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Dr. Indu Choudhary
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0 Cancer
0 Cell Culture
0 Proteomics
0 Toxicology
0 jellyfish venom

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Short Biography

Indu Choudhary was born in India on 2nd May 1983. She did her undergraduate and Master’s degree from India. She started her research career with Proteomics at the International Center for Genetic Engineering, New Delhi, India. She earned her doctoral degree from Gyeongsang National University, South Korea. Her research work was focused on jellyfish venom. She unrevealed the putative targets of jellyfish venom during cardiotoxicity and dermal toxicity. Her work also supports the role of jellyfish venom as an anticancer agent. Despite this, she also discovered the novel toxin proteins in the jellyfishes. She worked as a postdoctoral fellow at the University of Missouri, Columbia (USA) where she studied the role of copper in cancer cells.

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Journal article
Published: 27 April 2021 in Toxins
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Jellyfish venom is well known for its local skin toxicities and various lethal accidents. The main symptoms of local jellyfish envenomation include skin lesions, burning, prickling, stinging pain, red, brown, or purplish tracks on the skin, itching, and swelling, leading to dermonecrosis and scar formation. However, the molecular mechanism behind the action of jellyfish venom on human skin cells is rarely understood. In the present study, we have treated the human HaCaT keratinocyte with Nemopilema nomurai jellyfish venom (NnV) to study detailed mechanisms of actions behind the skin symptoms after jellyfish envenomation. Using two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption-ionization time-of-flight mass spectrometry (MALDI-TOF/MS), cellular changes at proteome level were examined. The treatment of NnV resulted in the decrease of HaCaT cell viability in a concentration-dependent manner. Using NnV (at IC50), the proteome level alterations were determined at 12 h and 24 h after the venom treatment. Briefly, 70 protein spots with significant quantitative changes were picked from the gels for MALDI-TOF/MS. In total, 44 differentially abundant proteins were successfully identified, among which 19 proteins were increased, whereas 25 proteins were decreased in the abundance levels comparing with their respective control spots. DAPs involved in cell survival and development (e.g., Plasminogen, Vinculin, EMILIN-1, Basonuclin2, Focal adhesion kinase 1, FAM83B, Peroxisome proliferator-activated receptor-gamma co-activator 1-alpha) decreased their expression, whereas stress or immune response-related proteins (e.g., Toll-like receptor 4, Aminopeptidase N, MKL/Myocardin-like protein 1, hypoxia up-regulated protein 1, Heat shock protein 105 kDa, Ephrin type-A receptor 1, with some protease (or peptidase) enzymes) were up-regulated. In conclusion, the present findings may exhibit some possible key players during skin damage and suggest therapeutic strategies for preventing jellyfish envenomation.

ACS Style

Indu Choudhary; Duhyeon Hwang; Jinho Chae; Wonduk Yoon; Changkeun Kang; Euikyung Kim. Proteomic Changes during the Dermal Toxicity Induced by Nemopilema nomurai Jellyfish Venom in HaCaT Human Keratinocyte. Toxins 2021, 13, 311 .

AMA Style

Indu Choudhary, Duhyeon Hwang, Jinho Chae, Wonduk Yoon, Changkeun Kang, Euikyung Kim. Proteomic Changes during the Dermal Toxicity Induced by Nemopilema nomurai Jellyfish Venom in HaCaT Human Keratinocyte. Toxins. 2021; 13 (5):311.

Chicago/Turabian Style

Indu Choudhary; Duhyeon Hwang; Jinho Chae; Wonduk Yoon; Changkeun Kang; Euikyung Kim. 2021. "Proteomic Changes during the Dermal Toxicity Induced by Nemopilema nomurai Jellyfish Venom in HaCaT Human Keratinocyte." Toxins 13, no. 5: 311.

Journal article
Published: 08 March 2019 in Toxins
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Nowadays, proliferation of jellyfish has become a severe matter in many coastal areas around the world. Jellyfish Nemopilema nomurai is one of the most perilous organisms and leads to significant deleterious outcomes such as harm to the fishery, damage the coastal equipment, and moreover, its envenomation can be hazardous to the victims. Till now, the components of Nemopilema nomurai venom (NnV) are unknown owing to scant transcriptomics and genomic data. In the current research, we have explored a proteomic approach to identify NnV components and their interrelation with pathological effects caused by the jellyfish sting. Altogether, 150 proteins were identified, comprising toxins and other distinct proteins that are substantial in nematocyst genesis and nematocyte growth by employing two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI/TOF/MS). The identified toxins are phospholipase A2, phospholipase D Li Sic Tox beta IDI, a serine protease, putative Kunitz-type serine protease inhibitor, disintegrin and metalloproteinase, hemolysin, leukotoxin, three finger toxin MALT0044C, allergens, venom prothrombin activator trocarin D, tripeptide Gsp 9.1, and along with other toxin proteins. These toxins are relatively well characterized in the venoms of other poisonous species to induce pathogenesis, hemolysis, inflammation, proteolysis, blood coagulation, cytolysis, hemorrhagic activity, and type 1 hypersensitivity, suggesting that these toxins in NnV can also cause similar deleterious consequences. Our proteomic works indicate that NnV protein profile represents valuable source which leads to better understanding the clinical features of the jellyfish stings. As one of the largest jellyfish in the world, Nemopilema nomurai sting is considered to be harmful to humans due to its potent toxicity. The identification and functional characterization of its venom components have been poorly described and are beyond our knowledge. Here is the first report demonstrating the methodical overview of NnV proteomics research, providing significant information to understand the mechanism of NnV envenomation. Our proteomics findings can provide a platform for novel protein discovery and development of practical ways to deal with jellyfish stings on human beings.

