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Rhone A Mendoza Department of Biomedical Sciences, Center of Excellence in Cancer Research, Texas Tech University Health Sciences Center, Paul L Foster School of Medicine, 5001 El Paso Drive, El Paso, Texas 79905, USA

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Marlene I Enriquez Department of Biomedical Sciences, Center of Excellence in Cancer Research, Texas Tech University Health Sciences Center, Paul L Foster School of Medicine, 5001 El Paso Drive, El Paso, Texas 79905, USA

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Sylvia M Mejia Department of Biomedical Sciences, Center of Excellence in Cancer Research, Texas Tech University Health Sciences Center, Paul L Foster School of Medicine, 5001 El Paso Drive, El Paso, Texas 79905, USA

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Emily E Moody Department of Biomedical Sciences, Center of Excellence in Cancer Research, Texas Tech University Health Sciences Center, Paul L Foster School of Medicine, 5001 El Paso Drive, El Paso, Texas 79905, USA

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Gudmundur Thordarson Department of Biomedical Sciences, Center of Excellence in Cancer Research, Texas Tech University Health Sciences Center, Paul L Foster School of Medicine, 5001 El Paso Drive, El Paso, Texas 79905, USA

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activation of the signaling pathways that induce apoptosis, where the elevation in ERβ expression and p38 MAPK phosphorylation play key roles. However, it should be pointed out that the data presented in this study are correlative and it still has to be

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-10-0235
Volume/Issue:
Volume 208: Issue 1
Free access
Mélissa Otis Service of Endocrinology,
Department of Physiology and Biophysics, Faculty of Medicine and Health sciences, University of Sherbrooke, Sherbrooke, 3001, 12th Avenue North, Quebec, Canada J1H 5N4

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Shirley Campbell Service of Endocrinology,
Department of Physiology and Biophysics, Faculty of Medicine and Health sciences, University of Sherbrooke, Sherbrooke, 3001, 12th Avenue North, Quebec, Canada J1H 5N4

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Marcel D Payet Service of Endocrinology,
Department of Physiology and Biophysics, Faculty of Medicine and Health sciences, University of Sherbrooke, Sherbrooke, 3001, 12th Avenue North, Quebec, Canada J1H 5N4

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Nicole Gallo-Payet Service of Endocrinology,
Department of Physiology and Biophysics, Faculty of Medicine and Health sciences, University of Sherbrooke, Sherbrooke, 3001, 12th Avenue North, Quebec, Canada J1H 5N4

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activation of protein kinase A ( Penhoat et al. 2001 , Gallo-Payet & Payet 2003 ). In addition, in the Y1 adrenocortical cell line, ACTH may also activate the mitogenic-activated protein kinase pathway, p42/p44 (p42/p44 mapk ; Watanabe et al. 1997

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-07-0055
Volume/Issue:
Volume 193: Issue 3
Free access
Christopher A Price Faculty of Veterinary Medicine, Centre de recherche en reproduction animale, University of Montreal, 3200 rue Sicotte, St‐Hyacinthe, Quebec, Canada J2S 7C6

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whether FGF18 alters p53 signaling. Most intriguingly, FGF18 does not result in the typical phosphorylation of MAPK3/1, but does phosphorylate MAPK14 (also known as p38); increased activity of MAPK14 has been linked to apoptosis in ovarian cells ( Uma et

Article Type:
Review Article
DOI:
https://doi.org/10.1530/JOE-15-0414
Volume/Issue:
Volume 228: Issue 2
Free access
Maria Petropavlovskaia Departments of Surgery,
Clinical Epidemiology, Research Institute of the McGill University Health Center, McGill University, 1650 Cedar Avenue, Montreal, Quebec, Canada H3G1A4

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Julia Makhlin Departments of Surgery,
Clinical Epidemiology, Research Institute of the McGill University Health Center, McGill University, 1650 Cedar Avenue, Montreal, Quebec, Canada H3G1A4

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John Sampalis Departments of Surgery,
Clinical Epidemiology, Research Institute of the McGill University Health Center, McGill University, 1650 Cedar Avenue, Montreal, Quebec, Canada H3G1A4

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Lawrence Rosenberg Departments of Surgery,
Clinical Epidemiology, Research Institute of the McGill University Health Center, McGill University, 1650 Cedar Avenue, Montreal, Quebec, Canada H3G1A4

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/42 MAPK and anti-phospho-p44/42 MAPK (Thr202/Tyr204), anti p38 MAPK and anti-phospho-p38 MAPK (Thr180/Tyr182), and rabbit polyclonal antibodies were purchased from Cell Signaling, Inc. (Beverly, MA, USA). Anti-GAPDH, polyclonal, was from Abcam (Cambridge

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06800
Volume/Issue:
Volume 191: Issue 1
Free access
Hyunju Chung Department of Pharmacology and MRC for Bioreaction to ROS and Institute for Medical Sciences, Kyunghee University School of Medicine, Seoul 130-701, South Korea

