Novel Uncoupling Proteins

Affourtit, Charles, Crichton, Paul G., Parker, Nadeene and Brand, Martin D. (2007) Novel Uncoupling Proteins. In: Mitochondrial Biology: New Perspectives. Novartis Foundation Symposia, 287 . Wiley, pp. 70-80. ISBN 9780470066577

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Abstract

Mitochondria are incompletely coupled because of proton leaks that shortcircuit oxidative phosphorylation. Basal proton leak is unregulated and is associated with the presence (but not catalytic activity) of the adenine nucleotide translocase. Inducible proton leak is regulated and is catalysed by the adenine nucleotide translocase and specific uncoupling proteins (UCPs). UCP1 catalyses proton conductance in mammalian brown adipose tissue. It is activated by fatty acids, which overcome nucleotide inhibition. UCP2, UCP3 and UCPs from birds, fish and plants also catalyse proton conductance that is inhibited by nucleotides. However, they require activation by superoxide or other reactive oxygen species (ROS). The mechanism of proton transport by the UCPs is unresolved. UCPs may also transport fatty acids or fatty acyl peroxides. Several physiological functions of UCPs are postulated. (1) UCP1 is specialised for thermogenesis; UCP3 and avian UCPs possibly share this function. (2) UCPs may attenuate ROS production and protect against oxidative damage, degenerative diseases and ageing. (3) UCP3 may catalyse fatty acid transport. (4) UCP2 has a signalling role in pancreatic β cells, where it attenuates insulin secretion. Other roles remain to be discovered.

Item Type: Book Section
Uncontrolled Keywords: mitochondrial proton leak,uncoupling proteins,mild uncoupling,reactive oxygen species,oxidative damage,degenerative disease,ageing,pancreatic beta cells,insulin secretion
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
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Depositing User: Pure Connector
Date Deposited: 03 Nov 2016 11:00
Last Modified: 22 Apr 2020 11:03
URI: https://ueaeprints.uea.ac.uk/id/eprint/61222
DOI: 10.1002/9780470725207.ch6

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