Intestinal-fatty acid binding protein and lipid transport in human intestinal epithelial cells
Autor: | Emile Levy, Dominic Jean, Edgard Delvin, D. Menard, Eric Tremblay, Moise Bendayan, Jean-François Beaulieu, Alain Montoudis |
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Rok vydání: | 2006 |
Předmět: |
Very low-density lipoprotein
Cell Survival Enterocyte Lipoproteins Biophysics Biology Fatty Acid-Binding Proteins Biochemistry Cytosol medicine Humans Intestinal Mucosa Microscopy Immunoelectron Molecular Biology Cells Cultured Phospholipids Triglycerides Cell Proliferation Cell growth Binding protein Biological Transport Epithelial Cells Lipid metabolism Cell Biology Transfection Lipid Metabolism Molecular biology Apolipoproteins medicine.anatomical_structure lipids (amino acids peptides and proteins) Cholesterol Esters Lipoprotein Chylomicron |
Zdroj: | Biochemical and Biophysical Research Communications. 339:248-254 |
ISSN: | 0006-291X |
Popis: | Intestinal-fatty acid binding protein (I-FABP) is a 14-15 kDa cytoplasmic molecule highly expressed in the enterocyte. Although different functions have been proposed for various FABP family members, the specific function of I-FABP in human intestine remains unclear. Here, we studied the role of I-FABP in molecularly modified normal human intestinal epithelial cells (HIEC-6). cDNA transfection resulted in 90-fold I-FABP overexpression compared to cells treated with empty pQCXIP vector. The high-resolution immunogold technique revealed labeling mainly in the cytosol and confirmed the marked phenotype abundance of I-FABP in cDNA transfected cells. I-FABP overexpression was not associated with alterations in cell proliferation and viability. Studies using these transfected cells cultured with [14C]oleic acid did not reveal higher efficiency in de novo synthesis or secretion of triglycerides, phospholipids, and cholesteryl esters compared to cells treated with empty pQCXIP vector only. Similarly, the incubation with [35S]methionine did not disclose a superiority in the biogenesis of apolipoproteins (apo) A-I, A-IV, B-48, and B-100. Finally, cells transfected with I-FABP did not exhibit an increased production of chylomicrons, VLDL, LDL, and HDL. Our observations establish that I-FABP overexpression in normal HIEC-6 is not related to cell proliferation, lipid esterification, apo synthesis, and lipoprotein assembly, and, therefore, exclude its role in intestinal fat transport. |
Databáze: | OpenAIRE |
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