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RESEARCH COMMUNICATION |
a Department of Physiology, Faculty of Medicine, University of Geneva, 1211 Geneva 4, Switzerland
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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Key Words: obesity • cachexia • muscle • uncoupling protein • FFA
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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In an attempt to assess quantitatively the reduction in energy expenditure directed specifically at enhancing fat replenishment, we previously described and validated an experimental rat model of weight recovery in which, after substantial depletion of the fat stores by food restriction, the energy expenditure and energy-partitioning between protein and fat could be assessed by pair-feeding the refed rats with weight-matched controls (12, 13). It was demonstrated that during the first 2–3 wk of such controlled refeeding, the energetic efficiency during refeeding was increased by nearly twofold relative to the controls and that the energy thus conserved was directed at fat deposition, not to protein. Furthermore, this increased metabolic efficiency specific for accelerating fat replenishment was found to persist unabated during cold exposure or at thermoneutrality, i.e., under conditions in which sympathetic neural control of thermogenesis in the rat is markedly activated or suppressed, respectively (14). Together, these studies have led to the proposal that a component in the suppression of thermogenesis during the period of food restriction is dictated by the state of depletion of the fat stores (11) and persists during the early phase of refeeding, with the energy thus conserved being directed specifically to replenishment of the fat stores. Furthermore, this component of energy conservation can be dissociated from sympathetic neural modulation of thermogenesis (14) and, by extension, from the modulation of uncoupling protein (UCP1)2 activity in brown adipose tisssue (BAT), an important site of sympathetically mediated thermogenesis (15–20).
On the other hand, since skeletal muscle, another important site of energy conservation during starvation (21), is unresponsive to modulation by the sympathetic nervous system (SNS) in response to diet and cold (22), the possibility arises that this tissue, unlike BAT, may be an important site for mechanisms underlying thermogenic mechanisms that are SNS independent and whose modulation could underlie the elevated energetic efficiency for accelerated fat replenishment. The recent cloning of UCP3, a gene with 1) high sequence homology to UCP1 (23, 24), 2) in vitro uncoupling activity when overexpressed in yeast (25), and 3) high mRNA expression specific to skeletal muscles as well as to BAT (23–25) therefore provides a candidate gene that may underlie the postulated SNS-independent control of thermogenesis in this tissue.
To explore this possibility, we have compared, in our rat model of weight recovery, the pattern of changes in mRNA of UCP3 in skeletal muscles with those of UCP1 and UCP3 in interscapular BAT (IBAT) during food restriction and at various time points during the course of controlled refeeding. The mRNA expression of UCP3 was assessed both in the gastrocnemius (a mixed fiber muscle that possesses high activities for both glycolytic and oxidative enzymes) and the soleus (a predominantly slow-twitch fiber muscle that has a low potential for glycolytic activity and high activities for oxidative enzymes), two muscles with different capacities for shifting between glucose and lipids as fuel substrate (26–28). We have also assessed in these tissues the changes in mRNA expression of UCP2, another UCP homologue, which, unlike UCP1 and UCP3, has been shown to be ubiquitously expressed in rat and human tissues (29, 30).
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MATERIALS AND METHODS |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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Study design
The experiment was conducted by using a design similar to that previously described in establishing the rat model of weight recovery for studying adjustments in energy expenditure and energy partitioning (12–14). Groups of rats (n=5–8) were food-restricted for 2 wk at approximately 50% of the spontaneous food intake of ad libitum-fed rats (mean intake of 30 g daily) by providing them with a fixed ration of 30 g every 2 days; the food-restricted rats were fasted on alternate days. At the end of this food restriction period (corresponding to day 0 of refeeding), two groups of rats were killed and the animals in the other groups were refed the chow diet at a level approximately equal in metabolizable energy (ME) content to the spontaneous food intake of rats matched for weight at the onset of refeeding. The refed animals were pair-fed to the weight-matched controls fed ad libitum. Two groups of these control animals (n=6) were also killed at this time (day 0); other groups (n=5–8) of refed and controls animals were killed at points corresponding to days 3, 5, 7, 10, and 14 of refeeding. All animals were killed by decapitation. Changes in body energy content, body composition (fat and protein), and energetic efficiency were determined during week 1 (wk 1) and wk 2 from groups killed on day 0, 7, or 14. Assays for UCP1 and the UCP homologues in IBAT and skeletal muscles as well as for serum free fatty acids (FFA) (NEFA C kit, Wako Chemicals GmbH, Neuss, Germany) were conducted in groups killed on days 0, 3, 5, and 10. The gastrocnemius and soleus muscles as well as IBAT were rapidly dissected out and cleaned of tissue debris, immediately frozen in liquid nitrogen, and then stored at -80dgC until later processing for assay of mRNA expression of the UCPs. The remaining carcasses were also analyzed for body fat content.
Determination of body composition
After the animals were killed, the skull, thorax, and abdominal cavity were incised and the gut was cleaned of undigested food. The whole carcasses were then dried to a constant weight in an oven maintained at 60°C and were subsequently homogenized. Triplicate samples of the homogenized carcass were analyzed for energy content by bomb calorimetry (31) and for fat content by the Soxhlet extraction method (32), which uses light petroleum ether. Body protein was determined from a general formula relating energy derived from fat, total energy value of the carcass, and energy derived from protein (12); the calorific values for body fat and protein were taken as 38.6 and 22.7 kJ/g, respectively.
Determination of energy balance and energetic efficiency
Energy balance measurements were conducted, as previously described (12–14), by the comparative carcass technique over two sequential periods of 1 wk each, during which food intake and food spillage were continuously monitored. For each period, energy expenditure was determined as the difference between energy gain and ME intake; the energetic efficiency was calculated as the percentage of energy gained per ME intake.
