Evidence map›Paper›PMID 25555908›Full record

ArticleThe Journal of biological chemistry2015

CD36 binds oxidized low density lipoprotein (LDL) in a mechanism dependent upon fatty acid binding.

Anthony G Jay, Alexander N Chen, Miguel A Paz, Justin P Hung, James A Hamilton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.5field-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

51 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Discovery andFrontiers in immunology · 2025
    Article
  12. Article
  13. Regulation of lipid storage and inflammation in the liver by CEACAM1.European journal of clinical investigation · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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.

Anthony G JayFrom the Departments of Biochemistry and; Physiology and Biophysics, Boston University, Boston, Massachusetts 02118.
Alexander N ChenPhysiology and Biophysics, Boston University, Boston, Massachusetts 02118.
Miguel A PazPhysiology and Biophysics, Boston University, Boston, Massachusetts 02118.
Justin P HungPhysiology and Biophysics, Boston University, Boston, Massachusetts 02118.
James A HamiltonPhysiology and Biophysics, Boston University, Boston, Massachusetts 02118. Electronic address: jhamilt@gmail.com.
Boston University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The association of unesterified fatty acid (FA) with the scavenger receptor CD36 has been actively researched, with focuses on FA and oxidized low density lipoprotein (oxLDL) uptake. CD36 has been shown to bind FA, but this interaction has been poorly characterized to date. To gain new insights into the physiological relevance of binding of FA to CD36, we characterized FA binding to the ectodomain of CD36 by the biophysical method surface plasmon resonance. Five structurally distinct FAs (saturated, monounsaturated (cis and trans), polyunsaturated, and oxidized) were pulsed across surface plasmon resonance channels, generating association and dissociation binding curves. Except for the oxidized FA HODE, all FAs bound to CD36, with rapid association and dissociation kinetics similar to HSA. Next, to elucidate the role that each FA might play in CD36-mediated oxLDL uptake, we used a fluorescent oxLDL (Dii-oxLDL) live cell assay with confocal microscopy imaging. CD36-mediated uptake in serum-free medium was very low but greatly increased when serum was present. The addition of exogenous FA in serum-free medium increased oxLDL binding and uptake to levels found with serum and affected CD36 plasma membrane distribution. Binding/uptake of oxLDL was dependent upon the FA dose, except for docosahexaenoic acid, which exhibited binding to CD36 but did not activate the uptake of oxLDL. HODE also did not affect oxLDL uptake. High affinity FA binding to CD36 and the effects of each FA on oxLDL uptake have important implications for protein conformation, binding of other ligands, functional properties of CD36, and high plasma FA levels in obesity and type 2 diabetes.

Indexed as

CD36 AntigensCell MembraneDiabetes Mellitus, Type 2Fatty AcidsHEK293 CellsHeLa CellsHumansLipoproteins, LDLObesityProtein BindingProtein Structure, TertiarySurface Plasmon ResonanceCD36 AntigensFatty AcidsLipoproteins, LDLoxidized low density lipoproteinConfocal MicroscopyDisulfideFatty AcidLow Density Lipoprotein (LDL)Surface Plasmon Resonance (SPR)

Identifiers

PMID25555908
PMCPMC4335201
OpenAlexW2051710738

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.