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Protein Misfolding and Cellular Stress in Disease and Aging

Volume 648 of the series Methods in Molecular Biology pp 43-62

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Consequences of Stress in the Secretary Pathway: The ER Stress Response and Its Role in the Metabolic Syndrome

  • Martin SchröderAffiliated withSchool of Biological and Biomedical Sciences, Durham University Email author 
  • , Louise SutcliffeAffiliated withSchool of Biological and Biomedical Sciences, Durham University

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Abstract

The unfolded protein response (UPR) was originally identified as a signaling network coordinating adaptive and apoptotic responses to accumulation of unfolded proteins in the endoplasmic reticulum (ER). More recent work has shown that UPR signaling can be triggered by a multitude of cellular events and that the UPR plays a critical role in the prevention, and also the progression, of a wide variety of diseases. Much attention has been paid to the role of the UPR in neurodegenerative diseases in the past. More recently, important roles for the UPR in diseases associated with the metabolic syndrome have been discovered. Here we review the role of the UPR in these diseases, including type 2 diabetes, atherosclerosis, fatty liver disease, and ischemia.

Key words

Apoptosis Conformational disease Diabetes Endoplasmic reticulum Inflammation Neurodegenerative disease Unfolded protein response