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Ji-Young Kim	2 Articles
Involvement of MAPK activation in chemokine or COX-2 productions by Toxoplasma gondii Ji-Young Kim, Myoung-Hee Ahn, Hyun-Ouk Song, Jong-Hak Choi, Jae-Sook Ryu, Duk-Young Min, Myung-Hwan Cho Korean J Parasitol 2006;44(3):197-207. Published online September 20, 2006 DOI: https://doi.org/10.3347/kjp.2006.44.3.197 Abstract PDF This experiment focused on MAPK activation in host cell invasion and replication of T. gondii, as well as the expression of CC chemokines, MCP-1 and MIP-1α, and enzyme, COX-2/prostaglandin E₂ (PGE₂) in infected cells via western blot, [³H]-uracil incorporation assay, ELISA and RT-PCR. The phosphorylation of ERK1/2 and p38 in infected HeLa cells was detected at 1 hr and/or 6 hr postinfection (PI). Tachyzoite proliferation was reduced by p38 or JNK MAPK inhibitors. MCP-1 secretion was enhanced in infected peritoneal macrophages at 6 hr PI. MIP-1α mRNA was increased in macrophages at 18 hr PI. MCP-1 and MIP-1α were reduced after treatment with inhibitors of ERK1/2 and JNK MAPKs. COX-2 mRNA gradually increased in infected RAW 264.7 cells and the secretion of COX-2 peaked at 6 hr PI. The inhibitor of JNK suppressed COX-2 expression. PGE₂ from infected RAW 264.7 cells was increased and synthesis was suppressed by PD98059, SB203580, and SP600125. In this study, the activation of p38, JNK and/or ERK1/2 MAPKs occurred during the invasion and proliferation of T. gondii tachyzoites in HeLa cells. Also, increased secretion and expression of MCP-1, MIP-1α, COX-2 and PGE₂ were detected in infected macrophages, and appeared to occur via MAPK signaling pathways. Citations Citations to this article as recorded by Differential Expression of hsa‐miR‐144‐3p and hsa‐miR‐125b‐5p in Gestational Toxoplasmosis Ingrid de Siqueira Pereira, Mariana Ramire Cortez, Tamires Santos de Arruda, Francieli Marinho Carneiro, Allecineia Bispo da Cruz, Ricardo Gava, Geraldo Magela de Faria Junior, Ingrid Gomes de Campos Truzzi, Lígia Cosentino Junqueira Franco Spegiorin, San Parasite Immunology.2025;[Epub] CrossRef Qualitative analysis of Fasciola gigantica excretory and secretory products coimmunoprecipitated with buffalo secondary infection sera shows dissimilar components from primary infection sera Mengwei Zheng, Xinping Kong, Xuelian Jiang, Yankun Yang, Shishi Fu, Chongli Wen, Weiyu Zhang, Wenda Di Acta Tropica.2024; 260: 107391. CrossRef The roles of COX-2 in protozoan infection Xinlei Wang, Jie Chen, Jingtong Zheng Frontiers in Immunology.2023;[Epub] CrossRef Immunomodulatory effects ofInonotus obliquuspolysaccharide on splenic lymphocytes infected withToxoplasma gondiivia NF-κB and MAPKs pathways Rui Sang, Fuliang Sun, Hongyuan Zhou, Meng Wang, Haitao Li, Chunting Li, Xinhui Sun, Xin Zhao, Xuemei Zhang Immunopharmacology and Immunotoxicology.2022; 44(1): 129. CrossRef Inhibitory Effects of Inonotus obliquus Polysaccharide on Inflammatory Response in Toxoplasma gondii-Infected RAW264.7 Macrophages Kexin Yan, Hongyuan Zhou, Meng Wang, Haitao Li, Rui Sang, Bingjie Ge, Xin Zhao, Chunting Li, Wei Wang, Xuemei Zhang, Angelica Oliveira Gomes Evidence-Based Complementary and Alternative Medicine.2021; 2021: 1. CrossRef Regulation