A new look at UCP 1.
There has been a resurgence of interest in mitochondrial uncoupling protein 1 due to a desire to understand the regulation of the prominent role it plays in control of metabolic flux in brown adipose tissue and non-shivering thermogenesis, combined with the fact that UCP 1 acts as a paradigm for other novel less abundant uncoupling proteins. In this manuscript, we review the recent evidence for detection, purification, identification and function of UCP 1 in thymus mitochondria. In addition, we review the two proposed mechanisms for fatty acid dependent UCP 1 activity, namely (a) the flippase (flip-flop) model and (b) the cofactor/activation model, and the implication for these models of recent data showing that glucose-O-omega-palmitate cannot facilitate UCP 1 activity.
Porter
Richard K
RK
School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland. rkporter@tcd.ie
D002001:Adipose Tissue, Brown / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D003067:Coenzymes / Q000378:metabolism; D004789:Enzyme Activation; D005227:Fatty Acids / Q000378:metabolism; D007473:Ion Channels; D008565:Membrane Proteins / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D024101:Mitochondrial Proteins; D008954:Models, Biological; D013950:Thymus Gland / Q000378:metabolism*; D000071256:Uncoupling Protein 1
D002352:Carrier Proteins; D003067:Coenzymes; D005227:Fatty Acids; D007473:Ion Channels; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; D000071256:Uncoupling Protein 1