Diabetes as a disease of endoplasmic reticulum stress
Endoplasmic reticulum (ER) stress is an integral part of life for all professional secretory cells, but it has been studied to greatest depth in the pancreatic β‐cell. This reflects both the crucial role played by ER stress in the pathogenesis of diabetes and also the exquisite vulnerability of thes...
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Published in | Diabetes/metabolism research and reviews Vol. 26; no. 8; pp. 611 - 621 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Chichester, UK
John Wiley & Sons, Ltd
01.11.2010
Wiley |
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Abstract | Endoplasmic reticulum (ER) stress is an integral part of life for all professional secretory cells, but it has been studied to greatest depth in the pancreatic β‐cell. This reflects both the crucial role played by ER stress in the pathogenesis of diabetes and also the exquisite vulnerability of these cells to ER dysfunction. The adaptive cellular response to ER stress, the unfolded protein response, comprises mechanisms to both regulate new protein translation and a transcriptional program to allow adaptation to the stress. The core of this response is a triad of stress‐sensing proteins: protein kinase R‐like endoplasmic reticulum kinase (PERK), inositol‐requiring enzyme 1 (IRE1) and activating transcription factor 6. All three regulate portions of the transcriptional unfolded protein response, while PERK also attenuates protein synthesis during ER stress and IRE1 interacts directly with the c‐Jun amino‐terminal kinase stress kinase pathway. In this review we shall discuss these processes in detail, with emphasis given to their impact on diabetes and how recent findings indicate that ER stress may be responsible for the loss of β‐cell mass in the disease. Copyright © 2010 John Wiley & Sons, Ltd. |
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AbstractList | Endoplasmic reticulum (ER) stress is an integral part of life for all professional secretory cells, but it has been studied to greatest depth in the pancreatic β-cell. This reflects both the crucial role played by ER stress in the pathogenesis of diabetes and also the exquisite vulnerability of these cells to ER dysfunction. The adaptive cellular response to ER stress, the unfolded protein response, comprises mechanisms to both regulate new protein translation and a transcriptional program to allow adaptation to the stress. The core of this response is a triad of stress-sensing proteins: protein kinase R-like endoplasmic reticulum kinase (PERK), inositol-requiring enzyme 1 (IRE1) and activating transcription factor 6. All three regulate portions of the transcriptional unfolded protein response, while PERK also attenuates protein synthesis during ER stress and IRE1 interacts directly with the c-Jun amino-terminal kinase stress kinase pathway. In this review we shall discuss these processes in detail, with emphasis given to their impact on diabetes and how recent findings indicate that ER stress may be responsible for the loss of β-cell mass in the disease. Abstract Endoplasmic reticulum (ER) stress is an integral part of life for all professional secretory cells, but it has been studied to greatest depth in the pancreatic β‐cell. This reflects both the crucial role played by ER stress in the pathogenesis of diabetes and also the exquisite vulnerability of these cells to ER dysfunction. The adaptive cellular response to ER stress, the unfolded protein response, comprises mechanisms to both regulate new protein translation and a transcriptional program to allow adaptation to the stress. The core of this response is a triad of stress‐sensing proteins: protein kinase R‐like endoplasmic reticulum kinase (PERK), inositol‐requiring enzyme 1 (IRE1) and activating transcription factor 6. All three regulate portions of the transcriptional unfolded protein response, while PERK also attenuates protein synthesis during ER stress and IRE1 interacts directly with the c‐Jun amino‐terminal kinase stress kinase pathway. In this review we shall discuss these processes in detail, with emphasis given to their impact on diabetes and how recent findings indicate that ER stress may be responsible for the loss of β‐cell mass in the disease. Copyright © 2010 John Wiley & Sons, Ltd. Endoplasmic reticulum (ER) stress is an integral part of life for all professional secretory cells, but it has been studied to greatest depth in the pancreatic β‐cell. This reflects both the crucial role played by ER stress in the pathogenesis of diabetes and also the exquisite vulnerability of these cells to ER dysfunction. The adaptive cellular response to ER stress, the unfolded protein response, comprises mechanisms to both regulate new protein translation and a transcriptional program to allow adaptation to the stress. The core of this response is a triad of stress‐sensing proteins: protein kinase R‐like endoplasmic reticulum kinase (PERK), inositol‐requiring enzyme 1 (IRE1) and activating transcription factor 6. All three regulate portions of the transcriptional unfolded protein response, while PERK also attenuates protein synthesis during ER stress and IRE1 interacts directly with the c‐Jun amino‐terminal kinase stress kinase pathway. In this review we shall discuss these processes in detail, with emphasis given to their impact on diabetes and how recent findings indicate that ER stress may be responsible for the loss of β‐cell mass in the disease. Copyright © 2010 John Wiley & Sons, Ltd. |
Author | Daly, Marie-Louise Dalton, Lucy E. Malzer, Elke Thomas, Sally E. Marciniak, Stefan J. |
Author_xml | – sequence: 1 givenname: Sally E. surname: Thomas fullname: Thomas, Sally E. organization: Department of Medicine, Cambridge Institute for Medical Research, University of Cambridge, Wellcome Trust/MRC Building, Cambridge, UK – sequence: 2 givenname: Lucy E. surname: Dalton fullname: Dalton, Lucy E. organization: Department of Medicine, Cambridge Institute for Medical Research, University of Cambridge, Wellcome Trust/MRC Building, Cambridge, UK – sequence: 3 givenname: Marie-Louise surname: Daly fullname: Daly, Marie-Louise organization: Department of Medicine, Cambridge Institute for Medical Research, University of Cambridge, Wellcome Trust/MRC Building, Cambridge, UK – sequence: 4 givenname: Elke surname: Malzer fullname: Malzer, Elke organization: Department of Medicine, Cambridge Institute for Medical Research, University of Cambridge, Wellcome Trust/MRC Building, Cambridge, UK – sequence: 5 givenname: Stefan J. surname: Marciniak fullname: Marciniak, Stefan J. email: sjm20@cam.ac.uk organization: Department of Medicine, Cambridge Institute for Medical Research, University of Cambridge, Wellcome Trust/MRC Building, Cambridge, UK |
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Snippet | Endoplasmic reticulum (ER) stress is an integral part of life for all professional secretory cells, but it has been studied to greatest depth in the pancreatic... Abstract Endoplasmic reticulum (ER) stress is an integral part of life for all professional secretory cells, but it has been studied to greatest depth in the... |
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SubjectTerms | Activating Transcription Factor 6 - physiology Animals Biological and medical sciences diabetes Diabetes Mellitus - physiopathology Diabetes Mellitus, Type 1 - physiopathology Diabetes. Impaired glucose tolerance DNA-Binding Proteins - physiology Endocrine pancreas. Apud cells (diseases) Endocrinopathies Endoplasmic Reticulum - physiology Endoribonucleases - physiology Epiphyses - abnormalities Epiphyses - physiopathology ER stress Etiopathogenesis. Screening. Investigations. Target tissue resistance Fundamental and applied biological sciences. Psychology General aspects Glycoproteins - physiology Humans Insulin-Secreting Cells - cytology Insulin-Secreting Cells - physiology Islets of Langerhans - physiology Medical sciences Mice Osteochondrodysplasias - physiopathology PERK Protein-Serine-Threonine Kinases - physiology Regulatory Factor X Transcription Factors Stress, Physiological - physiology Transcription Factors - physiology Unfolded Protein Response UPR Vertebrates: endocrinology |
Title | Diabetes as a disease of endoplasmic reticulum stress |
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