of Proinflammatory Enzymes by Peroxisome Proliferator–Activated Receptor Gamma in Astroglia Infected with Toxoplasma gondii Ling-Yuh Shyu, Ke-Min Chen, Cheng-You Lu, Shih-Chan Lai Journal of Parasitology.2020; 106(5): 564. CrossRef Increased Toxoplasma gondii Intracellular Proliferation in Human Extravillous Trophoblast Cells (HTR8/SVneo Line) Is Sequentially Triggered by MIF, ERK1/2, and COX-2 Iliana Claudia Balga Milian, Rafaela José Silva, Camilla Manzan-Martins, Bellisa Freitas Barbosa, Pamela Mendonça Guirelli, Mayara Ribeiro, Angelica de Oliveira Gomes, Francesca Ietta, José Roberto Mineo, Priscila Silva Franco, Eloisa Amália Vieira Ferro Frontiers in Microbiology.2019;[Epub] CrossRef Cyclooxygenase (COX)-2 Inhibitors Reduce Toxoplasma gondii Infection and Upregulate the Pro-inflammatory Immune Response in Calomys callosus Rodents and Human Monocyte Cell Line Ana Carolina Alcântara Pereira, Rafaela José Silva, Priscila Silva Franco, Angelica de Oliveira Gomes, Guilherme Souza, Iliana Claudia Balga Milian, Mayara Ribeiro, Alessandra Monteiro Rosini, Pâmela Mendonça Guirelli, Eliézer Lucas Pires Ramos, Tiago Wil Frontiers in Microbiology.2019;[Epub] CrossRef A Human Proteome Array Approach to Identifying Key Host Proteins Targeted by Toxoplasma Kinase ROP18 Zhaoshou Yang, Yongheng Hou, Taofang Hao, Hee-Sool Rho, Jun Wan, Yizhao Luan, Xin Gao, Jianping Yao, Aihua Pan, Zhi Xie, Jiang Qian, Wanqin Liao, Heng Zhu, Xingwang Zhou Molecular & Cellular Proteomics.2017; 16(3): 469. CrossRef Toxoplasma gondii GRA7-Induced TRAF6 Activation Contributes to Host Protective Immunity Chul-Su Yang, Jae-Min Yuk, Young-Ha Lee, Eun-Kyeong Jo, J. H. Adams Infection and Immunity.2016; 84(1): 339. CrossRef Transcriptional Regulation of CXCL5 in HIV-1-Infected Macrophages and Its Functional Consequences on CNS Pathology Debjani Guha, Cynthia R. Klamar, Todd Reinhart, Velpandi Ayyavoo Journal of Interferon & Cytokine Research.2015; 35(5): 373. CrossRef Susceptibility to Toxoplasma gondii proliferation in BeWo human trophoblast cells is dose-dependent of macrophage migration inhibitory factor (MIF), via ERK1/2 phosphorylation and prostaglandin E2 production B.F. Barbosa, L. Paulesu, F. Ietta, N. Bechi, R. Romagnoli, A.O. Gomes, S. Favoreto-Junior, D.A.O. Silva, J.R. Mineo, T.W.P. Mineo, E.A.V. Ferro Placenta.2014; 35(3): 152. CrossRef Differential Regulation of Proinflammatory Cytokine Expression by Mitogen-Activated Protein Kinases in Macrophages in Response to Intestinal Parasite Infection Mei Xing Lim, Chin Wen Png, Crispina Yan Bing Tay, Joshua Ding Wei Teo, Huipeng Jiao, Norbert Lehming, Kevin Shyong Wei Tan, Yongliang Zhang, J. A. Appleton Infection and Immunity.2014; 82(11): 4789. CrossRef Induction of matrix metalloproteinase-2 and -9 via Erk1/2-NF-κB pathway in human astroglia infected with Toxoplasma gondii Cheng-You Lu, Shih-Chan Lai Acta Tropica.2013; 127(1): 14. CrossRef AP-1 pathway-targeted inhibition of inflammatory responses in LPS-treated macrophages and EtOH/HCl-treated stomach by Archidendron clypearia methanol extract Woo Seok Yang, Deok Jeong, Gyeongsug Nam, Young-Su Yi, Deok Hyo Yoon, Tae Woong Kim, Yung Chul Park, Hyunsik Hwang, Man Hee Rhee, Sungyoul Hong, Jae Youl Cho Journal of