeutic agents in cancer treatment. View Full-Text
Keywords: jellyfish; Nemopilema nomurai; HepG2 cell; venom; proteomics; MALDI/TOF/MS; 2-DE jellyfish; Nemopilema nomurai; HepG2 cell; venom; proteomics; MALDI/TOF/MS; 2-DE
Figures

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

SciFeed

Share & Cite This Article

MDPI and ACS Style

Choudhary, I.; Lee, H.; Pyo, M.J.; Heo, Y.; Chae, J.; Yum, S.S.; Kang, C.; Kim, E. Proteomic Investigation to Identify Anticancer Targets of Nemopilema nomurai Jellyfish Venom in Human Hepatocarcinoma HepG2 Cells. Toxins 2018, 10, 194.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top