The uncoupling protein UCP1 from brown adipose tissue is a mitochondrial carrier which allows dissipation of metabolic energy as heat. We have characterized the human UCP1 (HsUCP1) recombinantly expressed in Saccharomyces cerevisiae and we demonstrate that HsUCP1 is activated by fatty acids and retinoids in a nucleotide sensitive manner just as its rodent orthologs. However, in the absence of regulators, rodent UCP1 presents a high ohmic proton conductance that cannot be detected in HsUCP1. Since the human protein can be activated in a nucleotide sensitive manner, we conclude that it must have lost selectively the basal proton conductance.
Keywords: Bioenergetics; Brown adipose tissue; Fatty acid; Retinoid; UCP1; Uncoupling protein.
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