Recombinant liver fatty acid binding protein interacts with fatty acyl-coenzyme A
| Autor: | Friedhelm Schroeder, Timothy Hubbell, William D. Behnke, Judith K. Woodford |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Phosphatidic Acids
Nerve Tissue Proteins Fatty Acid-Binding Proteins Biochemistry Fatty acid-binding protein chemistry.chemical_compound Acyl-CoA Escherichia coli adipocyte protein 2 Chromatography High Pressure Liquid Fluorescent Dyes chemistry.chemical_classification biology Binding protein Fatty acid Phosphatidic acid Recombinant Proteins Neoplasm Proteins Intestines Fatty acid synthase Spectrometry Fluorescence chemistry Liver biology.protein Free fatty acid receptor Microsomes Liver lipids (amino acids peptides and proteins) Acyl Coenzyme A Carrier Proteins Fatty Acid-Binding Protein 7 |
| Zdroj: | Biochemistry. 33(11) |
| ISSN: | 0006-2960 |
| Popis: | Rat liver fatty acid binding protein (L-FABP) and rat intestine fatty acid binding protein (I-FABP) are homologous proteins which are both found in intestinal epithelial cells. It was once well accepted that liver fatty acid binding protein bound fatty acyl-CoAs, but the recent finding of a novel acyl-CoA binding protein (ACBP) in preparations of L-FABP has challenged the role of FABPs in acyl-CoA metabolism. Prior to the discovery of ACBP, L-FABP preparations from liver were shown to modulate the rate of fatty acyl-CoA synthesis (Burrier et al., 1987) and their conversion to phospholipids (Bordewick et al., 1989). Studies using FABPs free of ACBP are needed to determine the role of I-FABP and L-FABP in fatty acyl-CoA metabolism. In this study, highly pure recombinant L-FABP and I-FABP were used first to establish binding to fatty acyl-CoAs and then to examine the effects of these FABPs on microsomal phosphatidic acid synthesis. The standard Lipidex-1000 binding assay using [14C]oleoyl-CoA and a new fluorescence binding assay using the fluorescent fatty acyl-CoA cis-parinaroyl-CoA were used to determine binding. The results of these assays indicate that L-FABP binds fatty acyl-CoAs at two sites with a high-affinity Kd = 3-14 microM. These binding assays showed that I-FABP has a much lower affinity for fatty acyl-CoAs than does L-FABP. Furthermore, in vitro only L-FABP significantly increases the rate of incorporation of oleoyl-CoA into lysophosphatidic acid and phosphatidic acid. |
| Databáze: | OpenAIRE |
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