ACS Style

Indu Choudhary; Du Hyeon Hwang; Hyunkyoung Lee; Won Duk Yoon; Jinho Chae; Chang Hoon Han; Seungshic Yum; Changkeun Kang; Euikyung Kim. Proteomic Analysis of Novel Components of Nemopilema nomurai Jellyfish Venom: Deciphering the Mode of Action. Toxins 2019, 11, 153 .

AMA Style

Indu Choudhary, Du Hyeon Hwang, Hyunkyoung Lee, Won Duk Yoon, Jinho Chae, Chang Hoon Han, Seungshic Yum, Changkeun Kang, Euikyung Kim. Proteomic Analysis of Novel Components of Nemopilema nomurai Jellyfish Venom: Deciphering the Mode of Action. Toxins. 2019; 11 (3):153.

Chicago/Turabian Style

Indu Choudhary; Du Hyeon Hwang; Hyunkyoung Lee; Won Duk Yoon; Jinho Chae; Chang Hoon Han; Seungshic Yum; Changkeun Kang; Euikyung Kim. 2019. "Proteomic Analysis of Novel Components of Nemopilema nomurai Jellyfish Venom: Deciphering the Mode of Action." Toxins 11, no. 3: 153.

Journal article
Published: 10 May 2018 in 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.

ACS Style

Indu Choudhary; Hyunkyoung Lee; Min Jung Pyo; Yunwi Heo; Jinho Chae; Seung Shic Yum; Changkeun Kang; Euikyung Kim. Proteomic Investigation to Identify Anticancer Targets of Nemopilema nomurai Jellyfish Venom in Human Hepatocarcinoma HepG2 Cells. Toxins 2018, 10, 194 .

AMA Style

Indu Choudhary, Hyunkyoung Lee, Min Jung Pyo, Yunwi Heo, Jinho Chae, Seung Shic Yum, Changkeun Kang, Euikyung Kim. Proteomic Investigation to Identify Anticancer Targets of Nemopilema nomurai Jellyfish Venom in Human Hepatocarcinoma HepG2 Cells. Toxins. 2018; 10 (5):194.

Chicago/Turabian Style

Indu Choudhary; Hyunkyoung Lee; Min Jung Pyo; Yunwi Heo; Jinho Chae; Seung Shic Yum; Changkeun Kang; Euikyung Kim. 2018. "Proteomic Investigation to Identify Anticancer Targets of Nemopilema nomurai Jellyfish Venom in Human Hepatocarcinoma HepG2 Cells." Toxins 10, no. 5: 194.

Journal article
Published: 19 July 2017 in Journal of Venomous Animals and Toxins including Tropical Diseases
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Because jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms. Although the effects of their toxins are a matter of concern, information on the venom components, biological activity and pathological mechanisms are still scarce. Therefore, the aim of the present study was to investigate a serine protease component of Nemopilema nomurai jellyfish venom (NnV) and unveil its characteristics. To determine the relationship between fibrinolytic activity of NnV and the serine protease, fibrin zymography was performed using metalloprotease and serine protease inhibitors. The biochemical characterization of serine proteases of NnV were determined by the amidolytic assay. Fractions with fibrinolytic activity were obtained by DEAE cation exchange column. NnV displayed fibrinolytic activities with molecular masses of approximately 70, 35, 30, and 28 kDa. The fibrinolytic activity of NnV was completely obliterated by phenylmethylsulfonyl fluoride, a prototype serine protease inhibitor. Based on amidolytic assays using chromogenic substrates specific for various kinds of serine proteases, NnV predominantly manifested a chymotrypsin-like feature. Its activity was completely eliminated at low pH (< 6) and high temperatures (> 37 °C). Some metal ions (Co2+, Cu2+, Zn2+ and Ni2+) strongly suppressed its fibrinolytic activity, while others (Ca2+ and Mg2+) failed to do so. Isolation of a serine protease with fibrionolytic activity from NnV revealed that only p3 showed the fibrinolytic activity, which was completely inhibited by PMSF. The present study showed that N. nomurai jellyfish venom has a chymotrypsin-like serine protease with fibrinolytic activity. Such information might be useful for developing clinical management of jellyfish envenomation and pharmacological agents with therapeutic potential for thrombotic diseases in the future.

