Evidence map›Paper›PMID 11696003›Full record

ArticleThe Biochemical journal2001

Fatty-acid-binding proteins do not protect against induced cytotoxicity in a kidney cell model.

A W Zimmerman, J H Veerkamp

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

12 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Macrophage programming is regulated by a cooperative interaction between fatty acid binding protein 5 and peroxisome proliferator-activated receptor γ.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
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  6. FABP5 deficiency enhances susceptibility to H1N1 influenza A virus-induced lung inflammation.American journal of physiology. Lung cellular and molecular physiology · 2013
    Article
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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

2 authors at 2 institutions in 1 country.

A W ZimmermanDepartment of Biochemistry, University Medical Center Nijmegen, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. A.Zimmerman@bioch.kun.nl
J H Veerkamp
Radboud University Medical Center · NLRadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracellular accumulation of fatty acids (FAs) is a well-described consequence of renal ischaemia and may lead to lethal cell injury. Fatty-acid-binding proteins (FABPs) are small cytosolic proteins with high affinity for FAs. They may protect vital cellular functions by binding to and promoting the metabolism of FAs, thereby reducing their intracellular concentration. In this study we investigated the putative cytoprotective role of FABPs in a Madin-Darby canine kidney (MDCK) cell model for renal damage. We studied the effects of transfection with cDNA encoding heart FABP, adipocyte FABP or liver FABP on cytotoxicity induced by chemical anoxia or FAs. Transfection of MDCK type II cells with these cDNA types caused a 5-20-fold increase in FABP content, but did not change the rate or extent of palmitate uptake. After 1 h of incubation with KCN, all cell types showed reduced viability and cellular ATP content and an intracellular accumulation of non-esterified FAs. High extracellular concentrations of oleate, but not palmitate, caused a markedly decreased cell viability and cellular ATP content. Oleate accumulated in non-esterified form in these cells. Simultaneous addition of glucose ameliorated the damaging effects of KCN or oleate, indicating that glycolytic ATP could substitute for uncoupled oxidative phosphorylation. No significant differences in the effects of chemical anoxia or oleate were observed between non-transfected, mock-transfected and FABP-cDNA-transfected cells. Non-esterified FA accumulation was not reduced in any of the FABP-cDNA-transfected cell lines. In conclusion, our data do not provide evidence for a cytoprotective role of FABP in this kidney cell model.

Indexed as

Neoplasm ProteinsAdenosine TriphosphateAnimalsCalcium PhosphatesCarrier ProteinsCell LineCell SurvivalDNA, ComplementaryDogsElectrophoresis, Polyacrylamide GelFatty Acid-Binding ProteinsImmunoblottingKidneyOleic AcidPalmitic AcidPlasmidsAdenosine Triphosphatealpha-tricalcium phosphatecalcium phosphatecalcium phosphate, dibasic, anhydrouscalcium phosphate, monobasic, anhydrousCalcium PhosphatesCarrier ProteinsDNA, ComplementaryFatty Acid-Binding ProteinsNeoplasm ProteinsOleic AcidPalmitic AcidPotassium Cyanidetetracalcium phosphate

Identifiers

PMID11696003
PMCPMC1222213
OpenAlexW1994572553

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.