Evidence map›Paper›PMID 7568234›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

3T3 fibroblasts transfected with a cDNA for mitochondrial aspartate aminotransferase express plasma membrane fatty acid-binding protein and saturable fatty acid uptake.

L M Isola, S L Zhou, C L Kiang, D D Stump, M W Bradbury, P D Berk

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed, 152 citations in OpenAlex.

  1. Review
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  6. Palmitoylation of ketogenic enzyme HMGCS2 enhances its interaction with PPARalpha and transcription at the Hmgcs2 PPRE.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    Article
  7. Review
  8. Review
  9. Protein-mediated Fatty Acid Uptake in the Heart.Current cardiology reviews · 2008
    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

6 authors at 2 institutions in 1 country.

L M IsolaDepartment of Medicine, Mount Sinai School of Medicine, New York, NY 10029, USA.
S L Zhou
C L Kiang
D D Stump
M W Bradbury
P D Berk
Icahn School of Medicine at Mount Sinai · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

MECHANISMS OF HEPATIC FATTY ACID TRANSPORTR01DK026438 · NIDDK · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI BERK, PAUL DAVID · 1986 to 2001
$453k
NIDDK NIH HHS DK-26438
6 · The paper itself

Abstract

To explore the relationship between mitochondrial aspartate aminotransferase (mAspAT; EC 2.6.1.1) and plasma membrane fatty acid-binding protein (FABPpm) and their role in cellular fatty acid uptake, 3T3 fibroblasts were cotransfected with plasmid pMAAT2, containing a full-length mAspAT cDNA downstream of a Zn(2+)-inducible metallothionein promoter, and pFR400, which conveys methotrexate resistance. Transfectants were selected in methotrexate, cloned, and exposed to increasing methotrexate concentrations to induce gene amplification. Stably transfected clones were characterized by Southern blotting; those with highest copy numbers of pFR400 alone (pFR400) or pFR400 and pMAAT2 (pFR400/pMAAT2) were expanded for further study. [3H]Oleate uptake was measured in medium containing 500 microM bovine serum albumin and 125-1000 microM total oleate (unbound oleate, 18-420 nM) and consisted of saturable and nonsaturable components. pFR400/pMAAT2 cells exhibited no increase in the rate constant for nonsaturable oleate uptake or in the uptake rate of [14C]octanoate under any conditions. By contrast, Vmax (fmol/sec per 50,000 cells) of the saturable oleate uptake component increased 3.5-fold in pFR400/pMAAT2 cells compared to pFR400, with a further 3.2-fold increase in the presence of Zn2+. Zn2+ had no effect in pFR400 controls (P > 0.5). The overall increase in Vmax between pFR400 and pFR400/pMAAT2 in the presence of Zn2+ was 10.4-fold (P < 0.01) and was highly correlated (r = 0.99) with expression of FABPpm in plasma membranes as determined by Western blotting. Neither untransfected 3T3 nor pFR400 cells expressed cell surface FABPpm detectable by immunofluorescence. By contrast, plasma membrane immunofluorescence was detected in pFR400/pMAAT2 cells, especially if cultured in 100 microM Zn2+. The data support the dual hypotheses that mAspAT and FABPpm are identical and mediate saturable long-chain free fatty acid uptake.

Indexed as

Neoplasm ProteinsNerve Tissue Proteins3T3 CellsAnimalsAspartate AminotransferasesBiological TransportBlotting, WesternCarrier ProteinsCell MembraneDNA, ComplementaryFatty Acid-Binding Protein 7Fatty Acid-Binding ProteinsFatty AcidsFluorescent Antibody TechniqueMembrane ProteinsMiceAspartate AminotransferasesCarrier ProteinsDNA, ComplementaryFabp5 protein, mouseFabp7 protein, mouseFatty Acid-Binding Protein 7Fatty Acid-Binding ProteinsFatty AcidsMembrane ProteinsMyelin P2 ProteinNeoplasm ProteinsNerve Tissue ProteinsRecombinant ProteinsZinc

Identifiers

PMID7568234
PMCPMC40903
OpenAlexW2066156775

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.