title: A complete epithelial organization of Caco-2 cells induces I-FABP and potentializes apolipoprotein gene expression.
abstract: The culture of Caco-2 cells on plastic support impairs the expression of several genes involved in lipid metabolism. We describe culture conditions that permit the expression of the I-FABP gene and better expression of the apolipoprotein A-I, C-III, and A-IV genes. Basal lamina deposited on filters as well as the nature of nutrients on the apical side differentially modulated mRNA expression of I-FABP, APOBEC-1, and apolipoprotein genes. Growing cells on a filter led to functional polarization, illustrated by a secretion of apo B at the basal side, which induced the expression of the I-FABP, APOBEC-1, and apo A-IV genes and highly increased the expression of the apo C-III gene. Moreover, basal lamina deposited on the filter enhances the mRNA expression of apo A-I. Apo C-III and A-IV mRNA levels were decreased when cells were grown on a filter covered with basal lamina in the presence of a medium deprived of protein and lipid on the apical side, whereas these conditions had no effect on I-FABP, apo A-I, and APOBEC-1 mRNA levels. The addition of lipid micelles on the apical side had various effects, according to the genes. Caco-2 cells cultured under the conditions described here closely resembled enterocytes and represent a useful tool for studying the regulation of genes involved in lipid metabolism.
authors.affiliation: INSERM CJF 9508, CNRS URA 1283, Université Pierre et Marie Curie, Paris, France.
authors.forename: J
authors.initials: J
authors.lastname: Le Beyec
authors.forename: F
authors.initials: F
authors.lastname: Delers
authors.forename: F
authors.initials: F
authors.lastname: Jourdant
authors.forename: C
authors.initials: C
authors.lastname: Schreider
authors.forename: J
authors.initials: J
authors.lastname: Chambaz
authors.forename: P
authors.initials: P
authors.lastname: Cardot
authors.forename: M
authors.initials: M
authors.lastname: Pinçon-Raymond
mesh_terms: D000071479:APOBEC-1 Deaminase; D001053:Apolipoproteins / Q000235:genetics*; D001485:Basement Membrane / Q000502:physiology; D001798:Blood Proteins / Q000494:pharmacology; D018938:Caco-2 Cells / Q000166:cytology* / Q000378:metabolism / Q000648:ultrastructure; D002352:Carrier Proteins / Q000235:genetics*; D002454:Cell Differentiation / Q000187:drug effects / Q000502:physiology; D003564:Cytidine Deaminase / Q000235:genetics; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids / Q000235:genetics; D005455:Fluorescent Antibody Technique; D015972:Gene Expression Regulation, Neoplastic / Q000187:drug effects / Q000502:physiology; D006801:Humans; D008055:Lipids / Q000494:pharmacology; D008823:Micelles; D008854:Microscopy, Electron; D018996:Myelin P2 Protein / Q000235:genetics*; D009363:Neoplasm Proteins; D012323:RNA Processing, Post-Transcriptional / Q000235:genetics; D012333:RNA, Messenger / Q000378:metabolism; D025521:Tumor Suppressor Proteins; D000098830:AICDA (Activation-Induced Cytidine Deaminase)
chemical_list: D001053:Apolipoproteins; D001798:Blood Proteins; D002352:Carrier Proteins; C107608:FABP7 protein, human; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D008055:Lipids; D008823:Micelles; D018996:Myelin P2 Protein; D009363:Neoplasm Proteins; D012333:RNA, Messenger; D025521:Tumor Suppressor Proteins; D000098830:AICDA (Activation-Induced Cytidine Deaminase); D000071479:APOBEC-1 Deaminase; C000605089:APOBEC1 protein, human; D003564:Cytidine Deaminase