Proteomics approach to examine the cardiotoxic effects of Nemopilema nomurai Jellyfish venom

Choudhary, Indu; Lee, Hyunkyoung; Pyo, Min-Jung; Heo, Yunwi; Bae, Seong Kyeong; Kwon, Young Chul; Yoon, Won Duk; Kang, Changkeun; Kim, Euikyung

doi:10.1016/j.jprot.2015.07.008

Cited by 18 publications

(16 citation statements)

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“…Our ecosystem has different kinds of venomous animals, including terrestrial, such as snake, scorpion, spider, centipede, etc., and aquatic organisms, such as sea anemone, fire coral, and jellyfish [ 1 , 2 ]. Venomous jellyfish species are found in both cubozoans, such as Chironex fleckeri , and scyphozoans ( Cyanea capillata , Pelagia noctiluca , and Nemopilema nomurai ) [ 3 , 4 , 5 , 6 ]. We have focused on Nemopilema nomurai in this study; it is one of the largest jellyfish species and can grow up to 2 m in bell diameter and 200 kg in weight [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

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

Choudhary

Lee

Pyo

et al. 2018

Toxins

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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.

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Section: Introductionmentioning

confidence: 99%

“…Envenomation by N. nomurai can result in a dermatological reaction with an intense burning sensation and erythematous eruption [ 9 ]. N. nomurai envenomation can also be accompanied by other types of toxicological symptoms, such as cardiotoxicity, hemolytic activity, and cytotoxic effects [ 6 , 10 ].…”

Section: Introductionmentioning

confidence: 99%

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

Choudhary

Lee

Pyo

et al. 2018

Toxins

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“…Data sets comprise of list of 34 proteins which were successfully identified by MALDI-TOF/MS after NnV treatment of H9c2 cell and 2-DE. Among these, 10 proteins were down-regulated and 24 proteins were up-regulated [1] . Differentially expressed (relative spot intensity) proteins and their fold-change along with the up- and down-regulated p -values are summarized in Supplementary Table 1 and Supplementary Table 2 , respectively.…”

Section: Data Experimental Design Materials and Methodsmentioning

confidence: 99%

“… This data article restrains data associated to the Choudhary et al [1] . Nemopilema nomurai Jellyfish venom (NnV) can lead to cardiac toxicity.…”

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Nemopilema nomurai Jellyfish venom treatment leads to alterations in rat cardiomyocytes proteome

et al. 2015

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This data article restrains data associated to the Choudhary et al. [1]. Nemopilema nomurai Jellyfish venom (NnV) can lead to cardiac toxicity. Here we analyzed the effect of NnV on rat cardiomyocytes cell line H9c2 at the proteome level using two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS). This analysis resulted in 34 proteins with differential expression. Here we provide the dataset for the proteins with amplified or reduced level as compare to control.

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“…Jellyfish nematocyst venom, composed of highly complex and toxic mixtures of proteins and peptides, is the underlying basis of severe envenomations. To date, some biological activities of these proteinaceous mixtures have been observed, including hemolytic [ 8 , 9 ], insecticidal [ 10 , 11 ], cardiotoxic [ 12 , 13 ] and cytotoxic [ 14 , 15 ] activity.…”

Section: Introductionmentioning

confidence: 99%

Functional Elucidation of Nemopilema nomurai and Cyanea nozakii Nematocyst Venoms’ Lytic Activity Using Mass Spectrometry and Zymography

Yue

et al. 2017

Toxins

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Background: Medusozoans utilize explosively discharging penetrant nematocysts to inject venom into prey. These venoms are composed of highly complex proteins and peptides with extensive bioactivities, as observed in vitro. Diverse enzymatic toxins have been putatively identified in the venom of jellyfish, Nemopilema nomurai and Cyanea nozakii, through examination of their proteomes and transcriptomes. However, functional examination of putative enzymatic components identified in proteomic approaches to elucidate potential bioactivities is critically needed. Methods: In this study, enzymatic toxins were functionally identified using a combined approach consisting of in gel zymography and liquid chromatography tandem mass spectrometry (LC-MS/MS). The potential roles of metalloproteinases and lipases in hemolytic activity were explored using specific inhibitors. Results: Zymography indicated that nematocyst venom possessed protease-, lipase- and hyaluronidase-class activities. Further, proteomic approaches using LC-MS/MS indicated sequence homology of proteolytic bands observed in zymography to extant zinc metalloproteinase-disintegrins and astacin metalloproteinases. Moreover, pre-incubation of the metalloproteinase inhibitor batimastat with N. nomurai nematocyst venom resulted in an approximate 62% reduction of hemolysis compared to venom exposed sheep erythrocytes, suggesting that metalloproteinases contribute to hemolytic activity. Additionally, species within the molecular mass range of 14–18 kDa exhibited both egg yolk and erythrocyte lytic activities in gel overlay assays. Conclusion: For the first time, our findings demonstrate the contribution of jellyfish venom metalloproteinase and suggest the involvement of lipase species to hemolytic activity. Investigations of this relationship will facilitate a better understanding of the constituents and toxicity of jellyfish venom.

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Proteomics approach to examine the cardiotoxic effects of Nemopilema nomurai Jellyfish venom

Cited by 18 publications

References 74 publications

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

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

Nemopilema nomurai Jellyfish venom treatment leads to alterations in rat cardiomyocytes proteome

Functional Elucidation of Nemopilema nomurai and Cyanea nozakii Nematocyst Venoms’ Lytic Activity Using Mass Spectrometry and Zymography

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