title: Expression of fatty acyl-CoA binding proteins in colon cells: response to butyrate and transformation.
abstract: Fatty acyl-CoA affect many cellular functions as well as serving as cellular building blocks. Several families of cytosolic fatty acyl-CoA binding proteins may modulate the activities of fatty acyl-CoA. Intestinal enterocytes contain at least three unique families of cytosolic proteins that bind fatty acyl-CoA: acyl-CoA binding protein (ACBP), fatty acid binding proteins (including the liver, L-FABP and intestinal, I-FABP), and sterol carrier protein-2 (SCP-2). Immortalized rat colon epithelial cell lines expressed only ACBP and SCP-2 at levels of 0.75 +/- 0.13 and 0.42 +/- 0.02 ng/microgram protein. Ras and src transformation increased colon cell density and differentially altered ACBP and SCP-2 expression without affecting I-FABP or L-FABP levels. ACBP levels were 1.8-fold and 1.5-fold increased in ras- and src-transformed cells, respectively. In contrast, SCP-2 expression was significantly decreased 55 and 67% in ras- and src-transformed cells, respectively. Butyrate treatment of ras- and src-transformed cells decreased cell proliferation up to 60-85% as compared to 25-30% in control cells. Butyrate treatment decreased ACBP expression in all cell lines but had no effect on the levels of SCP-2, I-FABP, or L-FABP. These studies suggest that the differential expression of ACBP and SCP-2 in rat colonic cell lines, as well as their modulation by butyrate, may be altered by cell transformation.
authors.affiliation: Department of Veterinary Pathobiology, Texas A&M University, TVMC, College Station 77843-4467, USA.
authors.forename: R E
authors.initials: RE
authors.lastname: Gossett
authors.forename: F
authors.initials: F
authors.lastname: Schroeder
authors.forename: J M
authors.initials: JM
authors.lastname: Gunn
authors.forename: A B
authors.initials: AB
authors.lastname: Kier
mesh_terms: D000199:Actins / Q000187:drug effects / Q000378:metabolism; D000818:Animals; D002087:Butyrates / Q000494:pharmacology*; D020148:Butyric Acid; D002352:Carrier Proteins / Q000187:drug effects / Q000378:metabolism*; D002455:Cell Division / Q000187:drug effects / Q000235:genetics; D002461:Cell Line, Transformed; D002471:Cell Transformation, Neoplastic / Q000235:genetics / Q000378:metabolism*; D002478:Cells, Cultured; D003106:Colon / Q000187:drug effects / Q000378:metabolism*; D026261:Diazepam Binding Inhibitor; D004847:Epithelial Cells; D004848:Epithelium / Q000187:drug effects / Q000378:metabolism; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D011905:Genes, ras; D016391:Genes, src; D015151:Immunoblotting; D018996:Myelin P2 Protein / Q000187:drug effects / Q000378:metabolism; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D011817:Rabbits; D051381:Rats
chemical_list: D000199:Actins; D002087:Butyrates; D002352:Carrier Proteins; D026261:Diazepam Binding Inhibitor; C493320:Fabp1 protein, mouse; C493321:Fabp1 protein, rat; C490174:Fabp7 protein, rat; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D018996:Myelin P2 Protein; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; C072087:sterol carrier proteins; D020148:Butyric Acid