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J Mol Endocrinol. 2016 Jul;57(1):R1-R17. doi: 10.1530/JME-15-0306. Epub 2016 Apr 11.

Endoplasmic reticulum stress and the unfolded protein response in pancreatic islet inflammation.

Author information

1
ULB Center for Diabetes ResearchUniversité Libre de Bruxelles (ULB), Brussels, Belgium.
2
Department of Cell and Developmental BiologyUniversidade de São Paulo, São Paulo, Brazil.
3
Department of Vascular SurgeryCentre Hospitalier Universitaire Vaudois (CHUV), Lausanne, Switzerland.
4
ULB Center for Diabetes ResearchUniversité Libre de Bruxelles (ULB), Brussels, Belgium akupperc@ulb.ac.be.

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.

KEYWORDS:

NF-kB; diabetes; inflammation; pancreatic beta cells; unfolded protein response

PMID:
27067637
DOI:
10.1530/JME-15-0306
[Indexed for MEDLINE]

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