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Mitochondrial uncoupling proteins in energy expenditure
1Pennington Biomedical Research Center, Baton Rouge, Louisiana 70808, USA. kozaklp@pbrc.edu
Annual Review of Nutrition
|August 15, 2000
Summary
New UCP1 protein relatives share structural traits but lack thermogenic function. Upregulating the original UCP1 protein effectively combats obesity.
Area of Science:
- Mitochondrial biology
- Adipose tissue research
- Protein biochemistry
Background:
- Brown adipose tissue (BAT) plays a key role in thermogenesis.
- Mitochondrial uncoupling protein 1 (UCP1) is central to BAT function.
- The physiological roles of UCP1 homologues are largely unknown.
Purpose of the Study:
- To investigate the functional similarity of four novel UCP1 homologues.
- To assess the potential thermogenic capacity of these homologues in vivo.
- To reinforce the role of UCP1 in adiposity regulation.
Main Methods:
- Sequence similarity analysis of UCP1 and its homologues.
- Expression of homologues in yeast to assess mitochondrial membrane potential.
- Review of existing evidence on UCP1 function and adiposity.
Main Results:
- Identified four UCP1 homologues with 29-58% sequence similarity.
- Demonstrated that homologues, like UCP1, can reduce mitochondrial membrane potential in yeast.
- Found no conclusive evidence for in vivo thermogenic function of the homologues.
- Accumulating evidence supports UCP1 upregulation in reducing adiposity.
Conclusions:
- UCP1 homologues share structural characteristics and can affect mitochondrial membrane potential.
- The thermogenic function of UCP1 homologues in vivo remains unproven.
- UCP1's role in reducing excessive adiposity is increasingly supported by evidence.