A role for fatty acids and liver fatty acid binding protein in peroxisome proliferation?

1992 ◽  
Vol 20 (4) ◽  
pp. 824-827 ◽  
Author(s):  
Isabelle Issemann ◽  
Rebecca Prince ◽  
Jonathan Tugwood ◽  
Stephen Green
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Peroxisome Proliferation ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Structural and functional interaction of fatty acids with human liver fatty acid-binding protein (L-FABP) T94A variant

FEBS Journal ◽  
2014 ◽  
Vol 281 (9) ◽  
pp. 2266-2283 ◽  
Author(s):  
Huan Huang ◽  
Avery L. McIntosh ◽  
Gregory G. Martin ◽  
Kerstin K. Landrock ◽  
Danilo Landrock ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Human Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Functional Interaction ◽  
Protein L ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Liver Fatty Acid-binding Protein Targets Fatty Acids to the Nucleus

2002 ◽  
Vol 277 (32) ◽  
pp. 29139-29151 ◽  
Author(s):  
Huan Huang ◽  
Olga Starodub ◽  
Avery McIntosh ◽  
Ann B. Kier ◽  
Friedhelm Schroeder
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Protein Targets ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Interaction of LY171883 and other peroxisome proliferators with fatty-acid-binding protein isolated from rat liver

1991 ◽  
Vol 280 (2) ◽  
pp. 387-391 ◽  
Author(s):  
J R Cannon ◽  
P I Eacho
Keyword(s):  
Fatty Acids ◽  
Oleic Acid ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Clofibric Acid ◽  
Peroxisome Proliferation ◽  
Peroxisome Proliferators ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Fatty-acid-binding protein (FABP) is a 14 kDa protein found in hepatic cytosol which binds and transports fatty acids and other hydrophobic ligands throughout the cell. The purpose of this investigation was to determine whether LY171883, a leukotriene D4 antagonist, and other peroxisome proliferators bind to FABP and displace an endogenous fatty acid. [3H]Oleic acid was used to monitor the elution of FABP during chromatographic purification. [14C]LY171883 had a similar elution profile when substituted in the purification, indicating a common interaction with FABP. LY171883 and its structural analogue, LY189585, as well as the hypolipidaemic peroxisome proliferators clofibric acid, ciprofibrate, bezafibrate and WY14,643, displaced [3H]oleic acid binding to FABP. Analogues of LY171883 that do not induce peroxisome proliferation only weakly displaced oleate binding. [3H]Ly171883 bound directly to FABP with a Kd of 10.8 microM, compared with a Kd of 0.96 microM for [3H]oleate. LY171883 binding was inhibited by LY189585, clofibric acid, ciprofibrate and bezafibrate. These findings demonstrate that peroxisome proliferators, presumably due to their structural similarity to fatty acids, are able to bind to FABP and displace an endogenous ligand from its binding site. Interaction of peroxisome proliferators with FABP may be involved in perturbations of fatty acid metabolism caused by these agents as well as in the development of the pleiotropic response of peroxisome proliferation.

Comparisons of the effects of temperature on the liver fatty acid binding proteins from hibernator and nonhibernator mammals

1998 ◽  
Vol 76 (4) ◽  
pp. 593-599 ◽  
Author(s):  
J M Stewart ◽  
T E English ◽  
K B Storey
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Ground Squirrel ◽  
Fatty Acid Binding Protein ◽  
Unsaturated Fatty Acids ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Long Chain

Hibernating mammals rely heavily on lipid metabolism to supply energy during hibernation. We wondered if the fatty acid binding protein from a hibernator responded to temperature differently than that from a nonhibernator. We found that the Kd for oleate of the liver fatty acid binding protein (1.5 micromolar) isolated from ground squirrel (Spermophilus richardsonii) was temperature insensitive over 5-37°C, while the rat liver fatty acid binding protein was affected with the Kd at 37°C being about half (0.8 micromolar) that found at lower temperatures. This same trend was observed when comparing the specificity of various fatty acids of differing chain length and degree of unsaturation for the two proteins at 5 and 37°C. At the lower temperature, ground squirrel protein bound long-chain unsaturated fatty acids, particularly linoleate and linolenate, at least as well as at the higher temperature and matched requirements for these fatty acids in the diet. The most common long-chain fatty acid, palmitate, was a more effective ligand for ground squirrel liver fatty acid binding protein at 5°C than at 37°C, with the opposite occurring in the eutherm. Rat protein was clearly not adapted to function optimally at temperatures lower than the animal's body temperature.Key words: fatty acid binding protein, temperature, hibernation.

Isoforms of Rat Liver Fatty Acid Binding Protein Differ in Structure and Affinity for Fatty Acids and Fatty Acyl CoAs†

Biochemistry ◽  
1997 ◽  
Vol 36 (21) ◽  
pp. 6545-6555 ◽  
Author(s):  
Andrey Frolov ◽  
Tae-Hyeon Cho ◽  
Eric J. Murphy ◽  
Friedhelm Schroeder
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acyl ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein
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