Evidence map›Paper›PMID 19289416›Full record

ArticleJournal of lipid research2009

L-FABP directly interacts with PPARalpha in cultured primary hepatocytes.

Heather A Hostetler, Avery L McIntosh, Barbara P Atshaves, Stephen M Storey, H Ross Payne, Ann B Kier, Friedhelm Schroeder

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
3.4field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

93 citing papers in PubMed, 147 citations in OpenAlex.

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33 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Heather A HostetlerDepartment of Physiology and Pharmacology, Texas A&M University, College of Veterinary Medicine and Biomedical Sciences, College Station, TX 77843, USA.
Avery L McIntosh
Barbara P Atshaves
Stephen M Storey
H Ross Payne
Ann B Kier
Friedhelm Schroeder
Texas A&M University · US

Funding

FATTY ACID BINDING PROTEINS-LIGAND SPECIFICITYR01DK041402 · NIDDK · UNIVERSITY OF CINCINNATI · PI SCHROEDER, FRIEDHELM · 1989 to 2010
$4.4M
The role of long chain acyl-CoAs in nuclear receptor regulationR00DK077573 · NIDDK · WRIGHT STATE UNIVERSITY · PI HOSTETLER, HEATHER A · 2009 to 2011
$747k
The role of long chain acyl-CoAs in nuclear receptor regulationK99DK077573 · NIDDK · TEXAS A&M AGRILIFE RESEARCH · PI HOSTETLER, HEATHER A · 2007 to 2008
$179k
Intracellular trafficking of long chain fatty acyl-CoAsF32DK066732 · NIDDK · TEXAS A&M UNIVERSITY SYSTEM · PI HOSTETLER, HEATHER A · 2004 to 2006
$142k
NIDDK NIH HHS DK-066732NIDDK NIH HHS DK-41402NIDDK NIH HHS DK-77573NIDDK NIH HHS F32 DK066732NIDDK NIH HHS K99 DK077573NIDDK NIH HHS R00 DK077573NIDDK NIH HHS R01 DK041402
6 · The paper itself

Abstract

Although studies with liver type fatty acid binding protein (L-FABP) gene ablated mice demonstrate a physiological role for L-FABP in hepatic fatty acid metabolism, little is known about the mechanisms whereby L-FABP elicits these effects. Studies indicate that L-FABP may function to shuttle lipids to the nucleus, thereby increasing the availability of ligands of nuclear receptors, such as peroxisome proliferator-activated receptor-alpha (PPARalpha). The data herein suggest that such mechanisms involve direct interaction of L-FABP with PPARalpha. L-FABP was shown to directly interact with PPARalpha in vitro through co-immunoprecipitation (co-IP) of pure proteins, altered circular dichroic (CD) spectra, and altered fluorescence spectra. In vitro fluorescence resonance energy transfer (FRET) between Cy3-labeled PPARalpha and Cy5-labeled L-FABP proteins showed that these proteins bound with high affinity (Kd approximately 156 nM) and in close proximity (intermolecular distance of 52A). This interaction was further substantiated by co-IP of both proteins from liver homogenates of wild-type mice. Moreover, double immunogold electron microscopy and FRET confocal microscopy of cultured primary hepatocytes showed that L-FABP was in close proximity to PPARalpha (intermolecular distance 40-49A) in vivo. Taken together, these studies were consistent with L-FABP regulating PPARalpha transcriptional activity in hepatocytes through direct interaction with PPARalpha. Our in vitro and imaging experiments demonstrate high affinity, structural molecular interaction of L-FABP with PPARalpha and suggest a functional role for L-FABP interaction with PPARalpha in long chain fatty acid (LCFA) metabolism.

Indexed as

AnimalsCell CompartmentationCell NucleusCells, CulturedFatty Acid-Binding ProteinsFatty AcidsHepatocytesLigandsMaleMiceMice, KnockoutPalmitic AcidPPAR alphaProtein BindingProtein ConformationProtein Structure, QuaternaryFabp1 protein, mouseFatty Acid-Binding ProteinsFatty AcidsLigandsPalmitic AcidPPAR alphaRecombinant ProteinsSterol Regulatory Element Binding Protein 1

Identifiers

PMID19289416
PMCPMC2724054
OpenAlexW2098534934

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.