Journal of Nutrition OpenSOurce Diets- www.ResearchDiets.com

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Knudsen, J.
Right arrow Articles by Hansen, J. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Knudsen, J.
Right arrow Articles by Hansen, J. K.
(Journal of Nutrition. 2000;130:294S-298S.)
© 2000 The American Society for Nutritional Sciences


Supplement

Role of Acyl-CoA Binding Protein in Acyl-CoA Metabolism and Acyl-CoA–Mediated Cell Signaling1 ,2

Jens Knudsen3, Thomas B. F. Neergaard, Barbara Gaigg, Mette Valentin Jensen and Jan Krogh Hansen

Institute of Biochemistry, Odense University, DK-5230 Odense M Denmark

3To whom correspondence should be addressed.

Long-chain acyl-CoA esters (LCA) act both as substrates and intermediates in metabolism and as regulators of various intracellular functions. Acyl-CoA binding protein (ACBP) binds LCA with high affinity and is believed to play an important role in intracellular acyl-CoA transport and pool formation and therefore also for the function of LCA as metabolites and regulators of cellular functions . The free concentration of cytosolic LCA is efficiently buffered to low nanomole concentration by ACBP and fatty acid binding protein (FABP). An additional important factor is the activity of acyl-CoA hydrolases. The estimated cellular free LCA concentration is two to four orders of magnitude lower than the concentrations reported to be necessary to regulate most LCA-affected cellular functions. Preliminary evidence indicates that the regulatory effect of LCA might be mediated by the LCA/ACBP complex.


KEY WORDS: • acyl-CoA • fatty acids • metabolism • cell signaling




This article has been cited by other articles:


Home page
EndocrinologyHome page
S. Yamada, M. Komatsu, Y. Sato, K. Yamauchi, T. Aizawa, and I. Kojima
Nutrient Modulation of Palmitoylated 24-Kilodalton Protein in Rat Pancreatic Islets
Endocrinology, December 1, 2003; 144(12): 5232 - 5241.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Dai, H. Zhu, J. Shi, and G. Woldegiorgis
Identification by Mutagenesis of Conserved Arginine and Tryptophan Residues in Rat Liver Carnitine Palmitoyltransferase I Important for Catalytic Activity
J. Biol. Chem., July 14, 2000; 275(29): 22020 - 22024.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2000 by American Society for Nutrition