Evidence map›Paper›PMID 20585041›Full record

ArticleBlood2010

Tropomodulin 1-null mice have a mild spherocytic elliptocytosis with appearance of tropomodulin 3 in red blood cells and disruption of the membrane skeleton.

Jeannette D Moyer, Roberta B Nowak, Nancy E Kim, Sandra K Larkin, Luanne L Peters, John Hartwig, Frans A Kuypers, Velia M Fowler

Abstract 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 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

55 citing papers in PubMed, 82 citations in OpenAlex.

  1. Trial
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  11. Review
  12. Tropomodulin Isoform-Specific Regulation of Dendrite Development and Synapse Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  13. Myosin IIA interacts with the spectrin-actin membrane skeleton to control red blood cell membrane curvature and deformability.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. eLife · 2017
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Jeannette D MoyerThe Scripps Research Institute, La Jolla, CA 92037, USA.
Roberta B Nowak
Nancy E Kim
Sandra K Larkin
Luanne L Peters
John Hartwig
Frans A Kuypers
Velia M Fowler
Scripps Research Institute · USBrigham and Women's Hospital · USJackson Laboratory · US

Funding

PREVENTION OF COLD INDUCED PLATELET STORAGE LESIONP01HL056949 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI WAGNER, DENISA D · 1996 to 2010
$26.2M
WIP in TCR signaling and actin reorganizationP01HL059561 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI GEHA, RAIF SALIM · 1997 to 2012
$21.8M
WORKSHOPS AND TRAININGP41RR017573 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI CARRAGHER, BRIDGET OLIVIA · 2002 to 2011
$14.2M
Capping Actin Growth in Erythroid and Nonerythroid CellsR01HL083464 · NHLBI · UNIVERSITY OF DELAWARE · PI FOWLER, VELIA M · 2006 to 2019
$7.1M
Genetic Identification of Novel Genes Critical in ErythropoiesisR01HL088468 · NHLBI · NEW YORK BLOOD CENTER · PI PETERS, LUANNE L · 2008 to 2011
$1.7M
Flow lysometry and its biomedical applicationsR21HL092535 · NHLBI · CHILDREN'S HOSPITAL & RES CTR AT OAKLAND · PI KUYPERS, FRANS A. · 2008 to 2009
$440k
NCRR NIH HHS P41 RR017573NCRR NIH HHS RR17573NHLBI NIH HHS HL083464NHLBI NIH HHS HL088468NHLBI NIH HHS HL092535NHLBI NIH HHS HL56949NHLBI NIH HHS HL59561NHLBI NIH HHS P01 HL056949NHLBI NIH HHS P01 HL059561NHLBI NIH HHS R01 HL083464NHLBI NIH HHS R01 HL088468NHLBI NIH HHS R21 HL092535
6 · The paper itself

Abstract

The short actin filaments in the red blood cell (RBC) membrane skeleton are capped at their pointed ends by tropomodulin 1 (Tmod1) and coated with tropomyosin (TM) along their length. Tmod1-TM control of actin filament length is hypothesized to regulate spectrin-actin lattice organization and membrane stability. We used a Tmod1 knockout mouse to investigate the in vivo role of Tmod1 in the RBC membrane skeleton. Western blots of Tmod1-null RBCs confirm the absence of Tmod1 and show the presence of Tmod3, which is normally not present in RBCs. Tmod3 is present at only one-fifth levels of Tmod1 present on wild-type membranes, but levels of actin, TMs, adducins, and other membrane skeleton proteins remain unchanged. Electron microscopy shows that actin filament lengths are more variable with spectrin-actin lattices displaying abnormally large and more variable pore sizes. Tmod1-null mice display a mild anemia with features resembling hereditary spherocytic elliptocytosis, including decreased RBC mean corpuscular volume, cellular dehydration, increased osmotic fragility, reduced deformability, and heterogeneity in osmotic ektacytometry. Insufficient capping of actin filaments by Tmod3 may allow greater actin dynamics at pointed ends, resulting in filament length redistribution, leading to irregular and attenuated spectrin-actin lattice connectivity, and concomitant RBC membrane instability.

Indexed as

Actin CytoskeletonActinsAnemiaAnimalsCytoskeletonCytosolErythrocytesErythrocytes, AbnormalGene Knockout TechniquesMiceOsmotic FragilityTropomodulinActinsTmod1 protein, mouseTmod3 protein, mouseTropomodulin

Identifiers

PMID20585041
PMCPMC2953891
OpenAlexW1999431237

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.