title: Intestinal fatty acid binding protein (fabp2) in Atlantic salmon (Salmo salar): Localization and alteration of expression during development of diet induced enteritis.
abstract: In the present study full-length cDNAs corresponding to three isoforms of intestinal fatty acid binding protein (fabp2) in Atlantic salmon were cloned and characterized. Gene expression of fabp2 was observed in all tissues investigated, although differences were observed between isoforms. The highest fabp2a1, fabp2a2, and fabp2b expression was in the intestine. A 15kDa protein, corresponding to putative Fabp2 protein, was identified by immunoblotting using anti-human Fabp2 antibody. Immunoblotting and immunohistochemistry confirmed that Fabp2 protein was present in most Atlantic salmon tissues. Similar to gene expression, intestinal tissues had the highest Fabp2 protein levels, decreasing gradually from proximal to distal intestine. During development of distal intestinal inflammation caused by dietary soybean meal from 0 to 21days, Fabp2 decreased significantly on both transcriptional and protein levels. The reduction in Fabp2 was preceded by a down regulation of peroxisome proliferator activated receptor (ppar) alpha and gamma, fabp2's presumed regulatory proteins, and followed by a progressive increase in proliferating cell nuclear antigen (Pcna) staining. Results illustrate that the early decline of distal intestinal fabp2 was likely caused by a down regulation of their regulatory proteins, but at later time points reduced Fabp2 may largely be due to a less mature enterocyte population resulting from rapid cell turnover.
authors.affiliation: Department of Basic Sciences and Aquatic Medicine, Norwegian School of Veterinary Science, P.O. Box 8146 Dep, NO-0033 Oslo, Norway. Fredrikfollesdal.venold@nvh.no
authors.forename: Fredrik F
authors.initials: FF
authors.lastname: Venold
authors.forename: Michael H
authors.initials: MH
authors.lastname: Penn
authors.forename: Jim
authors.initials: J
authors.lastname: Thorsen
authors.forename: Jinni
authors.initials: J
authors.lastname: Gu
authors.forename: Trond M
authors.initials: TM
authors.lastname: Kortner
authors.forename: Ashild
authors.initials: A
authors.lastname: Krogdahl
authors.forename: Anne Marie
authors.initials: AM
authors.lastname: Bakke
mesh_terms: D000818:Animals; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics / Q000378:metabolism; D004032:Diet / Q000009:adverse effects; D004751:Enteritis / Q000139:chemically induced* / Q000378:metabolism / Q000473:pathology; D050556:Fatty Acid-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D029941:Fish Proteins / Q000235:genetics / Q000378:metabolism*; D005786:Gene Expression Regulation; D015151:Immunoblotting; D007150:Immunohistochemistry; D007413:Intestinal Mucosa / Q000378:metabolism; D007422:Intestines / Q000473:pathology; D047493:PPAR alpha / Q000235:genetics / Q000378:metabolism; D018809:Proliferating Cell Nuclear Antigen / Q000235:genetics / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D020317:Salmo salar / Q000235:genetics / Q000378:metabolism*; D013025:Glycine max / Q000009:adverse effects*; D013997:Time Factors; D014158:Transcription, Genetic
chemical_list: D018076:DNA, Complementary; D050556:Fatty Acid-Binding Proteins; D029941:Fish Proteins; D047493:PPAR alpha; D018809:Proliferating Cell Nuclear Antigen; D020033:Protein Isoforms