Extraction of total RNA and Northern blotting
Total RNA was isolated by the method of Chomczynski and Sacchi (33). Fifteen micrograms of each RNA sample were loaded onto a 1.2% formaldehyde gel, as described by Lehrach et al. (34), and electrophoresed overnight. After vacuum blotting of the gel onto a nylon membrane (Electran Nylon Blotting Membrane, BDH Laboratory Supplies, Poole, U.K.) at 60 mBarrs for 3 h, the RNAs were UV cross-linked onto the membrane. The coloration of the membrane with a solution containing 0.04% Bromophenol blue/0.5 M sodium acetate, pH 5.2, showed an equal loading.
Northern blot analysis
The UCP3 and UCP2 probes were obtained as described previously (24, 35). Hybridizations were performed in QuickHyb solution (Stratagene, La Jolla, Calif.) with a probe random labeled with [
-3232P]dCTP and at a specific activity of 109 dpm/µg DNA. The membranes were then washed in 2 x SSC (20xSSC is 3M sodium chloride, 0.3 M sodium citrate, pH 7.0), 0.1% SDS twice for 5 min at 50°C, and finally once in 0.1 x SSC, 0.1% SDS at 50°C. The blots were exposed to ECL films (Amersham, Bucks, U.K.). Equal loading and transfer were checked by using an oligonucleotide specific for 18S RNA subunit labeled with [-32P]ATP. The signals on the autoradiograms were quantified by scanning photodensitometry using ImageQuant Software Version 3.3 (Molecular Dynamics, Sunnyvale, Calif.). To allow quantitative between-group comparison over time for a given UCP in a given tissue, the samples for refed and control animals at the four time points were loaded on the same gel. However, neither between-tissue comparisons nor between-UCP comparisons are possible because of loading limitations on a given gel and differences in the specific activity of labeled probes for the various UCPs.
Data analysis and statistics
The data were analyzed by using two-factor analysis of variance (ANOVA) for the main effects of groups and time as well as for the group x time interaction. Between-group comparisons at specific time points were conducted using the rank sum two-sample (Mann-Whitney) test; the level of statistical significance was taken as P < 0.05. All statistical analyses were performed using the computer software STATISTIX, version 4.0 (Analytical Software, St. Paul, Minnesota, Minn.).
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RESULTS |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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Table 1.
Body weight and protein at days 0, 7, and 14, as well as the gain in weight and protein between days 0–7 (wk 1) and days 7–14 (wk 2), are not significantly different for the refed and control groups. By contrast, body fat, which is reduced by approximately 50% below control levels at the end of food restriction (day 0 of refeeding), is found to be higher in the refed group than in controls on days 7 and 14; ANOVA indicates a significant group effect as well as a significant interaction between group and time (P<0.001), thereby suggesting a highly significant difference between refed and controls groups across time. Indeed, actual calculation of the gain in body fat suggests that body fat was laid down approximately 2.8-fold faster in the refed rats than in controls during both wk 1 and wk 2. As indicated by the results of ANOVA for body fat and body energy gain, the significant group effect but nonsignificant interaction term suggest that the differences between refed and controls in these parameters are not dependent on the time periods, i.e., they are significantly higher in the refed group than in the control group during both wk 1 and wk 2, despite no between-group difference in energy intake. By contrast, energy expenditure is significantly lower in the refed than in controls during both wk 1 (-17%) and wk 2 (-16%). This is reflected in the energetic efficiency, which is found to be greater in the refed than in controls by approximately twofold during both wk 1 and wk 2.
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UCP mRNA expression
These data on body fat at time points 0, 7, and 14, together with data for body fat measured in other groups of animals at time points 0, 3, 5, and 10, are presented in Fig. 1,
which shows the more rapid gain in body fat in the refed than in controls during all time intervals (0–3, 3–5, 5–7, 7–10, 10–14), even though food intake did not differ between these two groups. The results on mRNA expression of the various UCPs, measured at days 0, 3, 5, and 10, are hence described in relation to 1) the time point at the end of food restriction (day 0 of refeeding) when body fat is 50% depleted, with serum FFA being elevated; and 2) at time points (3, 5, and 10) during this phase of increased efficiency of fat gain (validated in the energy balance study conducted during the two sequential periods described above), with serum FFA being restored to control levels by day 5 of refeeding.
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In IBAT, mRNA expression of UCP3 in the refed group follows the same pattern as for UCP1. The expressions are markedly lower than in controls at the end of food restriction (day 0) and have returned to the levels found in controls by day 5 of refeeding, a time point that is still early in the phase of accelerated fat deposition. As shown in 
Fig. 1, the greater rate of body fat gain in the refed group persisted beyond 10 days of refeeding.
In both skeletal muscles, UCP3 mRNA expressions are found to be elevated relative to controls at the end of food restriction (day 0), an effect that is more marked in the gastrocnemius (5-fold increase, P<0.01) than in the soleus (2.5-fold increase, P=0.08). On day 3 of refeeding, UCP3 mRNA expression in both skeletal muscles is found to be lower than in controls, and again the effect is much more pronounced in the gastrocnemius (12-fold reduction, P<0.01) than in the soleus muscle (2.6-fold reduction, P<0.05). Furthermore, whereas the mRNA level of UCP3 in the gastrocnemius muscle remains markedly below control levels on day 5 of refeeding and remains incompletely restored relative to controls by day 10, in the soleus muscle, by contrast, it is found to be completely restored to control levels by day 5 of refeeding.
The changes in UCP2 mRNA expression in various tissues during food restriction and refeeding followed the same pattern as that found for UCP3 ( Table 2).
