Evidence map›Paper›PMID 19996109›Full record

ArticleThe Journal of biological chemistry2010

Identification of human plasma proteins as major clients for the extracellular chaperone clusterin.

Amy R Wyatt, Mark R Wilson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 48 citations in OpenAlex.

  1. Clusterin is enriched in plaque-associated astrocytes and localizes to synapses in Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Plasma Proteomic Analysis in Morquio A Disease.International journal of molecular sciences · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. How schistosomes alter the human serum proteome.Molecular and biochemical parasitology · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. Article
  15. Article
  16. Clusterin facilitates in vivo clearance of extracellular misfolded proteins.Cellular and molecular life sciences : CMLS · 2011
    Article
  17. Article
  18. Article
  19. Article
  20. Levels of plasma ceruloplasmin protein are markedly lower following dietary copper deficiency in rodents.Comparative biochemistry and physiology. Toxicology & pharmacology : CBP · 2010
    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

2 authors at 1 institution in 1 country.

Amy R WyattFrom the School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia.
Mark R WilsonFrom the School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia. Electronic address: mrw@uow.edu.
University of Wollongong · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clusterin (CLU) is an extracellular chaperone that is likely to play an important role in protein folding quality control. This study identified three deposition disease-associated proteins as major plasma clients for clusterin by studying CLU-client complexes formed in response to physiologically relevant stress (shear stress, approximately 36 dynes/cm(2) at 37 degrees C). Analysis of plasma samples by size exclusion chromatography indicated that (i) relative to control plasma, stressed plasma contained proportionally more soluble protein species of high molecular weight, and (ii) high molecular weight species were far more abundant when proteins purified by anti-CLU immunoaffinity chromatography from stressed plasma were compared with those purified from control plasma. SDS-PAGE and Western blot analyses indicated that a variety of proteins co-purified with CLU from both stressed and control plasma; however, several proteins were uniquely present or much more abundant when plasma was stressed. These proteins were identified by mass spectrometry as ceruloplasmin, fibrinogen, and albumin. Immunodot blot analysis of size exclusion chromatography fractionated plasma suggested that CLU-client complexes generated in situ are very large and may reach >or=4 x 10(7) Da. Lastly, sandwich enzyme-linked immunosorbent assay detected complexes containing CLU and ceruloplasmin, fibrinogen, or albumin in stressed but not control plasma. We have previously proposed that CLU-client complexes serve as vehicles to dispose of damaged misfolded extracellular proteins in vivo via receptor-mediated endocytosis. A better understanding of these mechanisms is likely to ultimately lead to the identification of new therapies for extracellular protein deposition disorders.

Indexed as

Blood ProteinsBlotting, WesternCeruloplasminChromatography, AffinityChromatography, GelClusterinElectrophoresis, Polyacrylamide GelEnzyme-Linked Immunosorbent AssayExtracellular SpaceFibrinogenHumansMolecular ChaperonesMolecular WeightProtein BindingProteomicsSerum AlbuminBlood ProteinsCeruloplasminClusterinFibrinogenMolecular ChaperonesSerum Albumin

Identifiers

PMID19996109
PMCPMC2823492
OpenAlexW2015259446

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.