| Lipid specificity and location of the sterol carrier protein-2 fatty acid-binding site: a fluorescence displacement and energy transfer study. | |
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MedLine Citation:
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PMID: 9397406 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Although it was recently recognized that sterol carrier protein-2 (SCP-2) interacts with fatty acids, little is known regarding the specificity of SCP-2 for long-chain fatty acids or branched-chain fatty-acid-like molecules. Likewise the location of the fatty-acid binding site within SCP-2 is unresolved. A fluorescent cis-parinaric acid displacement assay was used to show that SCP-2 optimally interacted with 14-22 carbon chain lipidic molecules: polyunsaturated fatty acids > monounsaturated, saturated > branched-chain isoprenoids > branched-chain phytol-derived fatty acids. In contrast, the other major fatty-acid binding protein in liver, fatty-acid binding protein (L-FABP), displayed a much narrower carbon chain preference in general: polyunsaturated fatty acids > branched-chain phytol-derived fatty acids > 14- and 16-carbon saturated > branched-chain isoprenoids. However, both SCP-2 and L-FABP displayed a very similar unsaturated fatty-acid specificity profile. The presence and location of the SCP-2 lipid binding site were investigated by fluorescence energy transfer. The distance between the SCP-2 Trp50 and bound cis-parinaric acid was determined to be 40 A. Thus, the SCP-2 fatty-acid binding site appeared to be located on the opposite side of the SCP-2 Trp50. These findings not only contribute to our understanding of the SCP-2 ligand binding site but also provide evidence suggesting a potential role for SCP-2 and/or L-FABP in metabolism of branched-chain fatty acids and isoprenoids. |
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Authors:
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A Frolov; K Miller; J T Billheimer; T H Cho; F Schroeder |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Lipids Volume: 32 ISSN: 0024-4201 ISO Abbreviation: Lipids Publication Date: 1997 Nov |
Date Detail:
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Created Date: 1998-01-13 Completed Date: 1998-01-13 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0060450 Medline TA: Lipids Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 1201-9 Citation Subset: IM |
Affiliation:
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Department of Physiology and Pharmacology, Texas A&M University, TVMC, College Station 77843-4466, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Binding Sites Carrier Proteins / metabolism* Energy Transfer* Fatty Acid-Binding Proteins Fatty Acids / metabolism* Fatty Acids, Unsaturated / metabolism Fluorescent Dyes* Humans Lipid Metabolism* Myelin P2 Protein / metabolism Neoplasm Proteins* Nerve Tissue Proteins* Plant Proteins* Rats Recombinant Proteins Spectrometry, Fluorescence Tumor Suppressor Proteins* |
| Grant Support | |
ID/Acronym/Agency:
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DK41402/DK/NIDDK NIH HHS; GM31651/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Carrier Proteins; 0/FABP1 protein, human; 0/FABP7 protein, human; 0/Fabp1 protein, mouse; 0/Fabp1 protein, rat; 0/Fabp7 protein, rat; 0/Fatty Acid-Binding Proteins; 0/Fatty Acids; 0/Fatty Acids, Unsaturated; 0/Fluorescent Dyes; 0/Myelin P2 Protein; 0/Neoplasm Proteins; 0/Nerve Tissue Proteins; 0/Plant Proteins; 0/Recombinant Proteins; 0/Tumor Suppressor Proteins; 0/sterol carrier proteins; 18427-44-6/parinaric acid |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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