Like UCP1 and UCP3 mRNA expressions in IBAT, the mRNA level of UCP2 is also lower in this tissue at the end of food restriction (day 0) and is restored to control levels by day 5 of refeeding; for all UCPs in IBAT, ANOVA indicates a highly significant interaction between the two groups (refed and control) over time (P<0.001). In skeletal muscle, mRNA expression of UCP2, like that for UCP3, is found to be increased both in the gastrocnemius and soleus at the end of food restriction (day 0). Although UCP2 and UCP3 expression in the gastrocnemius muscle is markedly decreased (below control levels) on day 3 of refeeding and remains incompletely restored even on day 10 of refeeding, its levels in the soleus muscle are not different from control values as early as day 3 of refeeding. ANOVA indicates a highly significant interaction between the refed and control groups over time for UCP2 and UCP3 mRNA levels in the gastrocnemius muscle (P<0.002), but no significant group effect or interaction between groups over time is found for UCP2 and UCP3 in the soleus muscle. Representative Northern blots showing the levels of mRNA expression of UCP1 in IBAT, and of UCP homologues in all three tissues from refed and control animals, are presented in Fig. 2.
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Additional experiment: fasting at thermoneutrality
In view of the findings described above of an unexpected increase in UCP3 and UCP2 mRNA expressions in skeletal muscles during food deprivation, we have conducted additional studies to investigate whether this up-regulation of skeletal muscle UCP homologues could be related to the increased thermoregulatory needs of the body consequential to the starvation-induced loss of body weight (hence increased ratio of surface area-to-volume) and loss of body fat (hence reduced insulation). To this end, two separate experiments assessed the effect of 48 h fasting on UCP2 and UCP3 mRNA expression in the gastrocnemius and soleus: one was conducted at laboratory temperature (22°C) and the other under conditions of thermoneutrality (29°C). In both experiments, the fed animals were allowed ad libitum access to food and water, whereas the fasted animals had access only to water containing 0.45% NaCl. The fasting period started 1 wk after adaptation to housing conditions and environmental temperature. The results show that in both gastrocnemius and soleus muscles, mRNA expression of UCP3 and UCP2 is markedly higher in fasted animals than in fed controls, and the fasting-induced up-regulation of muscle UCP homologues occurs even when the experiment is conducted under conditions of thermoneutrality ( Fig. 3).
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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Fig. 1showing that gain in body fat was higher in refed than in controls over all time intervals, as well as the lack of between-group differences in body protein and protein gain ( Table 1), suggest that virtually all the energy conserved in the refed animals was directed specifically at enhancing fat deposition throughout the 14-day refeeding period.
Dissociation of high efficiency of fat recovery from SNS-BAT-UCP1 axis
The results of this study pertaining to the pattern of mRNA expression of UCP1 during food restriction and refeeding provide evidence complementary to our previous suggestion that this component of suppressed thermogenesis for rapid fat deposition can be dissociated from the sympathetic control of thermogenesis (14), and by extension, to BAT, a tissue whose thermogenic activity is primarily under sympathetic control of its uncoupling protein, UCP1 (15–20). Figure 1shows the marked down-regulation of UCP1 mRNA levels in IBAT in response to food deprivation is in accordance with its well-established role in energy conservation during food deprivation (16–20). However, the present findings that its expression is restored to control levels by day 5, a time point still early in the phase of accelerated fat deposition (which lasts for ~14 days or more), is in line with our contention that tissues such as BAT, whose thermogenic activity is under SNS control, are unlikely be important sites for the component of reduced thermogenesis that underlies the elevated efficiency of fat recovery. Indeed, under conditions whereby the dietary modulations of SNS activity and BAT thermogenic capacity have been shown to be overridden by thermoregulatory needs—i.e., in the cold (36) and at thermoneutrality (37)—the efficiency of fat deposition in the refed animals remains higher than in controls (14).
Dissociation of regulatory thermogenesis from skeletal muscle UCPs
Since SNS activity in skeletal muscle is unresponsive to modulation by diet and cold exposure (22) and because this tissue is an important site of energy conservation during starvation (21), the possibility arises that the skeletal muscle is an important site for this component of suppressed thermogenesis, which is SNS independent. This led us to examine whether skeletal muscle UCP3 and UCP2, the two recently cloned genes with high sequence homology to BAT UCP1, could be implicated in energy conservation during food restriction and refeeding. Our results on the pattern of UCP mRNA expressions in both gastrocnemius and soleus muscles are at variance, however, with a role for skeletal muscle UCP homologues in dietary regulation of thermogenesis in general and in regulatory thermogenesis underlying energy conservation in particular. First, expression of these genes is found to be up-regulated during food deprivation, a directional change in mRNA expression that is opposite to that expected for any putative uncoupling protein with regulatory functions vis-à-vis energy conservation. Second, the possibility that the up-regulation of skeletal muscle UCPs during food deprivation may reflect their functional role as `inhibitory modulators' of thermogenesis in this tissue is not tenable, since one would expect such `inhibitory modulation' to be either sustained or to return gradually toward control levels during refeeding, when energy conservation persists in our animal model, rather than to be down-regulated below control levels. Third, it has been suggested that the mRNA up-regulation of skeletal muscle UCPs during food deprivation may still be reflecting an uncoupling effect, but whose functional importance is to meet the increased thermoregulatory needs of the body consequential to starvation-induced body wasting, loss of insulation, and overall energy conservation (25). However, this explanation is difficult to reconcile with 1) the demonstration, by blood flow studies coupled with regional arteriovenous oxygen differences, that skeletal muscle is a quantitatively important site of energy conservation during starvation (21), and 2) the findings that mRNA expressions of these UCP homologues are down-regulated (i.e., below control levels) during refeeding, a phase when the energy conservation phenomenon is still very much evident and has been shown to persist independent of the thermoregulatory needs of the rat (14). Furthermore, the data presented here ( Fig. 3) that fasting-induced up-regulation of UCP2 and UCP3 mRNA in skeletal muscles occurs even when the animals are maintained at thermoneutrality (i.e., under conditions of reduced thermoregulatory needs), coupled with previous reports that cold exposure has no effect on these UCP homologues in muscle (24, 35), also argue against a functional role for these UCPs in thermoregulatory thermogenesis.
