Titration and Exchange Studies of Liver Fatty Acid-Binding Protein with13C-Labeled Long-Chain Fatty Acids†

Biochemistry ◽  
2002 ◽  
Vol 41 (17) ◽  
pp. 5453-5461 ◽  
Author(s):  
Hsin Wang ◽  
Yan He ◽  
Christopher D. Kroenke ◽  
Sarala Kodukula ◽  
Judith Storch ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Long Chain Fatty Acids ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Long Chain ◽  
Chain Fatty Acids

scholarly journals Up-regulation of the expression of the gene for liver fatty acid-binding protein by long-chain fatty acids

1996 ◽  
Vol 319 (2) ◽  
pp. 483-487 ◽  
Author(s):  
Claire MEUNIER-DURMORT ◽  
Hélène POIRIER ◽  
Isabelle NIOT ◽  
Claude FOREST ◽  
Philippe BESNARD
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Fold Increase ◽  
Long Chain Fatty Acids ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Fabp Gene ◽  
Long Chain

The role of fatty acids in the expression of the gene for liver fatty acid-binding protein (L-FABP) was investigated in the well-differentiated FAO rat hepatoma cell line. Cells were maintained in serum-free medium containing 40 µM BSA/320 µM oleate. Western blot analysis showed that oleate triggered an approx. 4-fold increase in the cytosolic L-FABP level in 16 h. Oleate specifically stimulated L-FABP mRNA in time-dependent and dose-dependent manners with a maximum 7-fold increase at 16 h in FAO cells. Preincubation of FAO cells with cycloheximide prevented the oleate-mediated induction of L-FABP mRNA, showing that protein synthesis was required for the action of fatty acids. Run-on transcription assays demonstrated that the control of L-FABP gene expression by oleate was, at least in part, transcriptional. Palmitic acid, oleic acid, linoleic acid, linolenic acid and arachidonic acid were similarly potent whereas octanoic acid was inefficient. This regulation was also found in normal hepatocytes. Therefore long-chain fatty acids are strong inducers of L-FABP gene expression. FAO cells constitute a useful tool for studying the underlying mechanism of fatty acid action.

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.

Cytosolic fatty acid binding protein enhances rat hepatocyte [3H]palmitate uptake

1999 ◽  
Vol 77 (11) ◽  
pp. 896-901 ◽  
Author(s):  
F J Burczynski ◽  
S Fandrey ◽  
G Wang ◽  
P A Pavletic ◽  
Y Gong
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Long Chain Fatty Acids ◽  
Clearance Rates ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Palmitate Uptake ◽  
Long Chain

Liver cytosolic fatty acid binding protein (FABP) represents the intracellular equivalent to extracellular serum albumin, participating in the intracellular transport of long-chain fatty acids. In this study we observed the effect of increasing and decreasing FABP levels on hepatocyte [3H]palmitate uptake in male Sprague-Dawley rats. We also were interested to determine whether uptake, from either the unbound or unbound and protein-bound fractions, was fundamentally different at the different FABP levels. FABP levels were modified by hypophysectomy and clofibrate treatment (50 mg/100 g body weight for 10 days). Results showed that the [3H]palmitate clearance rates paralleled the 54% decrease and 73% increase in FABP levels in hypophysectomy and clofibrate-treated animals, respectively. In the presence of 2 and 20 µM albumin, hepatocyte clearance rates of unbound [3H]palmitate from hypophysectomized animals (0.16 ± 0.01 and 0.64 ± 0.01 mL·s-1·10-6 cells, respectively) were significantly lower (p < 0.01) than those of the sham group (0.30 ± 0.02 and 1.00 ± 0.06 mL·s-1·10-6 cells, respectively). However, the unbound [3H]palmitate clearance rates from the clofibrate-treated group (0.39 ± 0.04 and 1.18 ± 0.12 mL·s-1·10-6 cells) were significantly higher (p < 0.01) than the control group (0.29 ± 0.02 and 0.81 ± 0.05 mL·s-1·10-6 cells) for 2 and 20 µM albumin, respectively. To investigate whether uptake was fundamentally different between the hypophysectomized and clofibrate-treated groups, we expressed the clearance rates as enhancement factors, i.e., EF = CL20µM/CL2µM. No statistical difference was observed between EF of the hypophsectomized (3.8 ± 0.4) and EF of the clofibrate-treated (3.1 ± 0.3) groups, suggesting that the extracted ligand originated from similar fractions.Key words: palmitic acid, albumin, growth hormone, liver, fatty acid binding protein, uptake, hepatic, long-chain fatty acids, clofibrate, hypophysectomy.

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 Constitutive expression of a saturable transport system for non-esterified fatty acids in Xenopus laevis oocytes

1994 ◽  
Vol 297 (2) ◽  
pp. 315-319 ◽  
Author(s):  
S L Zhou ◽  
D Stump ◽  
L Isola ◽  
P D Berk
Keyword(s):  
Fatty Acids ◽  
Plasma Membrane ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Xenopus Laevis Oocytes ◽  
Long Chain Fatty Acids ◽  
Membrane Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Long Chain

In the presence of 150 microM BSA, uptake of [3H]oleate by Xenopus laevis oocytes was a saturable function of the unbound oleate concentration (Vmax. 110 +/- 4 pmol/h per oocyte; Km 193 +/- 11 nM unbound oleate). Oleate uptake was three orders of magnitude faster than that of another test substance, [35S]bromosulphophthalein, and was competitively inhibited by 55 nM unbound palmitate (Vmax. 111 +/- 14 pmol/h per oocyte; Km 424 +/- 63 nM unbound oleate) (P < 0.01). Oleate uptake was also inhibited by antibodies to a 43 kDa rat liver plasma-membrane fatty acid-binding protein, a putative transporter of long-chain fatty acids in mammalian cells; uptake of the medium-chain fatty acid [14C]octanoate was unaffected. Immunofluorescence and immunoblotting demonstrated that the antiserum reacted with a single 43 kDa protein on the oocyte surface. Hence a protein related to the mammalian plasma-membrane fatty acid-binding protein may play a role in saturable uptake of long-chain fatty acids by Xenopus oocytes.

Sign in / Sign up

Export Citation Format

Share Document