Evidence map›Paper›PMID 12857870›Full record

ArticleMolecular biology of the cell2003

Lectin-like Ox-LDL receptor is expressed in human INT-407 intestinal cells: involvement in the transcytosis of pancreatic bile salt-dependent lipase.

Nadine Bruneau, Stéphane Richard, Françoise Silvy, Alain Verine, Dominique Lombardo

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Trial
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  3. Article
  4. Review
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  6. Article
  7. Oxidized LDL and LOX-1 in experimental sepsis.Mediators of inflammation · 2013
    Review
  8. Procyanidins are potent inhibitors of LOX-1: a new player in the French Paradox.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2011
    Article
  9. Article
  10. Article
  11. 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

5 authors at 1 institution in 1 country.

Nadine BruneauINSERM U-559, Unité de Recherche de Physiopathologie des Cellules Epithéliales and Equipe d'Accueil 3289, Université de la Méditerranée, Faculté de Médecine, Marseilles, France. nadine.brunewu@medecine.univ-mrs.fr
Stéphane Richard
Françoise Silvy
Alain Verine
Dominique Lombardo
Inserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have recently shown that the pancreatic bile salt-dependent lipase (BSDL) can be taken up by intestinal cells and transported to the blood circulation. This mechanism likely involves (specific) receptor(s) able to bind BSDL and located at the apical intestinal cell membrane. In this study, using Int407 human intestinal cells cultured to form a tight epithelium, we attempted to characterize (the) BSDL receptor(s). We found that an apical 50-kDa protein was able to bind BSDL. Further, we have demonstrated that Int407 cells expressed the lectin-like oxidized-LDL receptor (LOX-1), the upregulation of which by oxidized-LDL potentiates the transcytosis of BSDL, whereas carrageenan and to a lesser extent polyinosinic acid and fucoidan decrease the enzyme transcytosis. The mAb JTX92, which blocks the LOX-1 receptor function, also impaired the BSDL transcytosis. To confirm these results, the cDNA encoding the human intestinal receptor LOX-1 has been cloned, inserted into vectors, and transfected into Int407 cells. Overexpression of LOX-1 by these cells leads to a substantial increase in the BSDL transcytosis. Globally, these data support the view that LOX-1 could be an intestinal receptor for BSDL, which is implicated in the transcytosis of this enzyme throughout Int407 cells.

Indexed as

Cell LineCloning, MolecularEndocytosisFlow CytometryHumansIntestinal MucosaIntestinesLipoproteins, LDLPoly IPolysaccharidesProtein BindingReceptors, LDLReceptors, Oxidized LDLScavenger Receptors, Class ESterol EsteraseTransferrinbile salt-stimulated lipaseLipoproteins, LDLOLR1 protein, humanoxidized low density lipoproteinPoly IPolysaccharidesReceptors, LDLReceptors, Oxidized LDLScavenger Receptors, Class ESterol EsteraseTransferrin

Identifiers

PMID12857870
PMCPMC165682
OpenAlexW2104924985

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.