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Takuya Yoshino Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Tomohisa Nagoshi Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Ryuko Anzawa Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Yusuke Kashiwagi Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Keiichi Ito Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Daisuke Katoh Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Masami Fujisaki Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Yosuke Kayama Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Taro Date Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Kenichi Hongo Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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Michihiro Yoshimura Division of Cardiology, Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan

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. 2010 , Turrell et al . 2011 ). Among the three major MAPK signaling pathways, we found that p38MAPK activation is dramatically altered by aldosterone preconditioning during IRI ( Fig. 5 ). Phosphorylation of p38 was significantly increased by

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-14-0067
Volume/Issue:
Volume 222: Issue 2
Free access
Joseph Aizen Marine Science Institute, The University of Texas at Austin, 750 Channel View Drive, Port Aransas, Texas 78373, USA

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Peter Thomas Marine Science Institute, The University of Texas at Austin, 750 Channel View Drive, Port Aransas, Texas 78373, USA

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zebrafish has previously been shown to involve Egfr and Mapk3/1 signaling ( Peyton & Thomas 2011 ). Treatment with E 2 and G-1 for 15–20 min caused increases in Mapk1/3 phosphorylation in denuded zebrafish oocytes, confirming these previous findings ( Fig

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-14-0576
Volume/Issue:
Volume 225: Issue 1
Free access
K Alexander H Iwen Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

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Oezge Senyaman Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

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Arne Schwartz Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

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Maren Drenckhan Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

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Britta Meier Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

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Dirk Hadaschik Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

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Johannes Klein Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

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chemiluminescence kit (Roche Molecular Biochemicals). UCP-1 antibody, β-actin antibody and specific MC receptor antibodies were purchased from Chemicon (Temecula, CA, USA). Phospho-specific and total p38 MAPK antibodies were obtained from Cell Signaling (Beverly, MA

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-07-0299
Volume/Issue:
Volume 196: Issue 3
Free access
Juthamard Surapongchai Exercise Physiology Laboratory, Department of Physiology, Faculty of Science, Mahidol University, Bangkok, Thailand

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Mujalin Prasannarong Department of Physical Therapy, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai, Thailand

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Tepmanas Bupha-Intr Exercise Physiology Laboratory, Department of Physiology, Faculty of Science, Mahidol University, Bangkok, Thailand

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Vitoon Saengsirisuwan Exercise Physiology Laboratory, Department of Physiology, Faculty of Science, Mahidol University, Bangkok, Thailand

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levels of these MAPKs ( Fig. 6C ). Figure 6 Effects of ANGII treatment on ROS generation and the MAPK pathway. 4-HNE, the marker of oxidative stress, induced by ANGII infusion (A). Expression of the signaling proteins SAPK/JNK, phosphorylated SAPK

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-16-0579
Volume/Issue:
Volume 232: Issue 3
Free access
Nami Kim Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea
Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Jung Ok Lee Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Hye Jeong Lee Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Yong Woo Lee Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Hyung Ip Kim Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Su Jin Kim Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Sun Hwa Park Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Chul Su Lee Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Sun Woo Ryoo Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Geum-Sook Hwang Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea
Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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Hyeon Soo Kim Department of Anatomy, Department of Medicine, Integrated Metabolomics Research Group, Department of Life Science, Korea University College of Medicine, Seoul 136-701, South Korea

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uptake ( Niu et al . 2003 , Cheng et al . 2006 ). To understand the signaling pathways involved in isoeugenol-induced glucose uptake, we investigated the effects of isoeugenol on p38MAPK. Isoeugenol (10 μM) increased p38MAPK phosphorylation in a time

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-15-0302
Volume/Issue:
Volume 228: Issue 2
Open access
Whasun Lim Department of Biotechnology, Department of Animal Resources Science, College of Life Sciences and Biotechnology, Korea University, Seoul 136‐713, Republic of Korea

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Wooyoung Jeong Department of Biotechnology, Department of Animal Resources Science, College of Life Sciences and Biotechnology, Korea University, Seoul 136‐713, Republic of Korea

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Gwonhwa Song Department of Biotechnology, Department of Animal Resources Science, College of Life Sciences and Biotechnology, Korea University, Seoul 136‐713, Republic of Korea

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. 2007 ). For example genistein, one of the phytoestrogens, affects transcriptional activity of ESR1 and ESR2 by modulating their binding affinity to estrogen-response elements (ERE) and inhibiting activity of both the PI3K/AKT and MAPK cell signaling

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-15-0418
Volume/Issue:
Volume 228: Issue 3
Free access
Rong Wan Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular Intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, People's Republic of China

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Chao Zhu Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular Intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, People's Republic of China

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Rui Guo Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular Intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, People's Republic of China

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Lai Jin Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular Intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, People's Republic of China

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Yunxin Liu Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular Intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, People's Republic of China

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Li Li Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular Intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, People's Republic of China

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Hao Zhang Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular Intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, People's Republic of China

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Shengnan Li Jiangsu Provincial Key Lab of Cardiovascular Diseases and Molecular Intervention, Department of Pharmacology, Nanjing Medical University, Nanjing 210029, People's Republic of China

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(TLR4), NF-κB p65, and p-NF-κB p65 were provided by Cell Signaling Technologies (Danvers, MA, USA). UCN1 antibody and HRP-conjugated rabbit anti-chicken IgG were obtained from Abcam (Cambridge, UK). Antibodies to p38MAPK, p-p38MAPK, ERK1/2, p-ERK1

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-13-0138
Volume/Issue:
Volume 218: Issue 3
Free access
Kumiko Taguchi Department of Physiology and Morphology, Institute of Medicinal Chemistry, Hoshi University, Shinagawa-ku, Tokyo, Japan

