Evidence map›Paper›PMID 20861458›Full record

ArticleBlood2010

Ligation of complement receptor 1 increases erythrocyte membrane deformability.

Aleksandra M Glodek, Rossen Mirchev, David E Golan, Joseph A Khoory, Jennie M Burns, Sergey S Shevkoplyas, Anne Nicholson-Weller, Ionita C Ghiran

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Trial
  2. Biomimetic erythrocyte-based drug delivery systems for organ-targeted therapy.Frontiers in bioengineering and biotechnology · 2025
    Review
  3. Review
  4. Review
  5. Biophysical Tools and Concepts Enable Understanding of Asexual Blood Stage Malaria.Frontiers in cellular and infection microbiology · 2022
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. eLife · 2017
    Article
  13. Review
  14. Drug delivery by erythrocytes: "Primum non nocere".Transfusion and apheresis science : official journal of the World Apheresis Association : official journal of the European Society for Haemapheresis · 2016
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

8 authors at 5 institutions in 1 country.

Aleksandra M GlodekDivision of Allergy and Inflammation, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA.
Rossen Mirchev
David E Golan
Joseph A Khoory
Jennie M Burns
Sergey S Shevkoplyas
Anne Nicholson-Weller
Ionita C Ghiran
Beth Israel Deaconess Medical Center · USHarvard University · USTulane University · USBrigham and Women's Hospital · USWorcester Polytechnic Institute · US

Funding

CRI (CD35) As a Cellular Receptor for CIqR01AI042987 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI NICHOLSON-WELLER, ANNE · 1998 to 2007
$2.8M
Molecular Regulation of Adhesive Integrin Interactions in Erythroblastic IslandsR01HL032854 · NHLBI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLAN, DAVID E. · 1985 to 2011
$2.0M
NHLBI NIH HHS R01 HL032854NHLBI NIH HHS R01HL32854NIAID NIH HHS AI42987NIAID NIH HHS R01 AI042987
6 · The paper itself

Abstract

Microbes as well as immune complexes and other continuously generated inflammatory particles are efficiently removed from the human circulation by red blood cells (RBCs) through a process called immune-adherence clearance. During this process, RBCs use complement receptor 1 (CR1, CD35) to bind circulating complement-opsonized particles and transfer them to resident macrophages in the liver and spleen for removal. We here show that ligation of RBC CR1 by antibody and complement-opsonized particles induces a transient Ca(++) influx that is proportional to the RBC CR1 levels and is inhibited by T1E3 pAb, a specific inhibitor of TRPC1 channels. The CR1-elicited RBC Ca(++) influx is accompanied by an increase in RBC membrane deformability that positively correlates with the number of preexisting CR1 molecules on RBC membranes. Biochemically, ligation of RBC CR1 causes a significant increase in phosphorylation levels of β-spectrin that is inhibited by preincubation of RBCs with DMAT, a specific casein kinase II inhibitor. We hypothesize that the CR1-dependent increase in membrane deformability could be relevant for facilitating the transfer of CR1-bound particles from the RBCs to the hepatic and splenic phagocytes.

Indexed as

AdducinsCalciumCalmodulin-Binding ProteinsCasein Kinase IIErythrocyte CountErythrocyte MembraneFlow CytometryHumansMacrophagesPhagocytosisPhosphorylationReceptors, ComplementSpectrinTRPC Cation ChannelsAdducinsCalciumCalmodulin-Binding ProteinsCasein Kinase IIReceptors, ComplementSpectrintransient receptor potential cation channel, subfamily C, member 1TRPC Cation Channels

Identifiers

PMID20861458
PMCPMC3031392
OpenAlexW2054770538

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.