Ethnopharmacology.2013; 146(2): 637. CrossRef Roles of Apicomplexan protein kinases at each life cycle stage Kentaro Kato, Tatsuki Sugi, Tatsuya Iwanaga Parasitology International.2012; 61(2): 224. CrossRef Serum Response Factor Regulates Immediate Early Host Gene Expression in Toxoplasma gondii-Infected Host Cells Mandi Wiley, Crystal Teygong, Eric Phelps, Jay Radke, Ira J. Blader, Thomas Templeton PLoS ONE.2011; 6(3): e18335. CrossRef Monocyte-Mediated Defense Against Microbial Pathogens Natalya V. Serbina, Ting Jia, Tobias M. Hohl, Eric G. Pamer Annual Review of Immunology.2008; 26(1): 421. CrossRef Toxoplasma gondiiRhoptry Discharge Correlates with Activation of the Early Growth Response 2 Host Cell Transcription Factor Eric D. Phelps, Kristin R. Sweeney, Ira J. Blader Infection and Immunity.2008; 76(10): 4703. CrossRef Several transcription factors regulate COX-2 gene expression in pancreatic β-cells Xiongfei Zhang, Jingjing Zhang, Xiaomin Yang, Xiao Han Molecular Biology Reports.2007; 34(3): 199. CrossRef 10,340 View 90 Download Crossref Partial characterization of a 29 kDa cysteine protease purified from Taenia solium metacestodes Ji-Young Kim, Hyun-Jong Yang, Kwang-Sig Kim, Young-Bae Chung Korean J Parasitol 2005;43(4):157-160. Published online December 20, 2005 DOI: https://doi.org/10.3347/kjp.2005.43.4.157 Abstract PDF A 29 kDa cysteine protease of Taenia solium metacestodes was purified by Mono Q anion-exchanger and Superose 6 HR gel filtration chromatography. The enzyme was effectively inhibited by cysteine protease inhibitors, such as iodoacetic acid (IAA) and trans-epoxy-succinyl-L-leucyl-amido (4-guanidino) butane (E-64) while inhibitors acting on serine- or metallo-proteases did not affect the enzyme activity. The purified enzyme degraded human immunoglobulin G (IgG), collagen and bovine serum albumin (BSA), but human IgG was more susceptible for proteolysis by the enzyme. To define the precise biological roles of the enzyme, more detailed biochemical and functional studies would be required. Citations Citations to this article as recorded by Molecular characterization of EcCLP1, a new putative cathepsin L protease from Echinococcus canadensis Ariel Naidich, Ariana M. Gutierrez, Federico Camicia Parasite.2024; 31: 39. CrossRef Cloning and characterization of a cathepsin L-like cysteine protease from Taenia pisiformis Qiuxia Wang, Shaohua Zhang, Xuenong Luo, Junling Hou, Xueliang Zhu, Xuepeng Cai Veterinary Parasitology.2013; 194(1): 26. CrossRef Partial Purification and Characterization of a Cysteine Protease Inhibitor from the Plerocercoid of Spirometra erinacei Young-Bae Chung, Hyun-Jong Yang The Korean Journal of Parasitology.2008; 46(3): 183. CrossRef Cloning and characterization of cathepsin L-like peptidases of Echinococcus multilocularis metacestodes Yasuhito Sako, Hiroshi Yamasaki, Kazuhiro Nakaya, Minoru Nakao, Akira Ito Molecular and Biochemical Parasitology.2007; 154(2): 181. CrossRef Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode Ai Hua Li, Sung-Ung Moon, Yun-Kyu Park, Byoung-Kuk Na, Myung-Gi Hwang, Chang-Mi Oh, Shin-Hyeong Cho, Yoon Kong, Tong-Soo Kim, Pyung-Rim Chung Veterinary Parasitology.2006; 141(3-4): 251. CrossRef 8,311 View 90 Download Crossref