Evidence map›Paper›PMID 19369259›Full record

ArticleThe Journal of biological chemistry2009

The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.

Sarah J Hoosdally, Edward J Andress, Carol Wooding, Catherine A Martin, Kenneth J Linton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 9% 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

70 citing papers in PubMed, 1 synthesis or guideline pooled it, 128 citations in OpenAlex.

  1. Pooled it
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  17. Molecular characterization of four innate immune genes inFish and shellfish immunology reports · 2022
    Article
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10 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

5 authors at 3 institutions in 1 country.

Sarah J HoosdallyFrom the Medical Research Council (MRC) Clinical Sciences Centre, Imperial College, Hammersmith Hospital Campus, London W12 0NN.
Edward J AndressFrom the Medical Research Council (MRC) Clinical Sciences Centre, Imperial College, Hammersmith Hospital Campus, London W12 0NN.
Carol WoodingFrom the Medical Research Council (MRC) Clinical Sciences Centre, Imperial College, Hammersmith Hospital Campus, London W12 0NN.
Catherine A MartinFrom the Medical Research Council (MRC) Clinical Sciences Centre, Imperial College, Hammersmith Hospital Campus, London W12 0NN.
Kenneth J LintonFrom the Medical Research Council (MRC) Clinical Sciences Centre, Imperial College, Hammersmith Hospital Campus, London W12 0NN; Institute of Cell and Molecular Science, Queen Mary University of London, Barts and The London School of Medicine and Dentistry, 4 Newark Street, London E1 2AT, United Kingdom. Electronic address: kenneth.linton@ic.ac.uk.
Hammersmith Hospital · GBMedical Research Council · GBQueen Mary University of London · GB

Funding

British Heart Foundation PG/03/044/15328Medical Research Council MC_U120088463
6 · The paper itself

Abstract

Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes. This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance. CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized. Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation. Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells established that glycosylation is necessary for trafficking to the plasma membrane. Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417. However, unlike SRBI, no individual site was found to be essential for proper trafficking of CD36. Surprisingly, these minimally glycosylated mutants appear to be predominantly core-glycosylated, indicating that mature glycosylation is not necessary for surface expression in mammalian cells. The data also show that neither the nature nor the pattern of glycosylation is relevant to binding of modified low density lipoprotein.

Indexed as

AnimalsAntigens, SurfaceAsparagineBinding SitesCD36 AntigensCell MembraneCells, CulturedElectrophoretic Mobility Shift AssayGene ExpressionGlycosylationHumansLipoproteins, LDLMass SpectrometryMutagenesisProtein BindingProtein TransportAntigens, SurfaceAsparagineCD36 AntigensLipoproteins, LDL

Identifiers

PMID19369259
PMCPMC2713513
OpenAlexW1965505615

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.