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Review
. 2017 May:34:135-140.
doi: 10.1016/j.mito.2017.03.005. Epub 2017 Mar 25.

Uncoupling protein 2 and metabolic diseases

Affiliations
Review

Uncoupling protein 2 and metabolic diseases

Annapoorna Sreedhar et al. Mitochondrion. 2017 May.

Abstract

Mitochondria are fascinating organelles involved in various cellular-metabolic activities that are integral for mammalian development. Although they perform diverse, yet interconnected functions, mitochondria are remarkably regulated by complex signaling networks. Therefore, it is not surprising that mitochondrial dysfunction is involved in plethora of diseases, including neurodegenerative and metabolic disorders. One of the many factors that lead to mitochondrial-associated metabolic diseases is the uncoupling protein-2, a family of mitochondrial anion proteins present in the inner mitochondrial membrane. Since their discovery, uncoupling proteins have attracted considerable attention due to their involvement in mitochondrial-mediated oxidative stress and energy metabolism. This review attempts to provide a summary of recent developments in the field of uncoupling protein 2 relating to mitochondrial associated metabolic diseases.

Keywords: Cancer; Diabetes; Metabolic disorder; Mitochondrial dysfunction; Obesity; Uncoupling proteins.

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Figures

Figure 1
Figure 1
Mitochondrial oxidative phosphorylation system Reduced cofactors such as NADH+ and FADH2 donate electrons to protein complexes (ETC) embedded on the inner mitochondrial membrane. Energy used from the electron transport is used to pump protons across the inner mitochondrial membrane, setting up a membrane potential that drives the ATP synthase to generate ATP. Uncoupling proteins are anion transporters, also present in the inner mitochondrial membrane that transport protons back into the mitochondrial matrix allowing them to bypass ATP synthase, thereby generating heat instead of ATP.
Figure 2
Figure 2
Structure of Uncoupling proteins Uncoupling proteins and other mitochondrial anion transporters share similar structure. UCPs are made up of six transmembrane domains that are linked by hydrophilic segments. Every third domain is made up of two α-helices and a polar domain.
Figure 3
Figure 3
Schematic diagram of uncoupling protein 2 activation
Figure 4
Figure 4
The role of UCP2 in various metabolic diseases

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