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E C Chin Reproduction and Development Group, Department of Veterinary Basic Sciences, Royal Veterinary College, Royal College Street, London NW1 0TU, UK

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D R E Abayasekara Reproduction and Development Group, Department of Veterinary Basic Sciences, Royal Veterinary College, Royal College Street, London NW1 0TU, UK

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) signal transduction pathway. The activation of the MAPK signal transduction pathway has been implicated in the regulation of steroidogenesis. Studies performed in rat ( Das et al. 1996 ) and pig ( Cameron et al. 1996 ) granulosa cells

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.05550
Volume/Issue:
Volume 183: Issue 1
Free access
Hyunju Chung Department of Pharmacology and Medical Research Center for Bioreaction to ROS and Biomedical Science Institute, Kyunghee University School of Medicine, Seoul 130-701, South Korea

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Sanghee Seo Department of Pharmacology and Medical Research Center for Bioreaction to ROS and Biomedical Science Institute, Kyunghee University School of Medicine, Seoul 130-701, South Korea

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Minho Moon Department of Pharmacology and Medical Research Center for Bioreaction to ROS and Biomedical Science Institute, Kyunghee University School of Medicine, Seoul 130-701, South Korea

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Seungjoon Park Department of Pharmacology and Medical Research Center for Bioreaction to ROS and Biomedical Science Institute, Kyunghee University School of Medicine, Seoul 130-701, South Korea

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from the apoptotic stimuli induced by OGD insult. The protective effects of AG and UAG were dependent on the activities of the MAPK and PI3K/Akt signaling pathways. AG- and UAG-induced stimulation of PI3K/Akt pathways resulted in inactivation of GSK-3β

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-08-0160
Volume/Issue:
Volume 198: Issue 3
Free access
Jorge G Ferreira Laboratory of Molecular Cell Biology,
Institute of Histology and Embryology, Faculty of Medicine of Porto, Porto, Portugal
Instituto de Biologia Molecular e Celular (IBMC), Porto, Portugal
IPATIMUP Porto Portugal

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Célia D Cruz Laboratory of Molecular Cell Biology,
Institute of Histology and Embryology, Faculty of Medicine of Porto, Porto, Portugal
Instituto de Biologia Molecular e Celular (IBMC), Porto, Portugal
IPATIMUP Porto Portugal

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Delminda Neves Laboratory of Molecular Cell Biology,
Institute of Histology and Embryology, Faculty of Medicine of Porto, Porto, Portugal
Instituto de Biologia Molecular e Celular (IBMC), Porto, Portugal
IPATIMUP Porto Portugal

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Duarte Pignatelli Laboratory of Molecular Cell Biology,
Institute of Histology and Embryology, Faculty of Medicine of Porto, Porto, Portugal
Instituto de Biologia Molecular e Celular (IBMC), Porto, Portugal
IPATIMUP Porto Portugal

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extracellular signal regulated kinases (ERKs) have begun to clarify the participation of these kinases not only in the regulatory mechanisms of adrenal function, particularly in steroid hormone synthesis, but also their pro-proliferative effects ( Watanabe et

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06961
Volume/Issue:
Volume 192: Issue 3
Free access
Isabelle Lee Department of Systems Pharmacology & Translational Therapeutics, Perelman School of Medicine, University of Philadelphia, Philadelphia, Pennsylvania, USA

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Guannan Zhang Department of Systems Pharmacology & Translational Therapeutics, Perelman School of Medicine, University of Philadelphia, Philadelphia, Pennsylvania, USA
Center of Excellence in Environmental Toxicology, Perelman School of Medicine, University of Philadelphia, Philadelphia, Pennsylvania, USA

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Clementina Mesaros Department of Systems Pharmacology & Translational Therapeutics, Perelman School of Medicine, University of Philadelphia, Philadelphia, Pennsylvania, USA
Center of Excellence in Environmental Toxicology, Perelman School of Medicine, University of Philadelphia, Philadelphia, Pennsylvania, USA

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Trevor M Penning Department of Systems Pharmacology & Translational Therapeutics, Perelman School of Medicine, University of Philadelphia, Philadelphia, Pennsylvania, USA
Center of Excellence in Environmental Toxicology, Perelman School of Medicine, University of Philadelphia, Philadelphia, Pennsylvania, USA

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et al. 2011 ) pathways have also been implicated in estrogen signaling in endometrial cancer. PAHs have similarly been implicated in EGFR and MAPK pathways in their role in cancer development ( Burdick et al. 2003 , Rodríguez-Fragoso et al. 2009

