Evidence map›Paper›PMID 19258325›Full record

ArticleThe Journal of biological chemistry2009

Loss of specific chaperones involved in membrane glycoprotein biosynthesis during the maturation of human erythroid progenitor cells.

Sian T Patterson, Jing Li, Jeong-Ah Kang, Amittha Wickrema, David B Williams, Reinhart A F Reithmeier

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Diffusion of glycophorin A in human erythrocytes.Biochimica et biophysica acta · 2016
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Role of heat shock proteins in stem cell behavior.Progress in molecular biology and translational science · 2012
    Review
  13. Article
  14. Article
  15. Article
  16. 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

6 authors at 2 institutions in 2 countries.

Sian T PattersonDepartment of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Jing Li
Jeong-Ah Kang
Amittha Wickrema
David B Williams
Reinhart A F Reithmeier
University of Toronto · CAUniversity of Chicago · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The production of erythrocytes requires the massive synthesis of red cell-specific proteins including hemoglobin, cytoskeletal proteins, as well as membrane glycoproteins glycophorin A (GPA) and anion exchanger 1 (AE1). We found that during the terminal differentiation of human CD34(+) erythroid progenitor cells in culture, key components of the endoplasmic reticulum (ER) protein translocation (Sec61alpha), glycosylation (OST48), and protein folding machinery, chaperones BiP, calreticulin (CRT), and Hsp90 were maintained to allow efficient red cell glycoprotein biosynthesis. Unexpected was the loss of calnexin (CNX), an ER glycoprotein chaperone, and ERp57, a protein-disulfide isomerase, as well as a major decrease of the cytosolic chaperones, Hsc70 and Hsp70, components normally involved in membrane glycoprotein folding and quality control. AE1 can traffic to the cell surface in mouse embryonic fibroblasts completely deficient in CNX or CRT, whereas disruption of the CNX/CRT-glycoprotein interactions in human K562 cells using castanospermine did not affect the cell-surface levels of endogenous GPA or expressed AE1. These results demonstrate that CNX and ERp57 are not required for major glycoprotein biosynthesis during red cell development, in contrast to their role in glycoprotein folding and quality control in other cells.

Indexed as

Cell DifferentiationAnimalsAnion Exchange Protein 1, ErythrocyteAntigens, CD34CalnexinCalreticulinCell MembraneCells, CulturedEndoplasmic ReticulumErythroid Precursor CellsFlow CytometryGene Expression RegulationHSC70 Heat-Shock ProteinsHumansImmunoblottingK562 CellsAnion Exchange Protein 1, ErythrocyteAntigens, CD34CalnexinCalreticulinHSC70 Heat-Shock ProteinsHSPA8 protein, humanMembrane GlycoproteinsMolecular ChaperonesMutant ProteinsRNA, Messenger

Identifiers

PMID19258325
PMCPMC2682903
OpenAlexW2088106795

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.