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Haruka Narimatsu Department of Physiology and Morphology, Institute of Medicinal Chemistry, Hoshi University, Shinagawa-ku, Tokyo, Japan

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Takayuki Matsumoto Department of Physiology and Morphology, Institute of Medicinal Chemistry, Hoshi University, Shinagawa-ku, Tokyo, Japan

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Tsuneo Kobayashi Department of Physiology and Morphology, Institute of Medicinal Chemistry, Hoshi University, Shinagawa-ku, Tokyo, Japan

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Signaling Technology), p38 mitogen-activated protein kinase (MAPK; Cell Signaling Technology), Jun amino-terminal kinase (JNK; Cell Signaling Technology) and caveolin-1 (Cell Signaling Technology) antibody (1:1000) and detected using a horseradish peroxidase

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-18-0616
Volume/Issue:
Volume 241: Issue 3
Free access
Elizabeth Gray Beta Cell Development and Function Group, Division of Reproduction and Endocrinology, School of Biomedical and Health Sciences, King’s College London, Hodgkin Building HB2.10N, Guy’s Campus, London SE1 9UL, UK
Department of Biological Sciences, Molecular Physiology, Biomedical Research Institute, University of Warwick, Warwick, UK
Division of Gene and Cell Based Therapy, King’s College London, London, UK

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Dany Muller Beta Cell Development and Function Group, Division of Reproduction and Endocrinology, School of Biomedical and Health Sciences, King’s College London, Hodgkin Building HB2.10N, Guy’s Campus, London SE1 9UL, UK
Department of Biological Sciences, Molecular Physiology, Biomedical Research Institute, University of Warwick, Warwick, UK
Division of Gene and Cell Based Therapy, King’s College London, London, UK

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Paul E Squires Beta Cell Development and Function Group, Division of Reproduction and Endocrinology, School of Biomedical and Health Sciences, King’s College London, Hodgkin Building HB2.10N, Guy’s Campus, London SE1 9UL, UK
Department of Biological Sciences, Molecular Physiology, Biomedical Research Institute, University of Warwick, Warwick, UK
Division of Gene and Cell Based Therapy, King’s College London, London, UK

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Henry Asare-Anane Beta Cell Development and Function Group, Division of Reproduction and Endocrinology, School of Biomedical and Health Sciences, King’s College London, Hodgkin Building HB2.10N, Guy’s Campus, London SE1 9UL, UK
Department of Biological Sciences, Molecular Physiology, Biomedical Research Institute, University of Warwick, Warwick, UK
Division of Gene and Cell Based Therapy, King’s College London, London, UK

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Guo-Cai Huang Beta Cell Development and Function Group, Division of Reproduction and Endocrinology, School of Biomedical and Health Sciences, King’s College London, Hodgkin Building HB2.10N, Guy’s Campus, London SE1 9UL, UK
Department of Biological Sciences, Molecular Physiology, Biomedical Research Institute, University of Warwick, Warwick, UK
Division of Gene and Cell Based Therapy, King’s College London, London, UK

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Stephanie Amiel Beta Cell Development and Function Group, Division of Reproduction and Endocrinology, School of Biomedical and Health Sciences, King’s College London, Hodgkin Building HB2.10N, Guy’s Campus, London SE1 9UL, UK
Department of Biological Sciences, Molecular Physiology, Biomedical Research Institute, University of Warwick, Warwick, UK
Division of Gene and Cell Based Therapy, King’s College London, London, UK

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Shanta J Persaud Beta Cell Development and Function Group, Division of Reproduction and Endocrinology, School of Biomedical and Health Sciences, King’s College London, Hodgkin Building HB2.10N, Guy’s Campus, London SE1 9UL, UK
Department of Biological Sciences, Molecular Physiology, Biomedical Research Institute, University of Warwick, Warwick, UK
Division of Gene and Cell Based Therapy, King’s College London, London, UK

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Peter M Jones Beta Cell Development and Function Group, Division of Reproduction and Endocrinology, School of Biomedical and Health Sciences, King’s College London, Hodgkin Building HB2.10N, Guy’s Campus, London SE1 9UL, UK
Department of Biological Sciences, Molecular Physiology, Biomedical Research Institute, University of Warwick, Warwick, UK
Division of Gene and Cell Based Therapy, King’s College London, London, UK

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′,6-Diamidino-2-phe-nylindole (DAPI) was from Molecular Probes (Eugene, OR, USA). The calcimimetic R-568 was a gift from Amgen Incorporation (Thousand Oaks, CA, USA). The monoclonal antibody against p42/44 mitogen-activated protein kinases (MAPK, 1:5000 final

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06891
Volume/Issue:
Volume 190: Issue 3
Free access
Mahsa Hamzeh Department of Pharmacology and Therapeutics, Department of Obstetrics and Gynecology, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir-William-Osler, Room 104, Montréal, Québec, Canada H3G 1Y6

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Bernard Robaire Department of Pharmacology and Therapeutics, Department of Obstetrics and Gynecology, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir-William-Osler, Room 104, Montréal, Québec, Canada H3G 1Y6
Department of Pharmacology and Therapeutics, Department of Obstetrics and Gynecology, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir-William-Osler, Room 104, Montréal, Québec, Canada H3G 1Y6

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, Falkenstein et al . 2000 ). The extracellular signal-regulated protein kinases (ERK1/2), members of the MAPK superfamily, are activated in response to androgens. These protein kinases play a key role in cell growth, differentiation, and function at both the

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-10-0223
Volume/Issue:
Volume 209: Issue 1
Free access