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  • "angiotensin(1–7)" x
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Xue-Lian Zhang Department of Endocrinology, Beijing Tongren Hospital, Capital Medical University, Beijing, China

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Xinyi Zhao Department of Physiology, School of Medicine, Jinan University, Guangzhou, China

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Yong Wu Department of Physiology, School of Medicine, Jinan University, Guangzhou, China
Department of Biomedical Engineering, Faculty of Engineering, The Hong Kong Polytechnic University, Hong Kong, China

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Wen-qing Huang Department of Transfusion Medicine, Shenzhen Hospital, Southern Medical University, Shenzhen, Guangdong, China

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Jun-jiang Chen Department of Physiology, School of Medicine, Jinan University, Guangzhou, China
Department of Biomedical Engineering, Faculty of Engineering, The Hong Kong Polytechnic University, Hong Kong, China

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Peijie Hu Department of Biomedical Engineering, Faculty of Engineering, The Hong Kong Polytechnic University, Hong Kong, China

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Wei Liu Department of Endocrinology, Beijing Tongren Hospital, Capital Medical University, Beijing, China

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Yi-Wen Chen Department of Endocrinology, Beijing Tongren Hospital, Capital Medical University, Beijing, China

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Jin Hao Department of Endocrinology, Beijing Tongren Hospital, Capital Medical University, Beijing, China

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Rong-Rong Xie Department of Endocrinology, Beijing Tongren Hospital, Capital Medical University, Beijing, China

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Hsiao Chang Chan Epithelial Cell Biology Research Center, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China

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Ye Chun Ruan Department of Biomedical Engineering, Faculty of Engineering, The Hong Kong Polytechnic University, Hong Kong, China

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Hui Chen Cell-Gene Therapy Translational Medicine Research Center, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China

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Jinghui Guo Department of Physiology, School of Medicine, Jinan University, Guangzhou, China

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of ACE-2, angiotensin(1–7) (Ang(1–7)) and its receptor (MAS-1), which causes vasodilation and therefore counteracts the pressor arm ( 4 ). While the over-activated pressor arm causes a deleterious effect contributing to the end-organ damage in

Article Type:
Research Article
Collections:
Metabolic Syndrome and Diabetes
DOI:
https://doi.org/10.1530/EC-21-0357
Volume/Issue:
Volume 11: Issue 1
Open access
Janaína Felix Braga Department of Physiology and Biophysics, National Institute of Science and Technology in Nanobiopharmaceutics, Institute of Biological Sciences, Federal University of Minas Gerais, Belo Horizonte, Minas Gerais, Brazil

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Daniela Ravizzoni Dartora Cardiology Institute of Rio Grande do Sul/University Foundation of Cardiology (IC/FUC), Porto Alegre, Rio Grande do Sul, Brazil

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Natalia Alenina Max-Delbruck Center of Molecular Medicine (MDC), Berlin-Buch, Berlin, Germany

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Michael Bader Cardiology Institute of Rio Grande do Sul/University Foundation of Cardiology (IC/FUC), Porto Alegre, Rio Grande do Sul, Brazil

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Robson Augusto Souza Santos Department of Physiology and Biophysics, National Institute of Science and Technology in Nanobiopharmaceutics, Institute of Biological Sciences, Federal University of Minas Gerais, Belo Horizonte, Minas Gerais, Brazil
Cardiology Institute of Rio Grande do Sul/University Foundation of Cardiology (IC/FUC), Porto Alegre, Rio Grande do Sul, Brazil

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the pathophysiology of diabetes and metabolic syndrome ( 2 ). In the past few years, our understanding of the role of the heptapeptide angiotensin(1–7) has been extended to include other organs and systems well beyond the heart, vessels and the

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-16-0098
Volume/Issue:
Volume 6: Issue 1
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M L M Barreto-Chaves Department of Anatomy, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil

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N Senger Department of Anatomy, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil

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M R Fevereiro Department of Anatomy, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil

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A C Parletta Department of Anatomy, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil

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A P C Takano Department of Anatomy, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil

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-(1–9), angiotensin-(1–9); Ang-(1–7), angiotensin-(1–7); ACE, angiotensin I converting enzyme; ACE2, angiotensin II converting enzyme; AT1R, angiotensin II receptor type 1; AT2R, angiotensin II receptor type 2. Although the RAS has been

Article Type:
Review Article
DOI:
https://doi.org/10.1530/EC-19-0543
Volume/Issue:
Volume 9: Issue 3
Open access
Martin Wiegand MRC Biostatistics Unit, School of Clinical Medicine, University of Cambridge, Cambridge, UK

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David J Halsall Cambridge University Hospitals NHS Foundation Trust, Cambridge, UK

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Sarah L Cowan Cambridge University Hospitals NHS Foundation Trust, Cambridge, UK

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Kevin Taylor Cambridge University Hospitals NHS Foundation Trust, Cambridge, UK

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Robert J B Goudie MRC Biostatistics Unit, School of Clinical Medicine, University of Cambridge, Cambridge, UK

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Jacobus Preller Cambridge University Hospitals NHS Foundation Trust, Cambridge, UK

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Mark Gurnell Cambridge University Hospitals NHS Foundation Trust, Cambridge, UK
Wellcome–MRC Institute of Metabolic Science, University of Cambridge and NIHR Cambridge Biomedical Research Centre, Addenbrooke’s Hospital, Cambridge, UK

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activation by converting angiotensin II (AngII) to angiotensin 1–7 (Ang 1–7). Ang 1–7 exerts anti-inflammatory, anti-oxidative and vasodilatory effects via binding to the Mas receptor ( 4 ). AngII binds AngII receptor type 1 which then exerts pro

Article Type:
Research Article
Collections:
Adrenal
DOI:
https://doi.org/10.1530/EC-22-0190
Volume/Issue:
Volume 11: Issue 11
Open access
Paraskevi Kazakou Diabetes Centre, Department of Clinical Therapeutics, Alexandra Hospital, School of Medicine, National and Kapodistrian University of Athens, Athens, Greece

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Stavroula A Paschou Endocrine Unit, Department of Clinical Therapeutics, Alexandra Hospital, School of Medicine, National and Kapodistrian University of Athens, Athens, Greece

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Theodora Psaltopoulou Unit of Hematology and Oncology, Department of Clinical Therapeutics, Alexandra Hospital, School of Medicine, National and Kapodistrian University of Athens, Athens, Greece

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Maria Gavriatopoulou Unit of Hematology and Oncology, Department of Clinical Therapeutics, Alexandra Hospital, School of Medicine, National and Kapodistrian University of Athens, Athens, Greece

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Eleni Korompoki Department of Clinical Therapeutics, Alexandra Hospital, School of Medicine, National and Kapodistrian University of Athens, Athens, Greece

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Katerina Stefanaki Endocrine Unit, Department of Clinical Therapeutics, Alexandra Hospital, School of Medicine, National and Kapodistrian University of Athens, Athens, Greece

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Fotini Kanouta Department of Endocrinology, Alexandra Hospital, Athens, Greece

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Georgia N Kassi Department of Endocrinology, Alexandra Hospital, Athens, Greece

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Meletios-Athanasios Dimopoulos Unit of Hematology and Oncology, Department of Clinical Therapeutics, Alexandra Hospital, School of Medicine, National and Kapodistrian University of Athens, Athens, Greece

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Asimina Mitrakou Diabetes Centre, Department of Clinical Therapeutics, Alexandra Hospital, School of Medicine, National and Kapodistrian University of Athens, Athens, Greece

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Yuan L . Activation of ACE2/angiotensin (1–7) attenuates pancreatic β cell dedifferentiation in a high-fat-diet mouse model . Metabolism: Clinical and Experimental 2018 81 83 – 96 . ( https://doi.org/10.1016/j.metabol.2017.12.003 ) 65 Shoemaker

Article Type:
Review Article
DOI:
https://doi.org/10.1530/EC-21-0184
Volume/Issue:
Volume 10: Issue 9
Open access