Enterocyte fatty acid uptake and intestinal fatty acid-binding protein

2004 ◽  
Vol 32 (1) ◽  
pp. 75-78 ◽  
Author(s):  
P. Tso ◽  
A. Nauli ◽  
C.-M. Lo
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Brush Border Membrane ◽  
Fatty Acid Uptake ◽  
Current Understanding ◽  
Fatty Acid Binding Proteins ◽  
Acid Uptake ◽  
Micellar Solubilization ◽  
Fatty Acid Binding

This article reviews our current understanding of the uptake of fatty acids by the enterocytes of the intestine. The micellar solubilization of fatty acids by bile salts and the factors regulating that process are discussed. The mechanism of how micellar solubilization of fatty acids promotes the uptake of fatty acids by enterocytes and their relative importance is reviewed. Additionally, discussion of the various fatty acid transporters located at the brush border membrane of the enterocytes is included. Finally, a summary of our current understanding of the function of fatty-acid-binding proteins inside enterocytes is provided.

Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8

2021 ◽  
Author(s):  
Kelli L. Sylvers-Davie ◽  
Brandon S.J. Davies
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Metabolism ◽  
Fatty Acid Uptake ◽  
Extracellular Proteins ◽  
Current Understanding ◽  
Acid Uptake ◽  
Lipoprotein Lipase Activity

Triglyceride-rich lipoproteins deliver fatty acids to tissues for oxidation and for storage. Release of fatty acids from circulating lipoprotein triglycerides is carried out by lipoprotein lipase (LPL), thus LPL serves as a critical gatekeeper of fatty acid uptake into tissues. LPL activity is regulated by a number of extracellular proteins including three members of the angiopoietin-like family of proteins. In this review we discuss our current understanding of how, where, and when ANGPTL3, ANGPTL4, and ANGPTL8 regulate lipoprotein lipase activity, with a particular emphasis on how these proteins interact with each other to coordinate triglyceride metabolism and fat partitioning.

scholarly journals L-FABP and I-FABP expression increase NBD-stearate uptake and cytoplasmic diffusion in L cells

1998 ◽  
Vol 275 (2) ◽  
pp. G244-G249 ◽  
Author(s):  
Eric J. Murphy
Keyword(s):  
Fatty Acid ◽  
Single Cell ◽  
Lipid Droplets ◽  
Fatty Acid Binding Protein ◽  
Diffusion Rate ◽  
Single Cells ◽  
Fatty Acid Uptake ◽  
Acid Uptake ◽  
Intact Cells ◽  
Fatty Acid Binding

The effects of intestinal and liver fatty acid binding protein (I- and L-FABP, respectively) expression on single-cell fatty acid uptake, internalization, and cytoplasmic diffusion were determined in transfected L cell fibroblasts. These parameters were measured using the nonesterifiable fluorescent fatty acid probe 12- N-methyl-(7-nitrobenz-2-oxa-1,3-diazol)aminostearate (NBD-stearate) and fluorescence digital imaging. In single-cell fluorescence imaging experiments, L-FABP-expressing cells, but not I-FABP-expressing cells, increased NBD-stearate uptake 1.7-fold compared with control cells. Both I- and L-FABP increased the cytoplasmic diffusion rate of the internalized NBD-stearate 2.6- and 1.9-fold, respectively, compared with control cells. However, increased NBD-stearate lateral membrane mobility was observed only in L-FABP-expressing cells. After incubation of the cells with 4 μM NBD-stearate at 37°C for 30 min, fluorescence deconvolution imaging indicated that NBD-stearate was localized primarily into lipid droplets in all cell lines. The differential effect of these proteins on fatty acid uptake and intracellular trafficking in single cells illustrates a possible difference in the physiological function of I- and L-FABP in intact cells.

scholarly journals Transfection of L6 myoblasts with adipocyte fatty acid-binding protein cDNA does not affect fatty acid uptake but disturbs lipid metabolism and fusion

1998 ◽  
Vol 329 (2) ◽  
pp. 265-273 ◽  
Author(s):  
F. M. Clemens PRINSEN ◽  
H. Jacques VEERKAMP
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Metabolism ◽  
Fatty Acid Binding Protein ◽  
Acid Metabolism ◽  
Binding Protein ◽  
Fatty Acid Uptake ◽  
Acid Uptake ◽  
Fatty Acid Binding ◽  
Transfected Cells ◽  
Acid Binding Protein

We studied the involvement of fatty acid-binding protein (FABP) in growth, differentiation and fatty acid metabolism of muscle cells by lipofection of rat L6 myoblasts with rat heart (H) FABP cDNA or with rat adipocyte (A) FABP cDNA in a eukaryotic expression vector which contained a puromycin acetyltransferase cassette. Stable transfectants showed integration into the genome for all constructs and type-specific overexpression at the mRNA and protein level for the clones with H-FABP and A-FABP cDNA constructs. The rate of proliferation of myoblasts transfected with rat A-FABP cDNA was 2-fold higher compared with all other transfected cells. In addition, these myoblasts showed disturbed fusion and differentiation, as assessed by morphological examination and creatine kinase activity. Uptake rates of palmitate were equal for all clone types, in spite of different FABP content and composition. Palmitate oxidation over a 3 h period was similar in all clones from growth medium. After being cultured in differentiation medium, mock- and H-FABP-cDNA-transfected cells showed a lower fatty acid-oxidation rate, in contrast with A-FABP-cDNA-transfected clones. The ratio of [14C]palmitic acid incorporation into phosphatidylcholine and phosphatidylethanolamine of A-FABP-cDNA-transfected clones changed in the opposite direction in differentiation medium from that of mock- and H-FABP-cDNA-transfected clones. In conclusion, transfection of L6 myoblasts with A-FABP cDNA does not affect H-FABP content and fatty acid uptake, but changes fatty acid metabolism. The latter changes may be related to the observed fusion defect.

scholarly journals Heart Fatty Acid Uptake Is Decreased in Heart Fatty Acid-binding Protein Gene-ablated Mice

2004 ◽  
Vol 279 (33) ◽  
pp. 34481-34488 ◽  
Author(s):  
Eric J. Murphy ◽  
Gwendolyn Barcelo-Coblijn ◽  
Bert Binas ◽  
Jan F. C. Glatz
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Protein Gene ◽  
Binding Protein ◽  
Fatty Acid Uptake ◽  
Acid Uptake ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Binding Protein Gene
Sign in / Sign up

Export Citation Format

Share Document