Recombinant human uncoupling protein‐3 increases thermogenesis in yeast cells

Hinz, Willy; Faller, Bernard; Grüninger, S.; Gazzotti, Paolo; Chiesi, Michele

doi:10.1016/s0014-5793(99)00331-2

Cited by 67 publications

(66 citation statements)

References 24 publications

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“…41 In our study, the observed reduction in mitochondria membrane potential after UCP2 gene transfer assessed by spectro¯uorometry could be con®rmed by FCM. A similar decrease was also obtained by FCM in yeast or myoblasts overexpressing UCP2 or UCP3 3,5,7,8,53,54 or even in adipocytes from transgenic mice overexpressing UCP1. 55 Moreover, we observed that GDP addition to mitochondrial preparations did not change mitochondria membrane potential analyzed by FCM, in muscles expressing UCP2 (data not shown), which is in agreement with recent reports.…”

Section: Effect Of Ucp2 Muscle Gene Transfer a Marti Et Alsupporting

confidence: 74%

UCP2 muscle gene transfer modifies mitochondrial membrane potential

et al. 2001

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OBJECTIVE:The aim of this work was to evaluate the effect of uncoupling protein 2 (UCP2) muscle gene transfer on mitochondrial activity. DESIGN: Five week-old male Wistar rats received an intramuscular injection of plasmid pXU1 containing UCP2 cDNA in the right tibialis anterior muscles. Left tibialis anterior muscles were injected with vehicle as control. Ten days after DNA injection, tibialis anterior muscles were dissected and muscle mitochondria isolated and analyzed. RESULTS: There were two mitochondrial populations in the muscle after UCP2 gene transfer, one of low¯uorescence and complexity and the other, showing high¯uorescence and complexity. UCP2 gene transfer resulted in a 3.6 fold increase in muscle UCP2 protein levels compared to control muscles assessed by Western blotting. Furthermore, a signi®cant reduction in mitochondria membrane potential assessed by spectro¯uorometry and¯ow cytometry was observed. The mitochondria membrane potential reduction might account for a decrease in¯uorescence of the low¯uorescence mitochondrial subpopulation. CONCLUSION: It has been demonstrated that UCP2 muscle gene transfer in vivo is associated with a lower mitochondria membrane potential. Our results suggest the potential involvement of UCP2 in uncoupling respiration.

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Section: Effect Of Ucp2 Muscle Gene Transfer a Marti Et Alsupporting

confidence: 74%

UCP2 muscle gene transfer modifies mitochondrial membrane potential

et al. 2001

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“…The present data indicate that UCP2, UCP3, StUCP and AtUCP alter the mitochondrial membrane potential recorded in i o in recombinant yeast and mammalian cells, and probably uncouple respiration [17,30,31,57,[59][60][61]84,85]. The respiration of isolated yeast mitochondria into which UCP2 had been introduced was less coupled than that of control mitochondria [30].…”

Section: Proton Transport Activity Of Ucp2 Ucp3 and Plant Ucps And mentioning

confidence: 57%

The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP

Ricquier¹,

Bouillaud

2000

Biochemical Journal

614

115

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Animal and plant uncoupling protein (UCP) homologues form a subfamily of mitochondrial carriers that are evolutionarily related and possibly derived from a proton\anion transporter ancestor. The brown adipose tissue (BAT) UCP1 has a marked and strongly regulated uncoupling activity, essential to the maintenance of body temperature in small mammals. UCP homologues identified in plants are induced in a cold environment and may be involved in resistance to chilling. The biochemical activities and biological functions of the recently identified mammalian UCP2 and UCP3 are not well known. However, recent data support a role for these UCPs in State 4 respiration, respiration uncoupling and proton leaks in mitochondria. Moreover, genetic studies suggest that UCP2 and UCP3 play a part in

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“…Measurements of UCP2 and UCP3 uncoupling activity. Using heterologous yeast and mammalian cell expression systems, UCP2 and UCP3 have been shown to reduce growth and decrease the mitochondrial membrane potential as measured by uptake of potential-sensitive fluorescent dyes (62, 74,75,87,[91][92][93]. Because qualitatively similar effects have been observed with UCP1 (75,87,94), uncoupling activity for UCP2 and UCP3 was suggested.…”

Section: Uncoupling Acitivity Of Ucp2 and Ucp3mentioning

confidence: 97%

Uncoupling proteins 2 and 3: potential regulators of mitochondrial energy metabolism.

Boss

Hagen²,

Lowell³

2000

Diabetes

393

310

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Mitochondria use energy derived from fuel combustion to create a proton electrochemical gradient across the mitochondrial inner membrane. This intermediate form of energy is then used by ATP synthase to synthesize AT P. Uncoupling protein-1 (UCP1) is a brown fat-specific mitochondrial inner membrane protein with proton transport activity. UCP1 catalyzes a highly regulated proton leak, converting energy stored within the mitochondrial proton electrochemical potential gradient to heat. This uncouples fuel oxidation from conversion of ADP to AT P. In rodents, UCP1 activity and brown fat contribute importantly to whole-body energy expenditure. Recently, two additional mitochondrial carriers with high similarity to UCP1 were molecularly cloned. In contrast to UCP1, UCP2 is expressed widely, and UCP3 is expressed preferentially in skeletal muscle. Biochemical studies indicate that UCP2 and UCP3, like UCP1, have uncoupling activity. While UCP1 is known to play an important role in regulating heat production during cold exposure, the biological functions of UCP2 and UCP3 are unknown. Possible functions include 1) control of adaptive thermogenesis in response to cold exposure and diet, 2) control of reactive oxygen species production by mitochondria, 3) regulation of ATP synthesis, and 4) regulation of fatty acid oxidation. This article will survey present knowledge regarding UCP1, UCP2, and UCP3, and review proposed functions for the two new uncoupling proteins. D i a b e t e s 4 9 :1 4 3-156, 2000 MITOCHONDRIAL RESPIRATION AND THE CHEMIOSMOTIC HYPOTHESISEnergy is released as foods are combusted to carbon dioxide and water. The organism must harness this energy in a useable form, suitable for driving biological work such as muscle contraction, protein synthesis, and ion pumping. This important task is accomplished by mitochondrial oxidative phosphorylation, a step-by-step process in which metabolic fuels and oxygen are converted into carbon dioxide, water, and ATP (Fig. 1). The key challenge for the organism is to regulate these many steps so that rates of ATP production are equal to rates of ATP utilization. This is not a small task given that rates of ATP utilization can quickly increase severalfold (up to 100-fold in muscle during contraction).Fuel metabolism and oxidative phosphorylation consist of many tightly coupled enzymatic reactions (Fig. 1), which are regulated, in part, by ADP availability. Control by ADP is accounted for by the chemiosmotic hypothesis of Mitchell (1). Oxidation of fuels via the electron transport chain generates a proton electrochemical potential gradient ( µ H +) across the mitochondrial inner membrane. Protons reenter the mitochondrial matrix via ATP synthase (F 0 F 1 -ATPase) in a reaction tightly linked to synthesis of ATP from ADP. When cells are inactive and rates of ATP consumption are reduced, ADP should be low. Consequently, proton entry through AT P synthase, which requires ADP, is reduced. Continued activity of the electron transport chain increases µ H +, and the resulting "back...

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Recombinant human uncoupling protein‐3 increases thermogenesis in yeast cells

Cited by 67 publications

References 24 publications

UCP2 muscle gene transfer modifies mitochondrial membrane potential

UCP2 muscle gene transfer modifies mitochondrial membrane potential

The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP

Uncoupling proteins 2 and 3: potential regulators of mitochondrial energy metabolism.

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