spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Summary Freely available
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Related articles in JEB
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schrauwen, P.
Right arrow Articles by Hesselink, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schrauwen, P.
Right arrow Articles by Hesselink, M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

UCP2 and UCP3 in muscle controlling body metabolism

Patrick Schrauwen1,* and Matthijs Hesselink2

Nutrition and Toxicology Research Institute Maastricht (NUTRIM)
1 Department of Human Biology, Maastricht University, The Netherlands
2 Department of Movement Sciences, Maastricht University, The Netherlands
* Present address: Department of Human Biology, Maastricht University, PO Box 616, 6200 MD Maastricht, The Netherlands



View larger version (25K):

[in a new window]
  		Fig. 1. Action of the electron transport chain leading to the build-up of a proton gradient across the inner mitochondrial membrane. Protons can cross the inner mitochondrial membrane via the F0F1 complex, thereby providing energy for the conversion of ADP to ATP. Alternatively, the proton gradient can be reduced by uncoupling proteins (UCP), either by direct transport of protons from the intermembrane space to the matrix or by transport of fatty acid anions in the opposite direction. Cyt c, cytochrome c. Q, coenzyme Q.

 


View larger version (18K):

[in a new window]
  		Fig. 2. Hypothesis for the function of uncoupling protein-3 (UCP3): fatty acid anions are transported out of the mitochondrial matrix to prevent accumulation of fatty acid anions inside the matrix (Schrauwen et al., 2001cGo). FA, fatty acid; CoA, coenzyme A; FAS, fatty acyl-CoA synthetase; CPT1, carnitine palmitoyl transferase-1; CPT2, carnitine palmitoyl transferase-2; {Delta}H+, proton gradient.

 

Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?



© The Company of Biologists Ltd 2002