Endoplasmic Reticulum Stress and Lipid Metabolism : Mechanisms and Therapeutic Potential

Joint Authors

Basseri, Sana
Austin, Richard C.

Source

Biochemistry Research International

Issue

Vol. 2012, Issue 2012 (31 Dec. 2012), pp.1-13, 13 p.

Publisher

Hindawi Publishing Corporation

Publication Date

2011-12-13

Country of Publication

Egypt

No. of Pages

13

Main Subjects

Chemistry

Abstract EN

The endoplasmic reticulum (ER) plays a crucial role in protein folding, assembly, and secretion.

Disruption of ER homeostasis may lead to accumulation of misfolded or unfolded proteins in the ER lumen, a condition referred to as ER stress.

In response to ER stress, a signal transduction pathway known as the unfolded protein response (UPR) is activated.

UPR activation allows the cell to cope with an increased protein-folding demand on the ER.

Recent studies have shown that ER stress/UPR activation plays a critical role in lipid metabolism and homeostasis.

ER-stress-dependent dysregulation of lipid metabolism may lead to dyslipidemia, insulin resistance, cardiovascular disease, type 2 diabetes, and obesity.

In this paper, we examine recent findings illustrating the important role ER stress/UPR signalling pathways play in regulation of lipid metabolism, and how they may lead to dysregulation of lipid homeostasis.

American Psychological Association (APA)

Basseri, Sana& Austin, Richard C.. 2011. Endoplasmic Reticulum Stress and Lipid Metabolism : Mechanisms and Therapeutic Potential. Biochemistry Research International،Vol. 2012, no. 2012, pp.1-13.
https://search.emarefa.net/detail/BIM-502483

Modern Language Association (MLA)

Basseri, Sana& Austin, Richard C.. Endoplasmic Reticulum Stress and Lipid Metabolism : Mechanisms and Therapeutic Potential. Biochemistry Research International No. 2012 (2012), pp.1-13.
https://search.emarefa.net/detail/BIM-502483

American Medical Association (AMA)

Basseri, Sana& Austin, Richard C.. Endoplasmic Reticulum Stress and Lipid Metabolism : Mechanisms and Therapeutic Potential. Biochemistry Research International. 2011. Vol. 2012, no. 2012, pp.1-13.
https://search.emarefa.net/detail/BIM-502483

Data Type

Journal Articles

Language

English

Notes

Includes bibliographical references

Record ID

BIM-502483