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-19-0579
Volume/Issue:
Volume 247: Issue 2
Free access
L Nicol
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M-O Faure MRC Human Reproductive Sciences Unit, The Queen's Medical Research Institute, UMR 6175 INRA-CNRS-Université de TOURS-Haras Nationaux, Centre for Reproductive Biology, 47 Little France Crescent, Edinburgh, EH16 4TJ, UK

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J R McNeilly
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J Fontaine MRC Human Reproductive Sciences Unit, The Queen's Medical Research Institute, UMR 6175 INRA-CNRS-Université de TOURS-Haras Nationaux, Centre for Reproductive Biology, 47 Little France Crescent, Edinburgh, EH16 4TJ, UK

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C Taragnat MRC Human Reproductive Sciences Unit, The Queen's Medical Research Institute, UMR 6175 INRA-CNRS-Université de TOURS-Haras Nationaux, Centre for Reproductive Biology, 47 Little France Crescent, Edinburgh, EH16 4TJ, UK

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A S McNeilly
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treatment groups. Values represent means± s.e.m. from one representative experiment; n =2. Effects of BMP-4 on the GnRH-induced activation of ERK1/2, p38 MAPK and CREB As there is evidence that, as well as signalling through the Smad pathways

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-07-0542
Volume/Issue:
Volume 196: Issue 3
Open access
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Lise M Sjøgaard-Frich Section for Cell Biology and Physiology, Department of Biology, Faculty of Science, University of Copenhagen, Denmark

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Morten Sølling Henriksen Section for Cell Biology and Physiology, Department of Biology, Faculty of Science, University of Copenhagen, Denmark

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Shi Min Lam Section for Cell Biology and Physiology, Department of Biology, Faculty of Science, University of Copenhagen, Denmark

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Frida Jolande Birkbak Section for Cell Biology and Physiology, Department of Biology, Faculty of Science, University of Copenhagen, Denmark

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Dominika Czaplinska Section for Cell Biology and Physiology, Department of Biology, Faculty of Science, University of Copenhagen, Denmark

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Mette Flinck Section for Cell Biology and Physiology, Department of Biology, Faculty of Science, University of Copenhagen, Denmark

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Stine Falsig Pedersen Section for Cell Biology and Physiology, Department of Biology, Faculty of Science, University of Copenhagen, Denmark

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, Schuster et al. 2018 , Powell et al. 2021 ), and fibrosis ( Kisseleva & Brenner 2021 ), driven by paracrine signaling between hepatocytes, hepatic stellate cells (HSCs), and resident macrophages (Kupffer cells) ( Tsuchida and Friedman, 2017 , Schwabe

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-24-0099
Volume/Issue:
Volume 263: Issue 2
Restricted access
A Trumper
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K Trumper
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D Horsch
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Glucose-dependent insulinotropic polypeptide (GIP) acts as a glucose-dependent growth factor for beta-cells. Here we show that GIP and glucose also act synergistically as anti-apoptotic factors for beta-cells, using the well-differentiated beta-cell line, INS-1. Mitogenic and anti-apoptotic signaling of GIP were dependent upon pleiotropic activation of protein kinase A (PKA)/cAMP regulatory element binder (CREB), mitogen-activated protein kinase (MAPK) and phosphatidylinositol 3-kinase (PI3-kinase)/PKB signaling modules. The signaling modules activated by GIP were dependent on glucose metabolism and calcium influx and were tightly linked by multiple activating and inhibiting cross-talk. These interactions included: (i) a central role of tyrosine phosphorylation for stimulation of PKA/CREB, MAPK and PI3-kinase/PKB, (ii) inhibition of PKA/CREB by the MAPK pathway at the level of MAPK kinase-1 or downstream, (iii) activation of MAPK signaling by PI3-kinase and PKA at the level of extracellular-signal regulated kinase 1/2 or upstream, and (iv) activation of PKB by MAPK and PKA signaling at the level of PKB or upstream. Furthermore, we demonstrated inhibition of CREB signaling by Ca(2+)/calmodulin kinase I/IV. These results indicated that GIP acts as a mitogenic and anti-apoptotic factor for beta-cells by pleiotropic activation of tightly linked signaling pathways in beta-cells.