Relationship between skeletal muscle UCP and altered lipid fuel utilization
By contrast, the tissue-dependent differential expression of UCP homologues in response to dietary manipulation in our study reveals a much more coherent relationship between the pattern of transcription of these genes and the tissue requirements for lipids as fuel substrates. First, mRNA up-regulation of UCP2 and UCP3 in both gastrocnemius and soleus muscles at the end of food restriction correlates with the increased circulating levels of FFA and hence with the expected increased uptake and utilization of lipids as fuel substrates by skeletal muscles during starvation. Second, down-regulation of UCPs in these skeletal muscles (in particular, the gastrocnemius muscle) during refeeding correlates with the need to reduce the utilization of lipids as a fuel substrate to levels well below those of controls, since the refed rats have to `spare' lipids for storage, given the drive (underlain by mechanisms that suppress thermogenesis) to accelerate fat deposition during weight recovery. Indeed, the still incomplete recovery of both UCP2 and UCP3 mRNA expression in the gastrocnemius muscle even on day 10 of refeeding correlates well with the phenomenon of the accelerated rate of fat deposition lasting for more than 10 days in our animal model. The close association between enhanced fat recovery and the expression of UCP homologues observed in gastrocnemius muscle contrasts with the weaker association found between enhanced fat recovery and the expression of UCP1 and UCP homologues in BAT, and hence could underlie a more important role for skeletal muscles than for BAT as a site for the modulation of fat utilization during weight recovery after starvation. Third, the differential responses of the two skeletal muscles studied (gastrocnemius and the soleus) to food deprivation vis-à-vis mRNA expression of UCP2 and UCP3, as well as differences in their pattern of expression during the course of refeeding, are also consistent with the heterogeneity in skeletal muscle types in their glycolytic and oxidative enzymes activities and hence in their capacity to shift between lipids and glucose as fuel substrates (26–28). In the gastrocnemius muscle (mixed fiber type), with its great capacity to switch between lipids and glucose for fuel substrates, the magnitude of increase in its UCP mRNA expressions during food restriction (period of increased lipid uptake and utilization) was severalfold greater than in the soleus muscle, which is an oxidative (red fiber) type muscle that has a low glycolytic capacity, high dependency on lipids as fuel substrates even in the fed state, and thus has less capacity to increase lipid utilization further during food deprivation. The same explanation is also valid for the differential responses of UCP expression in these two muscle types during refeeding. The much more sustained down-regulation of UCP2 and UCP3 mRNA expression in the gastrocnemius vs. the soleus muscle can be attributed to the much larger glycolytic capacity of the gastrocnemius, and hence to its greater ability to sustain a shift toward glucose utilization in order to `spare' lipids for storage during a phase of increased efficiency of fat deposition. Indeed, the greater dependency of the soleus muscle (than the gastrocnemius muscle) on lipids as fuel substrates is reflected in the close association of its UCP mRNA expressions with circulating FFA both during food restriction and refeeding ( Fig. 1). These observations also raise the possibility that FFA might be a modulator of gene transcription of these UCP homologues in highly oxidative skeletal muscles, and investigations using both pharmacological and nutritional approaches are under way in our laboratory to test this hypothesis.
Role of UCP homologues in adipose tissues
Finally, the proposed role of UCP2 and UCP3 in regulating lipids as fuel substrate in the skeletal muscles can be extended to adipose tissues. In BAT, a tissue that is highly dependent on lipids to fuel its thermogenesis, and in which increased glucose uptake (e.g., during cold exposure) is generally directed at lipogenesis to meet the high FFA demands for fuel rather than for substrate oxidation (38, 39), regulation of its lipids for fuel is intimately linked with the regulation of this tissue's thermogenic state. This is well illustrated in the present study, where the pattern of changes in IBAT mRNA expression of UCP1 (the established functional uncoupler) is similar to that for UCP2 and UCP3 in this tissue: all are markedly down-regulated during food deprivation and simultaneously restored during refeeding. These findings, together with other reports that expression is up-regulated in this tissue in response to cold (35), would also be consistent with a role for UCP2 and UCP3 homologues in regulating lipids as fuel substrates for UCP-1-mediated thermogenesis in BAT. In white adipose tissue, on the other hand, reports that mRNA expression of UCP2 and/or of UCP3 are up-regulated under conditions of increased lipid utilization—specifically, 1) in rats resisting obesity when fed a high-fat diet (29), 2) treated with adrenoceptor agonists (25), or 3) infused with a recombinant adenovirus containing leptin (40)—are also in line with a role for these UCP homologues as regulators of lipids as a fuel substrate.
In summary, this study reveals tissue dependency in transcriptional changes in these UCP2 and UCP3 homologues (not only between IBAT and the skeletal muscles, but also between muscle types) that are consistent both with the differential requirements of these tissues for lipids during food deprivation and in their capacity to shift from lipids to glucose during refeeding. These findings are therefore much more consistent with a functional role for UCP2 and UCP3 as regulators of lipids as fuel substrate rather than as mediators of regulatory thermogenesis. Additional studies would need to dissect out the exact control points at which these UCPs homologues may be acting in this postulated regulation of fuel lipids and, among some of the contenders, whether this can be pinpointed to regulation at the level of competition between lipids and carbohydrates utilization (Randle glucose–FFA cycle), to the regulation of lipolysis within the tissue's triglyceride pool, to FFA carriers across the mitochondrial membrane, or to the regulation of lipid oxidation and peroxidation. The development of assays for the protein products and their exact localization within the cell would no doubt be the first steps in elucidating the exact functional role of these UCP homologues. A better understanding of the mechanisms underlying the regulation of fuel lipids will have wide implications in the field of metabolism and in clinical medicine, particularly in elucidating the metabolic basis of obesity and its relapse, in the etiology of non-insulin-dependent diabetes, and in pathophysiological cachexic conditions (e.g., AIDS, cancer, sepsis) in which nutritional rehabilitation is characterized by the tendency to recover fat rather than lean tisssue, leading to difficulties in restoring body functions.
