RGD Reference Report - Localization of a portion of the liver isoform of fatty-acid-binding protein (L-FABP) to peroxisomes. - Rat Genome Database

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Localization of a portion of the liver isoform of fatty-acid-binding protein (L-FABP) to peroxisomes.

Authors: Antonenkov, VD  Sormunen, RT  Ohlmeier, S  Amery, L  Fransen, M  Mannaerts, GP  Hiltunen, JK 
Citation: Antonenkov VD, etal., Biochem J. 2006 Mar 1;394(Pt 2):475-84.
RGD ID: 1626442
Pubmed: PMID:16262600   (View Abstract at PubMed)
PMCID: PMC1408678   (View Article at PubMed Central)
DOI: DOI:10.1042/BJ20051058   (Journal Full-text)

The liver isoform of fatty-acid-binding protein (L-FABP) facilitates the cellular uptake, transport and metabolism of fatty acids and is also involved in the regulation of gene expressions and cell differentiation. Consistent with these functions, L-FABP is predominantly present in the cytoplasm and to a lesser extent in the nucleus; however, a significant portion of this protein has also been detected in fractions containing different organelles. More recent observations, notably on L-FABP-deficient mice, indicated a possible direct involvement of L-FABP in the peroxisomal oxidation of long-chain fatty acids. In order to clarify the links between L-FABP and peroxisomal lipid metabolism, we reinvestigated the subcellular distribution of the protein. Analytical subcellular fractionation by a method preserving the intactness of isolated peroxisomes, two-dimensional gel electrophoresis of peroxisomal matrix proteins combined with MS analysis, and immunoelectron microscopy of liver sections demonstrate the presence of L-FABP in the matrix of peroxisomes as a soluble protein. Peroxisomal L-FABP was highly inducible by clofibrate. The induction of L-FABP was accompanied by a marked increase in the binding capacity of peroxisomal matrix proteins for oleic acid and cis-parinaric acid. The peroxisomal beta-oxidation of palmitoyl-CoA and acyl-CoA thioesterase activity were stimulated by L-FABP, indicating that the protein modulates the function of peroxisomal lipid-metabolizing enzymes. The possible role of intraperoxisomal L-FABP in lipid metabolism is discussed.

Gene Ontology Annotations    

Biological Process

Cellular Component

Objects Annotated

Genes (Rattus norvegicus)
Fabp1  (fatty acid binding protein 1)

Additional Information