Article Type:
Other
DOI:
https://doi.org/10.1677/joe.0.1740233
Volume/Issue:
Volume 174: Issue 2
Free access
Birgitte N Friedrichsen Novo Nordisk A/S, Department of Islet Discovery Research, Krogshoejvej 31, 9R2.28, 2880 Bagsværd, Denmark
The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark

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Nicole Neubauer Novo Nordisk A/S, Department of Islet Discovery Research, Krogshoejvej 31, 9R2.28, 2880 Bagsværd, Denmark
The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark

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Ying C Lee Novo Nordisk A/S, Department of Islet Discovery Research, Krogshoejvej 31, 9R2.28, 2880 Bagsværd, Denmark
The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark

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Vivian K Gram Novo Nordisk A/S, Department of Islet Discovery Research, Krogshoejvej 31, 9R2.28, 2880 Bagsværd, Denmark
The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark

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Niels Blume Novo Nordisk A/S, Department of Islet Discovery Research, Krogshoejvej 31, 9R2.28, 2880 Bagsværd, Denmark
The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark

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Jacob S Petersen Novo Nordisk A/S, Department of Islet Discovery Research, Krogshoejvej 31, 9R2.28, 2880 Bagsværd, Denmark
The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark

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Jens H Nielsen Novo Nordisk A/S, Department of Islet Discovery Research, Krogshoejvej 31, 9R2.28, 2880 Bagsværd, Denmark
The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark

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Annette Møldrup Novo Nordisk A/S, Department of Islet Discovery Research, Krogshoejvej 31, 9R2.28, 2880 Bagsværd, Denmark
The University of Copenhagen, Department of Medical Biochemistry and Genetics, Copenhagen, Denmark

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pancreatic β-cells ( Hussain et al. 2000 ). The effects of GLP-1 and GIP on proliferation of the primary β-cells were found to be dependent on cAMP/ PKA, p42 MAPK and PI3K signalling pathways according to inhibitor experiments, similar to previous

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06160
Volume/Issue:
Volume 188: Issue 3
Free access
Samira Fargali Departments of, Neuroscience, Medicine, Geriatrics, Box 1065, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA

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Thomas Scherer Departments of, Neuroscience, Medicine, Geriatrics, Box 1065, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA

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Andrew C Shin Departments of, Neuroscience, Medicine, Geriatrics, Box 1065, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA

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Masato Sadahiro Departments of, Neuroscience, Medicine, Geriatrics, Box 1065, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA

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Christoph Buettner Departments of, Neuroscience, Medicine, Geriatrics, Box 1065, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA
Departments of, Neuroscience, Medicine, Geriatrics, Box 1065, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA

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Stephen R Salton Departments of, Neuroscience, Medicine, Geriatrics, Box 1065, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA
Departments of, Neuroscience, Medicine, Geriatrics, Box 1065, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA

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(LI-COR, Lincoln, NE, USA) 1:1 in TBS. Membranes were incubated overnight at 4 °C with the following rabbit antisera (Cell Signaling, Boston, MA, USA), unless otherwise indicated, diluted in blocking buffer: phospho-AMP-activated protein kinase (AMPKα

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-12-0172
Volume/Issue:
Volume 215: Issue 2
Free access
Bethania Mongi-Bragato Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica, Córdoba, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Investigaciones en Ciencias de la Salud (INICSA), Córdoba, Argentina

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Ezequiel Grondona Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica, Córdoba, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Investigaciones en Ciencias de la Salud (INICSA), Córdoba, Argentina

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Liliana del Valle Sosa Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica, Córdoba, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Investigaciones en Ciencias de la Salud (INICSA), Córdoba, Argentina

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Natacha Zlocowski Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica, Córdoba, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Investigaciones en Ciencias de la Salud (INICSA), Córdoba, Argentina

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Ana Clara Venier Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica, Córdoba, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Investigaciones en Ciencias de la Salud (INICSA), Córdoba, Argentina

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Alicia Inés Torres Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica, Córdoba, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Investigaciones en Ciencias de la Salud (INICSA), Córdoba, Argentina

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Alexandra Latini Laboratório de Bioenergética e Estresse Oxidativo – LABOX, Departamento de Bioquímica, Universidade Federal de Santa Catarina, Campus Universitário, Córrego Grande, Florianópolis, Brasil

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Rodrigo Bainy Leal Departamento de Bioquímica e Programa de Pós-graduação em Bioquímica, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, Florianópolis, Santa Catarina, Brasil

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Silvina Gutiérrez Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica, Córdoba, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Investigaciones en Ciencias de la Salud (INICSA), Córdoba, Argentina

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Ana Lucía De Paul Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica, Córdoba, Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas, Instituto de Investigaciones en Ciencias de la Salud (INICSA), Córdoba, Argentina

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Signaling); anti-p-p38 MAPK (1:10,000, Millipore), anti-t-p38 MAPK (1:10,000), anti-t-JNK (1:5000), or anti-α-Tubulin (1:2000) (Sigma-Aldrich). After washing, membranes were incubated with a peroxidase-conjugated (HRP) goat anti-rabbit (1:5000; Bio

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-19-0506
Volume/Issue:
Volume 245: Issue 2
Restricted access