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ACKNOWLEDGMENTS |
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FOOTNOTES |
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2 Abbreviations: BAT, brown adipose tissue; SNS, sympathetic nervous system; FFA, free fatty acids; UCP, uncoupling protein; IBAT, intercapsular BAT; wk 1, week 1; ME, metabolizable energy; ANOVA, analysis of variance; UCP, uncoupling protein.
Received for publication December 2, 1997. Accepted for publication January 22, 1998.
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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 M. Damon, I. Louveau, L. Lefaucheur, B. Lebret, A. Vincent, P. Leroy, M. P. Sanchez, P. Herpin, and F. Gondret Number of intramuscular adipocytes and fatty acid binding protein-4 content are significant indicators of intramuscular fat level in crossbred Large White x Duroc pigs J Anim Sci, May 1, 2006; 84(5): 1083 - 1092. [Abstract] [Full Text] [PDF]
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M. Jastroch, S. Wuertz, W. Kloas, and M. Klingenspor Uncoupling protein 1 in fish uncovers an ancient evolutionary history of mammalian nonshivering thermogenesis Physiol Genomics, July 14, 2005; 22(2): 150 - 156. [Abstract] [Full Text] [PDF]
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 K De Bock, E. A Richter, A. P Russell, B. O Eijnde, W Derave, M Ramaekers, E Koninckx, B Leger, J Verhaeghe, and P Hespel Exercise in the fasted state facilitates fibre type-specific intramyocellular lipid breakdown and stimulates glycogen resynthesis in humans J. Physiol., April 15, 2005; 564(2): 649 - 660. [Abstract] [Full Text] [PDF]
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 P. Cettour-Rose, S. Samec, A. P. Russell, S. Summermatter, D. Mainieri, C. Carrillo-Theander, J.-P. Montani, J. Seydoux, F. Rohner-Jeanrenaud, and A. G. Dulloo Redistribution of Glucose From Skeletal Muscle to Adipose Tissue During Catch-Up Fat: A Link Between Catch-Up Growth and Later Metabolic Syndrome Diabetes, March 1, 2005; 54(3): 751 - 756. [Abstract] [Full Text] [PDF]
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M. Katsumata, M. Matsumoto, S. Kawakami, and Y. Kaji Effect of heat exposure on uncoupling protein-3 mRNA abundance in porcine skeletal muscle J Anim Sci, December 1, 2004; 82(12): 3493 - 3499. [Abstract] [Full Text] [PDF]
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M. A. Stavinoha, J. W. RaySpellicy, M. F. Essop, C. Graveleau, E. D. Abel, M. L. Hart-Sailors, H. J. Mersmann, M. S. Bray, and M. E. Young Evidence for mitochondrial thioesterase 1 as a peroxisome proliferator-activated receptor-{alpha}-regulated gene in cardiac and skeletal muscle Am J Physiol Endocrinol Metab, November 1, 2004; 287(5): E888 - E895. [Abstract] [Full Text] [PDF]
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 A Mostyn, J C Litten, K S Perkins, M C Alves-Guerra, C Pecqueur, B Miroux, M E Symonds, and L Clarke Influence of genotype on the differential ontogeny of uncoupling protein 2 and 3 in subcutaneous adipose tissue and muscle in neonatal pigs J. Endocrinol., October 1, 2004; 183(1): 121 - 131. [Abstract] [Full Text] [PDF]
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M. Guzman, J. Lo Verme, J. Fu, F. Oveisi, C. Blazquez, and D. Piomelli Oleoylethanolamide Stimulates Lipolysis by Activating the Nuclear Receptor Peroxisome Proliferator-activated Receptor {alpha} (PPAR-{alpha}) J. Biol. Chem., July 2, 2004; 279(27): 27849 - 27854. [Abstract] [Full Text] [PDF]
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M. D'Adamo, L. Perego, M. Cardellini, M. A. Marini, S. Frontoni, F. Andreozzi, A. Sciacqua, D. Lauro, P. Sbraccia, M. Federici, et al. The -866A/A Genotype in the Promoter of the Human Uncoupling Protein 2 Gene Is Associated With Insulin Resistance and Increased Risk of Type 2 Diabetes Diabetes, July 1, 2004; 53(7): 1905 - 1910. [Abstract] [Full Text] [PDF]
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M. Jastroch, K. Withers, and M. Klingenspor Uncoupling protein 2 and 3 in marsupials: identification, phylogeny, and gene expression in response to cold and fasting in Antechinus flavipes Physiol Genomics, April 13, 2004; 17(2): 130 - 139. [Abstract] [Full Text] [PDF]
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C. B. Chan, M. C. Saleh, V. Koshkin, and M. B. Wheeler Uncoupling Protein 2 and Islet Function Diabetes, February 1, 2004; 53(90001): S136 - 142. [Abstract] [Full Text]
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 U. Dressel, T. L. Allen, J. B. Pippal, P. R. Rohde, P. Lau, and G. E. O. Muscat The Peroxisome Proliferator-Activated Receptor {beta}/{delta} Agonist, GW501516, Regulates the Expression of Genes Involved in Lipid Catabolism and Energy Uncoupling in Skeletal Muscle Cells Mol. Endocrinol., December 1, 2003; 17(12): 2477 - 2493. [Abstract] [Full Text] [PDF]
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A. M. Rodriguez, P. Roca, M. L. Bonet, C. Pico, P. Oliver, and A. Palou Positive correlation of skeletal muscle UCP3 mRNA levels with overweight in male, but not in female, rats Am J Physiol Regulatory Integrative Comp Physiol, October 1, 2003; 285(4): R880 - R888. [Abstract] [Full Text] [PDF]
