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Katarzyna Czarzasta Department of Experimental and Clinical Physiology, Laboratory of Center for Preclinical Research, Medical University of Warsaw, Warszawa, Poland

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Luminita H Pojoga Division of Endocrinology, Diabetes and Hypertension, Department of Medicine, Brigham and Women’s Hospital/Harvard Medical School, Boston, Massachusetts, USA

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epidermal growth factor receptor (EGFR), or the novel G protein-coupled receptor GPER1 ( Krug et al. 2011 ). Caveolin-1 is an organizer of MR signaling pathways Interestingly, the rapid MR-mediated signaling cascades mentioned above (e

Article Type:
Review Article
DOI:
https://doi.org/10.1530/JOE-23-0341
Volume/Issue:
Volume 262: Issue 3
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Young Hoon Son Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea

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Seok-Jin Lee Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea

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Ki-Baek Lee Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea

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Jin-Haeng Lee Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea

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Eui Man Jeong Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea
Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea

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Sun Gun Chung Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea

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Sang-Chul Park Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea

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In-Gyu Kim Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea
Department of Biochemistry and Molecular Biology, Institute of Human–Environment Interface Biology, Department of Rehabilitation Medicine, Seoul National University College of Medicine, 103 Daehak‐ro, Jongno‐Gu, Seoul 110‐799, Korea

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comparison with the control cells ( Fig. 1 D). Figure 1 Dexamethasone suppresses caveolin-1 expression at the transcriptional level in C2C12 myotubes. (A) Effect of DEX treatment on the expression of caveolins. C2C12 myotubes were treated with DEX (100 nM, 1

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-14-0490
Volume/Issue:
Volume 225: Issue 1
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Weihua Liu Department of Pediatrics, The Second Affiliated Hospital of Xi’an Jiaotong University, Xi’an, Shaanxi, China
Department of Pediatrics, First Hospital of Xi’an, Xi’an, Shaanxi, China

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Yuqiang Ji Department of Cardiovascular Medicine, First Hospital of Xi’an, Xi’an, Shaanxi, China

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Haiping Chu Department of Pediatrics, First Hospital of Xi’an, Xi’an, Shaanxi, China

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Mo Wang Department of Pediatrics, Maternal and Child Health Hospital of Chang’an District, Xi’an, Shaanxi, China

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Bin Yang Department of Pediatrics, Maternal and Child Health Hospital of Chang’an District, Xi’an, Shaanxi, China

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Chunyan Yin Department of Pediatrics, The Second Affiliated Hospital of Xi’an Jiaotong University, Xi’an, Shaanxi, China

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diabetes ( Wang et al. 2020 ). SFRP5 can improve metabolism disorder by inhibiting inflammatory cell activation in adipose tissue, and Wnt/JNK may be the critical signal pathway in this process ( Ouchi et al . 2010 ). Caveolin-1 is the structural protein

Article Type:
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DOI:
https://doi.org/10.1530/JOE-20-0328
Volume/Issue:
Volume 247: Issue 3
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Cecilia Brännmark Department of Physiology/Metabolic Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Emma I Kay Department of Physiology/Metabolic Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden
Bioscience Metabolism, Research and Early Development, Cardiovascular, Renal and Metabolism, Biopharmaceuticals R&D, AstraZeneca, Gothenburg, Sweden

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Unn Örtegren Kugelberg Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden

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Belén Chanclón Department of Physiology/Metabolic Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Man Mohan Shrestha Department of Physiology/Metabolic Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Ingrid Wernstedt Asterholm Department of Physiology/Metabolic Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Peter Strålfors Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden

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Charlotta S Olofsson Department of Physiology/Metabolic Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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& Draznin 2005 , Cong et al. 2007 , Blumer et al. 2008 , Lim et al. 2015 ). The adipocyte plasma membrane is covered with bulb-like invaginations called caveolae. Maintenance of the caveolae structure requires caveolin-1 (Cav1; Lipardi et al

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-20-0078
Volume/Issue:
Volume 247: Issue 1
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Liliana del V Sosa Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica – Consejo Nacional de Investigaciones Científicas Técnicas (CONICET) Instituto de Investigaciones en Ciencias de la Salud, Córdoba, Argentina

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Juan P Petiti Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica – Consejo Nacional de Investigaciones Científicas Técnicas (CONICET) Instituto de Investigaciones en Ciencias de la Salud, Córdoba, Argentina

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Florencia Picech Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica – Consejo Nacional de Investigaciones Científicas Técnicas (CONICET) Instituto de Investigaciones en Ciencias de la Salud, Córdoba, Argentina

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Sabrina Chumpen Universidad Nacional de Córdoba, Facultad de Ciencias Químicas, CIQUIBIC-CONICET, Cordoba, Argentina

