Evidence map›Paper›PMID 8061221›Full record

ArticleBiophysical journal1994

Cooperative action between band 3 and glycophorin A in human erythrocytes: immobilization of band 3 induced by antibodies to glycophorin A.

D W Knowles, J A Chasis, E A Evans, N Mohandas

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biophysical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
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

25 citing papers in PubMed, 74 citations in OpenAlex.

  1. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  7. Article
  8. Diffusion of glycophorin A in human erythrocytes.Biochimica et biophysica acta · 2016
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Protein 4.1R-dependent multiprotein complex: new insights into the structural organization of the red blood cell membrane.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  18. Article
  19. Article
  20. Erythrocyte membrane vesiculation: model for the molecular mechanism of protein sorting.Proceedings of the National Academy of Sciences of the United States of America · 1997
    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

4 authors at 2 institutions in 2 countries.

D W KnowlesDepartment of Physics, University of British Columbia, Vancouver, Canada.
J A Chasis
E A Evans
N Mohandas
University of British Columbia · CAUniversity of California, Berkeley · US

Funding

YEAST MEMBRANE CYTOSKELETONP01DK032094 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1987 to 2021
$26.7M
RED CELL DEFORMABILITY IN VITRO AND SURVIVAL IN VIVOR37DK026263 · NIDDK · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI NARLA, MOHANDAS · 1995 to 2017
$4.5M
RHEOLOGICAL AND ADHERENCE PROPERTIES OF SICKLE CELLSR01HL031579 · NHLBI · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1985 to 2010
$3.8M
RED CELL DEFORMABILITY IN VITRO AND SURVIVAL IN VIVOR01DK026263 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1986 to 2007
$1.6M
NHLBI NIH HHS HL31579NIDDK NIH HHS DK26263NIDDK NIH HHS DK32094
6 · The paper itself

Abstract

The ability of transmembrane receptor proteins to change their association with the cytoskeleton in response to ligand binding seems to be a key mechanism of signal transduction across membranes. To investigate the molecular features of this mechanism we have used the red cell membrane as a model system to study signal transduction through the integral protein, glycophorin A. In these studies the lateral mobility of integral proteins was measured in situ by fluorescence recovery after photobleaching, and membrane rigidity was characterized by micropipette aspiration technique. We found that binding either a monoclonal antibody or its monovalent Fab to the exoplasmic domain of glycophorin A in normal red cells immobilized the receptor and rigidified the membrane. Further, immobilization and rigidification did not occur when antibodies were bound to Miltenberger V cells containing a mutant form of glycophorin A lacking the cytoplasmic domain. These results imply that the site of the immobilization/rigidification lies within the membrane skeletal structure, not in exofacial receptor crosslinking, and requires the extended cytoplasmic domain of normal glycophorin A. In addition, we found that glycophorin A immobilization and membrane skeletal rigidification were accompanied by immobilization of band 3 receptors. This unexpected result indicates a cooperative coupling between liganded glycophorin A, band 3, and the membrane skeleton. We speculate that cooperation of this type may represent a general mechanism for cytoskeletal linkage and transformation initiated by receptors with short cytoplasmic sequences, such as integrins.

Indexed as

AnimalsAnion Exchange Protein 1, ErythrocyteAntibodiesBiophysical PhenomenaBiophysicsCamelids, New WorldCytoskeletonErythrocyte DeformabilityErythrocyte MembraneErythrocytesGlycophorinsHumansIn Vitro TechniquesMutationReceptors, Cell SurfaceSpecies SpecificityAnion Exchange Protein 1, ErythrocyteAntibodiesGlycophorinsReceptors, Cell Surface

Identifiers

PMID8061221
PMCPMC1275892
OpenAlexW1972510866

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.