ACS Style

Seong Kyeong Bae; Hyunkyoung Lee; Yunwi Heo; Min Jung Pyo; Indu Choudhary; Chang Hoon Han; Won Duk Yoon; Changkeun Kang; Euikyung Kim. In vitro characterization of jellyfish venom fibrin(ogen)olytic enzymes from Nemopilema nomurai. Journal of Venomous Animals and Toxins including Tropical Diseases 2017, 23, 1 -9.

AMA Style

Seong Kyeong Bae, Hyunkyoung Lee, Yunwi Heo, Min Jung Pyo, Indu Choudhary, Chang Hoon Han, Won Duk Yoon, Changkeun Kang, Euikyung Kim. In vitro characterization of jellyfish venom fibrin(ogen)olytic enzymes from Nemopilema nomurai. Journal of Venomous Animals and Toxins including Tropical Diseases. 2017; 23 (1):1-9.

Chicago/Turabian Style

Seong Kyeong Bae; Hyunkyoung Lee; Yunwi Heo; Min Jung Pyo; Indu Choudhary; Chang Hoon Han; Won Duk Yoon; Changkeun Kang; Euikyung Kim. 2017. "In vitro characterization of jellyfish venom fibrin(ogen)olytic enzymes from Nemopilema nomurai." Journal of Venomous Animals and Toxins including Tropical Diseases 23, no. 1: 1-9.

Journal article
Published: 05 July 2016 in Toxins
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An enzyme in a nematocyst extract of the Nemopilema nomurai jellyfish, caught off the coast of the Republic of Korea, catalyzed the cleavage of chymotrypsin substrate in an amidolytic kinetic assay, and this activity was inhibited by the serine protease inhibitor, phenylmethanesulfonyl fluoride. We isolated the full-length cDNA sequence of this enzyme, which contains 850 nucleotides, with an open reading frame of 801 encoding 266 amino acids. A blast analysis of the deduced amino acid sequence showed 41% identity with human chymotrypsin-like (CTRL) and the CTRL-1 precursor. Therefore, we designated this enzyme N. nomurai CTRL-1. The primary structure of N. nomurai CTRL-1 includes a leader peptide and a highly conserved catalytic triad of His69, Asp117, and Ser216. The disulfide bonds of chymotrypsin and the substrate-binding sites are highly conserved compared with the CTRLs of other species, including mammalian species. Nemopilema nomurai CTRL-1 is evolutionarily more closely related to Actinopterygii than to Scyphozoan (Aurelia aurita) or Hydrozoan (Hydra vulgaris). The N. nomurai CTRL1 was amplified from the genomic DNA with PCR using specific primers designed based on the full-length cDNA, and then sequenced. The N. nomurai CTRL1 gene contains 2434 nucleotides and four distinct exons. The 5′ donor splice (GT) and 3′ acceptor splice sequences (AG) are wholly conserved. This is the first report of the CTRL1 gene and cDNA structures in the jellyfish N. nomurai.

ACS Style

Yunwi Heo; Young Chul Kwon; Seong Kyeong Bae; Duhyeon Hwang; Hye Ryeon Yang; Indu Choudhary; Hyunkyoung Lee; Seungshic Yum; Kyoungsoon Shin; Won Duk Yoon; Changkeun Kang; Euikyung Kim. Cloning a Chymotrypsin-Like 1 (CTRL-1) Protease cDNA from the Jellyfish Nemopilema nomurai. Toxins 2016, 8, 205 .

AMA Style

Yunwi Heo, Young Chul Kwon, Seong Kyeong Bae, Duhyeon Hwang, Hye Ryeon Yang, Indu Choudhary, Hyunkyoung Lee, Seungshic Yum, Kyoungsoon Shin, Won Duk Yoon, Changkeun Kang, Euikyung Kim. Cloning a Chymotrypsin-Like 1 (CTRL-1) Protease cDNA from the Jellyfish Nemopilema nomurai. Toxins. 2016; 8 (7):205.

Chicago/Turabian Style

Yunwi Heo; Young Chul Kwon; Seong Kyeong Bae; Duhyeon Hwang; Hye Ryeon Yang; Indu Choudhary; Hyunkyoung Lee; Seungshic Yum; Kyoungsoon Shin; Won Duk Yoon; Changkeun Kang; Euikyung Kim. 2016. "Cloning a Chymotrypsin-Like 1 (CTRL-1) Protease cDNA from the Jellyfish Nemopilema nomurai." Toxins 8, no. 7: 205.