[PDF][PDF] Endoplasmic reticulum stress and the unfolded protein response in pancreatic islet inflammation

K Meyerovich, F Ortis, F Allagnat, AK Cardozo - J Mol …, 2016 - Soc Endocrinology
K Meyerovich, F Ortis, F Allagnat, AK Cardozo
J Mol Endocrinol, 2016Soc Endocrinology
Insulin-secreting pancreatic β-cells are extremely dependent on their endoplasmic reticulum
(ER) to cope with the oscillatory requirement of secreted insulin to maintain normoglycemia.
Insulin translation and folding rely greatly on the unfolded protein response (UPR), an array
of three main signaling pathways designed to maintain ER homeostasis and limit ER stress.
However, prolonged or excessive UPR activation triggers alternative molecular pathways
that can lead to β-cell dysfunction and apoptosis. An increasing number of studies suggest a …
Abstract
Insulin-secreting pancreatic β-cells are extremely dependent on their endoplasmic reticulum (ER) to cope with the oscillatory requirement of secreted insulin to maintain normoglycemia. Insulin translation and folding rely greatly on the unfolded protein response (UPR), an array of three main signaling pathways designed to maintain ER homeostasis and limit ER stress. However, prolonged or excessive UPR activation triggers alternative molecular pathways that can lead to β-cell dysfunction and apoptosis. An increasing number of studies suggest a role of these pro-apoptotic UPR pathways in the downfall of β-cells observed in diabetic patients. Particularly, the past few years highlighted a cross talk between the UPR and inflammation in the context of both type 1 (T1D) and type 2 diabetes (T2D). In this article, we describe the recent advances in research regarding the interplay between ER stress, the UPR, and inflammation in the context of β-cell apoptosis leading to diabetes.
Soc Endocrinology