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Sanghee Seo Department of Pharmacology and MRC for Bioreaction to ROS and Institute for Medical Sciences, Kyunghee University School of Medicine, Seoul 130-701, South Korea

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Minho Moon Department of Pharmacology and MRC for Bioreaction to ROS and Institute for Medical Sciences, Kyunghee University School of Medicine, Seoul 130-701, South Korea

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Seungjoon Park Department of Pharmacology and MRC for Bioreaction to ROS and Institute for Medical Sciences, Kyunghee University School of Medicine, Seoul 130-701, South Korea

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( Yoshida et al. 2004 ). It is shown that IGF-I inhibited OGD-induced apoptosis through the suppression of Par-4 expression. The protective effects of IGF-I were dependent on the activities of the MAPK, PI3K, and PKA signaling pathways. It is also

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-07-0073
Volume/Issue:
Volume 194: Issue 1
Free access
Karen Forbes School of Biomedicine, Maternal and Fetal Health Research Centre, Manchester Academic Health Sciences Centre, University of Manchester, Manchester M13 9WL, UK

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Melissa Westwood School of Biomedicine, Maternal and Fetal Health Research Centre, Manchester Academic Health Sciences Centre, University of Manchester, Manchester M13 9WL, UK

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–23 ( Beenken & Mohammadi 2009 ). Not all members of the FGF family have the potential to signal, but those that do exert their effects by interacting with four different receptors (FGFR1–4) to activate signal transduction pathways, such as the MAPK cascade, and

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-10-0174
Volume/Issue:
Volume 207: Issue 1
Free access
Nasser Al-Shanti Institute for Biomedical Research into Human Movement and Health, Manchester Metropolitan University, Hassall Road, Alsager, Cheshire ST7 2HL, England, UK

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Claire E Stewart Institute for Biomedical Research into Human Movement and Health, Manchester Metropolitan University, Hassall Road, Alsager, Cheshire ST7 2HL, England, UK

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fibroblast growth factor, that mediate their biological effects through various intracellular signalling cascades, such as Janus kinase/signal transducers and activators of transcription, Ras/mitogen-activated protein kinase (MAPK) and phosphatidylinositol 3

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-08-0151
Volume/Issue:
Volume 198: Issue 1
Free access
Diego Safian Reproductive Biology Group, Division Developmental Biology, Institute of Biodynamics and Biocomplexity, Department of Biology , Faculty of Science, University of Utrecht, Utrecht, The Netherlands

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Jan Bogerd Reproductive Biology Group, Division Developmental Biology, Institute of Biodynamics and Biocomplexity, Department of Biology , Faculty of Science, University of Utrecht, Utrecht, The Netherlands

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Rüdiger W Schulz Reproductive Biology Group, Division Developmental Biology, Institute of Biodynamics and Biocomplexity, Department of Biology , Faculty of Science, University of Utrecht, Utrecht, The Netherlands
Reproduction and Developmental Biology Group, Institute of Marine Research, Nordnes, Bergen, Norway

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 µM XAV939 for 5 days to analyze the expression of selected genes. Igf1 receptor activation mainly triggers the MAPK pathway and the PI3K pathway ( LeRoith 2008 ). To study which mechanism Igf3 uses to stimulate β-catenin signaling, we examined if a

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-18-0124
Volume/Issue:
Volume 238: Issue 3
Free access
Lei Li Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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Ping Ma Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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Chen Huang Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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Yongjun Liu Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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Ye Zhang Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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Chen Gao Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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Tianxia Xiao Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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Pei-Gen Ren Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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Brian A Zabel Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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Jian V Zhang Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China
Laboratory for Reproductive Health, Palo Alto Institute for Research and Education, Guangdong Key Laboratory of Nanomedicine, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

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(Erk1/2) (1:2000, #4370, Cell signaling, Boston, MA, USA), rabbit MAB to p44/42 MAPK (Erk1/2) (1:1000, #4695, Cell signaling), followed by an incubation with HRP-conjugated goat anti-rabbit IgG (1:8000, ab136817, Abcam). Specific bands were visualised

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-13-0275
Volume/Issue:
Volume 220: Issue 2
Free access
S Greco Laboratory of Cellular Physiology, Department of Biological and Environmental Sciences and Technologies (DiSTeBA), Ecotekne, Via Provinciale per Monteroni, 73100 Lecce, Italy

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C Storelli Laboratory of Cellular Physiology, Department of Biological and Environmental Sciences and Technologies (DiSTeBA), Ecotekne, Via Provinciale per Monteroni, 73100 Lecce, Italy

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S Marsigliante Laboratory of Cellular Physiology, Department of Biological and Environmental Sciences and Technologies (DiSTeBA), Ecotekne, Via Provinciale per Monteroni, 73100 Lecce, Italy

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activation of the mitogen-activated protein kinase (MAPK) cascade ( Jaffa et al. 1997 , Graness et al. 1998 , Naraba et al. 1998 ). There are several modes of coupling of the B 2 receptor to the MAPK extracellular signal-regulated kinases 1 and 2

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06433
Volume/Issue:
Volume 188: Issue 1
Free access