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X. Sun, C. Wray, X. Tian, P.-O. Hasselgren, and J. Lu Expression of uncoupling protein 3 is upregulated in skeletal muscle during sepsis Am J Physiol Endocrinol Metab, September 1, 2003; 285(3): E512 - E520. [Abstract] [Full Text] [PDF]
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C. T Putman, M. Kiricsi, J. Pearcey, I. M MacLean, J. A Bamford, G. K Murdoch, W. T Dixon, and D. Pette AMPK activation increases uncoupling protein-3 expression and mitochondrial enzyme activities in rat muscle without fibre type transitions J. Physiol., August 15, 2003; 551(1): 169 - 178. [Abstract] [Full Text] [PDF]
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 H.R. Gosker, P. Schrauwen, M.K.C. Hesselink, G. Schaart, G.J. van der Vusse, E.F.M. Wouters, and A.M.W.J. Schols Uncoupling protein-3 content is decreased in peripheral skeletal muscle of patients with COPD Eur. Respir. J., July 1, 2003; 22(1): 88 - 93. [Abstract] [Full Text] [PDF]
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R. Crescenzo, S. Samec, V. Antic, F. Rohner-Jeanrenaud, J. Seydoux, J.-P. Montani, and A. G. Dulloo A Role for Suppressed Thermogenesis Favoring Catch-Up Fat in the Pathophysiology of Catch-Up Growth Diabetes, May 1, 2003; 52(5): 1090 - 1097. [Abstract] [Full Text] [PDF]
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A. Collin, M. Taouis, J. Buyse, N. B. Ifuta, V. M. Darras, P. Van As, R. D. Malheiros, V. M. B. Moraes, and E. Decuypere Thyroid status, but not insulin status, affects expression of avian uncoupling protein mRNA in chicken Am J Physiol Endocrinol Metab, April 1, 2003; 284(4): E771 - E777. [Abstract] [Full Text] [PDF]
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T. E. Jones, K. Baar, E. Ojuka, M. Chen, and J. O. Holloszy Exercise induces an increase in muscle UCP3 as a component of the increase in mitochondrial biogenesis Am J Physiol Endocrinol Metab, January 1, 2003; 284(1): E96 - E101. [Abstract] [Full Text] [PDF]
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J. St-Pierre, J. A. Buckingham, S. J. Roebuck, and M. D. Brand Topology of Superoxide Production from Different Sites in the Mitochondrial Electron Transport Chain J. Biol. Chem., November 15, 2002; 277(47): 44784 - 44790. [Abstract] [Full Text] [PDF]
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R. T. JAGOE, S. H. LECKER, M. GOMES, and A. L. GOLDBERG Patterns of gene expression in atrophying skeletal muscles: response to food deprivation FASEB J, November 1, 2002; 16(13): 1697 - 1712. [Abstract] [Full Text] [PDF]
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A. V. Medvedev, J. Robidoux, X. Bai, W. Cao, L. M. Floering, K. W. Daniel, and S. Collins Regulation of the Uncoupling Protein-2 Gene in INS-1 beta -Cells by Oleic Acid J. Biol. Chem., November 1, 2002; 277(45): 42639 - 42644. [Abstract] [Full Text] [PDF]
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 T. Peng, T. R. Golub, and D. M. Sabatini The Immunosuppressant Rapamycin Mimics a Starvation-Like Signal Distinct from Amino Acid and Glucose Deprivation Mol. Cell. Biol., August 1, 2002; 22(15): 5575 - 5584. [Abstract] [Full Text] [PDF]
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M.-E. Harper, R. Dent, S. Monemdjou, V. Bezaire, L. Van Wyck, G. Wells, G. N. Kavaslar, A. Gauthier, F. Tesson, and R. McPherson Decreased Mitochondrial Proton Leak and Reduced Expression of Uncoupling Protein 3 in Skeletal Muscle of Obese Diet-Resistant Women Diabetes, August 1, 2002; 51(8): 2459 - 2466. [Abstract] [Full Text] [PDF]
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D. M. Muoio, P. S. MacLean, D. B. Lang, S. Li, J. A. Houmard, J. M. Way, D. A. Winegar, J. C. Corton, G. L. Dohm, and W. E. Kraus Fatty Acid Homeostasis and Induction of Lipid Regulatory Genes in Skeletal Muscles of Peroxisome Proliferator-activated Receptor (PPAR) alpha Knock-out Mice. EVIDENCE FOR COMPENSATORY REGULATION BY PPARdelta J. Biol. Chem., July 12, 2002; 277(29): 26089 - 26097. [Abstract] [Full Text] [PDF]
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H. M. Roche, E. Noone, C. Sewter, S. Mc Bennett, D. Savage, M. J. Gibney, S. O'Rahilly, and A. J. Vidal-Puig Isomer-Dependent Metabolic Effects of Conjugated Linoleic Acid: Insights From Molecular Markers Sterol Regulatory Element-Binding Protein-1c and LXR{alpha} Diabetes, July 1, 2002; 51(7): 2037 - 2044. [Abstract] [Full Text] [PDF]
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N A Curtin, J C Clapham, and C J Barclay Excess recovery heat production by isolated muscles from mice overexpressing uncoupling protein-3 J. Physiol., July 1, 2002; 542(1): 231 - 235. [Abstract] [Full Text] [PDF]
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 V. M Rodriguez, M. P Portillo, C. Pico, M T. Macarulla, and A. Palou Olive oil feeding up-regulates uncoupling protein genes in rat brown adipose tissue and skeletal muscle Am. J. Clinical Nutrition, February 1, 2002; 75(2): 213 - 220. [Abstract] [Full Text] [PDF]
