Modulation of intestinal and liver fatty acid-binding proteins in Caco-2 cells by lipids, hormones and cytokines

✍ Scribed by Nadia Dubé; Edgard Delvin; Wagner Yotov; Carole Garofalo; Moise Bendayan; Jacques H. Veerkamp; Dr. Emile Levy

• Publisher: John Wiley and Sons
• Year: 2001
• Tongue: English
• Weight: 236 KB
• Volume: 81
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.1090

✦ Synopsis

Abstract

Intestinal and liver fatty acid binding proteins (I‐ and L‐FABP) are thought to play a role in enterocyte fatty acid (FA) trafficking. Their modulation by cell differentiation and various potential effectors was investigated in the human Caco‐2 cell line. With the acquisition of enterocytic features, Caco‐2 cells seeded on plastic progressively increased L‐FABP quantities, whereas I‐FABP was not detectable even very late in the maturation process. On permeable filters that improved differentiation markers (sucrase, alkaline phosphatase, transepithelial resistance), Caco‐2 cells furthered their L‐FABP content and expressed I‐FABP. Western blot analysis showed a significant increase in I‐ and L‐FABP expression following an 8‐hour incubation period with butyric acid, oleic acid, and phosphatidylcholine. However, in all cases, I‐FABP levels were higher than L‐FABP concentrations regardless of the lipid substrates added. Similarly, hydrocortisone and insulin enhanced the cellular content of I‐ and L‐FABP whereas leptin triggered I‐FABP expression only after an 8‐hour incubation. Finally, tumor necrosis factor‐α was more effective in increasing the cytosolic amount of I‐FABP levels. In conclusion, our data demonstrate that I‐FABP expression is limited to fully differentiated Caco‐2 cells and can be more easily regulated than L‐FABP by lipids, hormones, and cytokines. J. Cell. Biochem. 81: 613–620, 2001. © 2001 Wiley‐Liss, Inc.