Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Uncoupling proteins--how do they work and how are they regulated.

M Klingenberg1

  • 1Institute of Physical Biochemistry, University of Munich, Germany. klingenberg@pbm.med.uni-muenchen.de

IUBMB Life
|January 19, 2002
PubMed
Summary

Uncoupling proteins (UCPs) are mitochondrial transporters. Reconstituted UCPs from E. coli show proton transport, suggesting potential roles beyond thermogenesis.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Clinical impact of a comprehensive nurse-led discharge intervention on patients being discharged home from an acute medical unit: Randomised controlled trial.

International journal of nursing studies·2019
Same author

Multifibre Application in Laser-Induced Interstitial Thermotherapy under On-Line MR Control.

Lasers in medical science·2014
Same author

Uncoupling protein, H+ transport and regulation.

Biochemical Society transactions·2001
Same author

Chimers of two fused ADP/ATP carrier monomers indicate a single channel for ADP/ATP transport.

Archives of biochemistry and biophysics·2001
Same author

Role of intrahelical arginine residues in functional properties of uncoupling protein (UCP1).

Biochemistry·2001
Same author

UCP3 expressed in yeast is primarily localized in extramitochondrial particles.

Biochemical and biophysical research communications·2001

Area of Science:

  • Mitochondrial physiology
  • Molecular biology
  • Biochemistry

Background:

  • Uncoupling proteins (UCPs) are mitochondrial inner membrane transporters.
  • UCP1 is crucial for thermogenesis in brown adipose tissue.
  • The functions of other UCPs (UCP2, UCP3) remain largely undetermined.

Purpose of the Study:

  • To investigate the functional reconstitution and proton transport activity of UCPs expressed in E. coli.
  • To explore potential roles of UCPs beyond thermogenesis.

Main Methods:

  • Expression of UCP1, UCP2, and UCP3 in E. coli as inclusion bodies.
  • Reconstitution of purified UCPs into liposomes.
  • Measurement of proton (H+) transport activity.

Main Results:

  • Reconstituted UCPs (UCP1, UCP2, UCP3) from E. coli exhibited proton transport activity.
  • Proton transport required coenzyme Q (CoQ) and fatty acids, similar to native UCP1.
  • Transport rates were comparable to native UCP1 and sensitive to nucleotide inhibition.
  • Native UCP1 activity is regulated by endogenous CoQ.

Conclusions:

  • Functional proton transport can be reconstituted from bacterial-expressed UCPs.
  • CoQ and fatty acids are essential for UCP activity, suggesting conserved regulatory mechanisms.
  • UCPs may have roles beyond thermogenesis, potentially in immune response or insulin secretion.
  • Differential regulation, possibly via ATP/ADP ratios, may dictate specific cellular functions.

Related Experiment Videos