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 S. Collins, W. Cao, K. W. Daniel, T. M. Dixon, A. V. Medvedev, H. Onuma, and R. Surwit Adrenoceptors, Uncoupling Proteins, and Energy Expenditure Experimental Biology and Medicine, December 1, 2001; 226(11): 982 - 990. [Abstract] [Full Text] [PDF]
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 K. A. J. M. Van der Lee, P. H. M. Willemsen, S. Samec, J. Seydoux, A. G. Dulloo, M. M. A. L. Pelsers, J. F. C. Glatz, G. J. Van der Vusse, and M. Van Bilsen Fasting-induced changes in the expression of genes controlling substrate metabolism in the rat heart J. Lipid Res., November 1, 2001; 42(11): 1752 - 1758. [Abstract] [Full Text] [PDF]
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P. SCHRAUWEN, W. H. M. SARIS, and M. K. C. HESSELINK An alternative function for human uncoupling protein 3: protection of mitochondria against accumulation of nonesterified fatty acids inside the mitochondrial matrix FASEB J, November 1, 2001; 15(13): 2497 - 2502. [Abstract] [Full Text] [PDF]
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V. Bezaire, W. Hofmann, J. K. G. Kramer, L. P. Kozak, and M.-E. Harper Effects of fasting on muscle mitochondrial energetics and fatty acid metabolism in Ucp3(-/-) and wild-type mice Am J Physiol Endocrinol Metab, November 1, 2001; 281(5): E975 - E982. [Abstract] [Full Text] [PDF]
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 L. T. Dalgaard, T. I. A. Sørensen, T. Drivsholm, K. Borch-Johnsen, T. Andersen, T. Hansen, and O. Pedersen A Prevalent Polymorphism in the Promoter of the UCP3Gene and Its Relationship to Body Mass Index and Long Term Body Weight Change in the Danish Population J. Clin. Endocrinol. Metab., March 1, 2001; 86(3): 1398 - 1402. [Abstract] [Full Text]
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R. Fabris, E. Nisoli, A. M. Lombardi, C. Tonello, R. Serra, M. Granzotto, I. Cusin, F. Rohner-Jeanrenaud, G. Federspil, M. O. Carruba, et al. Preferential Channeling of Energy Fuels Toward Fat Rather Than Muscle During High Free Fatty Acid Availability in Rats Diabetes, March 1, 2001; 50(3): 601 - 608. [Abstract] [Full Text]
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J. Himms-Hagen and M.-E. Harper Physiological Role of UCP3 May Be Export of Fatty Acids from Mitochondria When Fatty Acid Oxidation Predominates: An Hypothesis Experimental Biology and Medicine, February 1, 2001; 226(2): 78 - 84. [Abstract] [Full Text]
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 Abdul.G. Dulloo and S. Samec Uncoupling Proteins: Do They Have a Role in Body Weight Regulation? Physiology, December 1, 2000; 15(6): 313 - 318. [Abstract] [Full Text] [PDF]
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S. Diano, H. F. Urbanski, B. Horvath, I. Bechmann, A. Kagiya, G. Nemeth, F. Naftolin, C. H. Warden, and T. L. Horvath Mitochondrial Uncoupling Protein 2 (UCP2) in the Nonhuman Primate Brain and Pituitary Endocrinology, November 1, 2000; 141(11): 4226 - 4238. [Abstract] [Full Text] [PDF]
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 P. M. Fuller, C. H. Warden, S. J. Barry, and C. A. Fuller Effects of 2-G exposure on temperature regulation, circadian rhythms, and adiposity in UCP2/3 transgenic mice J Appl Physiol, October 1, 2000; 89(4): 1491 - 1498. [Abstract] [Full Text] [PDF]
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 D. B. West, F. Y. Blohm, A. A. Truett, and J. P. DeLany Conjugated Linoleic Acid Persistently Increases Total Energy Expenditure in AKR/J Mice without Increasing Uncoupling Protein Gene Expression J. Nutr., October 1, 2000; 130(10): 2471 - 2477. [Abstract] [Full Text]
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M. Katsumata, D. Cattaneo, P. White, K. A. Burton, and M. J. Dauncey Growth Hormone Receptor Gene Expression in Porcine Skeletal and Cardiac Muscles Is Selectively Regulated by Postnatal Undernutrition J. Nutr., October 1, 2000; 130(10): 2482 - 2488. [Abstract] [Full Text]
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M. Zhou, B.-Z. Lin, S. Coughlin, G. Vallega, and P. F. Pilch UCP-3 expression in skeletal muscle: effects of exercise, hypoxia, and AMP-activated protein kinase Am J Physiol Endocrinol Metab, September 1, 2000; 279(3): E622 - E629. [Abstract] [Full Text] [PDF]
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X. X. Yu, J. L. Barger, B. B. Boyer, M. D. Brand, G. Pan, and S. H. Adams Impact of endotoxin on UCP homolog mRNA abundance, thermoregulation, and mitochondrial proton leak kinetics Am J Physiol Endocrinol Metab, August 1, 2000; 279(2): E433 - E446. [Abstract] [Full Text] [PDF]
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S. Hidaka, H. Yoshimatsu, T. Kakuma, H. Sakino, S. Kondou, R. Hanada, K. Oka, Y. Teshima, M. Kurokawa, and T. Sakata Tissue-Specific Expression of the Uncoupling Protein Family in Streptozotocin-Induced Diabetic Rats Experimental Biology and Medicine, July 1, 2000; 224(3): 172 - 177. [Abstract] [Full Text]
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J. A Yanovski, A. L Diament, K. N Sovik, T. T Nguyen, H. Li, N. G Sebring, and C. H Warden Associations between uncoupling protein 2, body composition, and resting energy expenditure in lean and obese African American, white, and Asian children Am. J. Clinical Nutrition, June 1, 2000; 71(6): 1405 - 1420. [Abstract] [Full Text] [PDF]
