Study of Enterocyte Fatty acid Binding Proteins specific functions in caco-2 cell model

BOTTASSO ARIAS NM; RODRIGUEZ SAWICKI L; GARCÍA KA; FALOMIR LOCKHART LJ; SCAGLIA N; VES LOSADA, A; STORCH J; CÓRSICO B

Mar del Plata

Congreso; LI Reunión Anual de SAIB; 2015

SAIB

Two isoforms of Fatty Acid Binding Proteins (FABPs) are abundantly expressed within intestinal epithelial cells: liver FABP (LFABP) and intestinal FABP (IFABP). They are associated with intracellular dietary lipid transport and trafficking towards diverse cell fates. But still their functions are not well understood. By means of Caco-2 intestinal cell model, we addressed the matter following two pathways: protein interaction and FABP ablation. Firstly, intestinal FABPs interaction study revealed two candidates for LFABP: HSP60 and calreticulin, by Far Western Blot-MS. IFABP interaction with PPARγ was found by Co-immunoprecipitation. Currently, our efforts are focused on recombinant PPARγ purification to analyze the interaction with IFABP in vitro and studying changes in the expression of PPARγ downstream genes in cultivo, using inhibitors and activators of FABPs and PPARγ, alternatively. Secondly, LFABP ablated Caco-2 cells by mRNA antisense strategy showed interesting modifications in lipid uptake, distribution and secretion. LFABP expression was reduced up to 85% in different cell populations and no compensatory increase in IFABP was observed. Nowadays, we are studying the role of LFABP on membrane phospholipid synthesis and β-oxidation. In summary, our work improves existing knowledge of FABPs functions, enforcing the idea of differential roles for I and LFABP in these cells.