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UCP2 and UCP3 in muscle controlling body metabolism

Patrick Schrauwen^1,* and Matthijs Hesselink²

Nutrition and Toxicology Research Institute Maastricht (NUTRIM)
¹ Department of Human Biology, Maastricht University, The Netherlands
² Department of Movement Sciences, Maastricht University, The Netherlands
^* Present address: Department of Human Biology, Maastricht University, PO Box 616, 6200 MD Maastricht, The Netherlands

View larger version (25K): [in a new window]   Fig. 1. Action of the electron transport chain leading to the build-up of a proton gradient across the inner mitochondrial membrane. Protons can cross the inner mitochondrial membrane via the F0F1 complex, thereby providing energy for the conversion of ADP to ATP. Alternatively, the proton gradient can be reduced by uncoupling proteins (UCP), either by direct transport of protons from the intermembrane space to the matrix or by transport of fatty acid anions in the opposite direction. Cyt c, cytochrome c. Q, coenzyme Q.

View larger version (18K): [in a new window]   Fig. 2. Hypothesis for the function of uncoupling protein-3 (UCP3): fatty acid anions are transported out of the mitochondrial matrix to prevent accumulation of fatty acid anions inside the matrix (Schrauwen et al., 2001c). FA, fatty acid; CoA, coenzyme A; FAS, fatty acyl-CoA synthetase; CPT1, carnitine palmitoyl transferase-1; CPT2, carnitine palmitoyl transferase-2; H+, proton gradient.