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J. H. Pinkney, O. Boss, G. A. Bray, K. Bulmer, S. W. Coppack, and V. Mohamed-Ali Physiological Relationships of Uncoupling Protein-2 Gene Expression in Human Adipose Tissue in Vivo J. Clin. Endocrinol. Metab., June 1, 2000; 85(6): 2312 - 2317. [Abstract] [Full Text]
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A. L. Hildebrandt and P. D. Neufer Exercise attenuates the fasting-induced transcriptional activation of metabolic genes in skeletal muscle Am J Physiol Endocrinol Metab, June 1, 2000; 278(6): E1078 - E1086. [Abstract] [Full Text] [PDF]
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S. H. Adams Uncoupling Protein Homologs: Emerging Views of Physiological Function J. Nutr., April 1, 2000; 130(4): 711 - 714. [Abstract] [Full Text]
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K. A. J. M. VAN DER LEE, P. H. M. WILLEMSEN, G. J. VAN DER VUSSE, and M. VAN BILSEN Effects of fatty acids on uncoupling protein-2 expression in the rat heart FASEB J, March 1, 2000; 14(3): 495 - 502. [Abstract] [Full Text]
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 T. L. Horvath, C. H. Warden, M. Hajos, A. Lombardi, F. Goglia, and S. Diano Brain Uncoupling Protein 2: Uncoupled Neuronal Mitochondria Predict Thermal Synapses in Homeostatic Centers J. Neurosci., December 1, 1999; 19(23): 10417 - 10427. [Abstract] [Full Text] [PDF]
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H. Vidal, D. Langin, F. Andreelli, L. Millet, D. Larrouy, and M. Laville Lack of skeletal muscle uncoupling protein 2 and 3 mRNA induction during fasting in type-2 diabetic subjects Am J Physiol Endocrinol Metab, November 1, 1999; 277(5): E830 - E837. [Abstract] [Full Text] [PDF]
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 B. Desvergne and W. Wahli Peroxisome Proliferator-Activated Receptors: Nuclear Control of Metabolism Endocr. Rev., October 1, 1999; 20(5): 649 - 688. [Abstract] [Full Text]
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A. Matthias, A. Jacobsson, B. Cannon, and J. Nedergaard The Bioenergetics of Brown Fat Mitochondria from UCP1-ablated Mice. UCP1 IS NOT INVOLVED IN FATTY ACID-INDUCED DE-ENERGIZATION ("UNCOUPLING") J. Biol. Chem., October 1, 1999; 274(40): 28150 - 28160. [Abstract] [Full Text] [PDF]
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C. Curcio, A. M. Lopes, M. O. Ribeiro, O. A. Francoso Jr., S. D. Carvalho, F. B. Lima, J. E. Bicudo, and A. C. Bianco Development of Compensatory Thermogenesis in Response to Overfeeding in Hypothyroid Rats Endocrinology, August 1, 1999; 140(8): 3438 - 3443. [Abstract] [Full Text]
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D. M. Muoio, G. L. Dohm, E. B. Tapscott, and R. A. Coleman Leptin opposes insulin's effects on fatty acid partitioning in muscles isolated from obese ob/ob mice Am J Physiol Endocrinol Metab, May 1, 1999; 276(5): E913 - E921. [Abstract] [Full Text] [PDF]
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K. D. Chavin, S. Yang, H. Z. Lin, J. Chatham, V. P. Chacko, J. B. Hoek, E. Walajtys-Rode, A. Rashid, C.-H. Chen, C.-C. Huang, et al. Obesity Induces Expression of Uncoupling Protein-2 in Hepatocytes and Promotes Liver ATP Depletion J. Biol. Chem., February 26, 1999; 274(9): 5692 - 5700. [Abstract] [Full Text] [PDF]
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 A. Berger, M. Brand, and S. O'Rahilly Uncoupling proteins: the unravelling of obesity? BMJ, December 12, 1998; 317(7173): 1607 - 1608. [Full Text]
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J.-A. Simoneau, D. E. Kelley, M. Neverova, and C. H. Warden Overexpression of muscle uncoupling protein 2 content in human obesity associates with reduced skeletal muscle lipid utilization FASEB J, December 1, 1998; 12(15): 1739 - 1745. [Abstract] [Full Text]
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B. M. Jucker, J. Ren, S. Dufour, X. Cao, S. F. Previs, K. S. Cadman, and G. I. Shulman 13C/31P NMR Assessment of Mitochondrial Energy Coupling in Skeletal Muscle of Awake Fed and Fasted Rats. RELATIONSHIP WITH UNCOUPLING PROTEIN 3 EXPRESSION J. Biol. Chem., December 8, 2000; 275(50): 39279 - 39286. [Abstract] [Full Text] [PDF]
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A. V. Medvedev, S. K. Snedden, S. Raimbault, D. Ricquier, and S. Collins Transcriptional Regulation of the Mouse Uncoupling Protein-2 Gene. DOUBLE E-BOX MOTIF IS REQUIRED FOR PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR-gamma -DEPENDENT ACTIVATION J. Biol. Chem., March 30, 2001; 276(14): 10817 - 10823. [Abstract] [Full Text] [PDF]
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S. Cadenas, K. S. Echtay, J. A. Harper, M. B. Jekabsons, J. A. Buckingham, E. Grau, A. Abuin, H. Chapman, J. C. Clapham, and M. D. Brand The Basal Proton Conductance of Skeletal Muscle Mitochondria from Transgenic Mice Overexpressing or Lacking Uncoupling Protein-3 J. Biol. Chem., January 18, 2002; 277(4): 2773 - 2778. [Abstract] [Full Text] [PDF]
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