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Juan P Nicola Universidad Nacional de Córdoba, Facultad de Ciencias Químicas, CIBICI-CONICET, Cordoba, Argentina

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Pablo Perez Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica – Consejo Nacional de Investigaciones Científicas Técnicas (CONICET) Instituto de Investigaciones en Ciencias de la Salud, Córdoba, Argentina

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

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Javier Valdez-Taubas Universidad Nacional de Córdoba, Facultad de Ciencias Químicas, CIQUIBIC-CONICET, Cordoba, Argentina

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Silvina Gutierrez Universidad Nacional de Córdoba, Facultad de Ciencias Médicas, Centro de Microscopía Electrónica – Consejo Nacional de Investigaciones Científicas Técnicas (CONICET) Instituto de Investigaciones en Ciencias de la Salud, Córdoba, Argentina

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

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lipid residues increases hydrophobicity, promoting steroid receptor translocation to the caveolae regions of the plasma membrane ( Razandi et al . 2002 , Peffer et al . 2014 ), with the different isoforms of caveolin (caveolin-1 and caveolin-2) being

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-18-0418
Volume/Issue:
Volume 240: Issue 2
Free access
Kotaro Horiguchi Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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Ken Fujiwara Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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Cimi Ilmiawati Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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Motoshi Kikuchi Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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Takehiro Tsukada Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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Tom Kouki Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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Takashi Yashiro Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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was incubated overnight with mouse monoclonal caveolin 1 (12.5 ng/ml; BD Biosciences) or caveolin 3 (5 ng/ml; BD Biosciences), or rabbit polyclonal cyclin D1 (1:2000; NeoMarkers, Inc., Fremont, CA, USA), ERK1/2 (1:3000; Assay Designs, Ann Arbor, MI

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-11-0103
Volume/Issue:
Volume 210: Issue 1
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Ruslan Rafikov
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Fabio V Fonseca Pulmonary Vascular Disease Program, Department of Cell Biology, Vascular Biology Center: CB-3211B, Georgia Health Sciences University, 1459 Laney Walker Boulevard, Augusta, Georgia 30912, USA

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Sanjiv Kumar
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Daniel Pardo
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Charles Darragh
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Shawn Elms
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David Fulton
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Stephen M Black
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this location is important for eNOS activity. The localization of eNOS within the caveolae renders the enzyme inactive due to the interaction of eNOS with caveolin-1 ( Ju et al . 1997 ). This interaction requires that eNOS be both myristoylated and

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-11-0083
Volume/Issue:
Volume 210: Issue 3
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Vincent Ricchiuti Division of Endocrinology, Diabetes and Hypertension, Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, Massachusetts 02115, USA

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Nathalie Lapointe Division of Endocrinology, Diabetes and Hypertension, Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, Massachusetts 02115, USA

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Luminita Pojoga Division of Endocrinology, Diabetes and Hypertension, Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, Massachusetts 02115, USA

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Tham Yao Division of Endocrinology, Diabetes and Hypertension, Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, Massachusetts 02115, USA

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Loc Tran Division of Endocrinology, Diabetes and Hypertension, Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, Massachusetts 02115, USA

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Gordon H Williams Division of Endocrinology, Diabetes and Hypertension, Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, Massachusetts 02115, USA

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Gail K Adler Division of Endocrinology, Diabetes and Hypertension, Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, 221 Longwood Avenue, Boston, Massachusetts 02115, USA

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western blot results using sc-1173 antibody and quantification of AT 1 R in tissue by radioligand binding with I 125 -labeled ANGII ( Oestreicher et al . 2006 ). The following antibodies were also used: caveolin-1 (CAV-1; Cat# RDI-CAVEOL1abrx, Research

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-10-0458
Volume/Issue:
Volume 211: Issue 1
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Stefanie Ruhs Julius Bernstein Institute of Physiology, Martin Luther University Halle-Wittenberg, Halle, Germany

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Alexander Nolze Julius Bernstein Institute of Physiology, Martin Luther University Halle-Wittenberg, Halle, Germany

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Ralf Hübschmann Julius Bernstein Institute of Physiology, Martin Luther University Halle-Wittenberg, Halle, Germany

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Claudia Grossmann Julius Bernstein Institute of Physiology, Martin Luther University Halle-Wittenberg, Halle, Germany

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, striatin and caveolin-1 (CAV1) were identified as candidates for such scaffolding proteins ( Coutinho et al. 2014 , Ashton et al. 2015 ). For both proteins evidence for an involvement in nongenomic signaling as part of a larger membrane complex exists

Article Type:
Review Article
DOI:
https://doi.org/10.1530/JOE-16-0659
Volume/Issue:
Volume 234: Issue 1
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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
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