Loss of intracellular lipid binding proteins differentially impacts saturated fatty acid uptake and nuclear targeting in mouse hepatocytes.
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Research Areas
- Ethics and Fundamental Issues of Law and Justice (Fundamental Issues and Purpose of Human Life)
- Evolution of Thought (Fundamental Issues and Purpose of Human Life)
- Humanities (Human and social sciences)
- Language, Knowledge, Significance and Thought Building (Fundamental Issues and Purpose of Human Life)
- Ontological and Metaphysical Matters (Fundamental Issues and Purpose of Human Life)
- Social Relations and Structures (Human and social sciences)
Publication Details
Output type: Journal article
Author list: Storey, McIntosh, Huang, Martin, Landrock, Landrock, Payne, Kier, Schroeder
Publication year: 2012
Journal acronym: Am J Physiol Gastrointest Liver Physiol
Volume number: 303
Issue number: 7
Start page: G837
End page: 50
ISSN: 1522-1547
eISSN: 1522-1547
Languages: English-Great Britain (EN-GB)
Unpaywall Data
Open access status: green
Full text URL: https://europepmc.org/articles/pmc3469595
Abstract
The liver expresses high levels of two proteins with high affinity for long-chain fatty acids (LCFAs): liver fatty acid binding protein (L-FABP) and sterol carrier protein-2 (SCP-2). Real-time confocal microscopy of cultured primary hepatocytes from gene-ablated (L-FABP, SCP-2/SCP-x, and L-FABP/SCP-2/SCP-x null) mice showed that the loss of L-FABP reduced cellular uptake of 12-N-methyl-(7-nitrobenz-2-oxa-1,3-diazo)-aminostearic acid (a fluorescent-saturated LCFA analog) by ∼50%. Importantly, nuclear targeting of the LCFA was enhanced when L-FABP was upregulated (SCP-2/SCP-x null) but was significantly reduced when L-FABP was ablated (L-FABP null), thus impacting LCFA nuclear targeting. These effects were not associated with a net decrease in expression of key membrane proteins involved in LCFA or glucose transport. Since hepatic LCFA uptake and metabolism are closely linked to glucose uptake, the effect of glucose on L-FABP-mediated LCFA uptake and nuclear targeting was examined. Increasing concentrations of glucose decreased cellular LCFA uptake and even more extensively decreased LCFA nuclear targeting. Loss of L-FABP exacerbated the decrease in LCFA nuclear targeting, while loss of SCP-2 reduced the glucose effect, resulting in enhanced LCFA nuclear targeting compared with control. Simply, ablation of L-FABP decreases LCFA uptake and even more extensively decreases its nuclear targeting.
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