Evidence map›Paper›PMID 2065188›Full record

ArticleBiophysical journal1991

Detachment of agglutinin-bonded red blood cells. I. Forces to rupture molecular-point attachments.

E Evans, D Berk, A Leung

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
8.0field-weighted citation impact, top 1% 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

88 citing papers in PubMed, 297 citations in OpenAlex.

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  12. Stochastic simulation of single-molecule pulling experiments.The European physical journal. E, Soft matter · 2014
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  18. Cellular morphogenesis in silico.Biophysical journal · 2009
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  20. Article

28 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

E EvansDepartment of Pathology, University of British Columbia, Vancouver, Canada.
D Berk
A Leung
University of British Columbia · CA

Funding

BLOOD CELL MECHANICS, SURFACE AFFINITY AND ADHESIONR01HL045099 · NHLBI · UNIVERSITY OF BRITISH COLUMBIA · PI EVANS, EVAN A · 1990 to 1992
–
NHLBI NIH HHS HL45099
6 · The paper itself

Abstract

A simple micromechanical method has been developed to measure the rupture strength of a molecular-point attachment (focal bond) between two macroscopically smooth membrane capsules. In the procedure, one capsule is prepared with a low density coverage of adhesion molecules, formed as a stiff sphere, and held at fixed position by a micropipette. The second capsule without adhesion molecules is pressurized into a spherical shape with low suction by another pipette. This capsule is maneuvered to initiate point contact at the pole opposite the stiff capsule which leads to formation of a few (or even one) molecular attachments. Then, the deformable capsule is slowly withdrawn by displacement of the pipette. Analysis shows that the end-to-end extension of the capsule provides a direct measure of the force at the point contact and, therefore, the rupture strength when detachment occurs. The range for point forces accessible to this technique depends on the elastic moduli of the membrane, membrane tension, and the size of the capsule. For biological and synthetic vesicle membranes, the range of force lies between 10(-7)-10(-5) dyn (10(-12)-10(-10) N) which is 100-fold less than presently measurable by Atomic Force Microscopy! Here, the approach was used to study the forces required to rupture microscopic attachments between red blood cells formed by a monoclonal antibody to red cell membrane glycophorin, anti-A serum, and a lectin from the snail-helix pomatia. Failure of the attachments appeared to be a stochastic function of the magnitude and duration of the detachment force. We have correlated the statistical behavior observed for rupture with a random process model for failure of small numbers of molecular attachments. The surprising outcome of the measurements and analysis was that the forces deduced for short-time failure of 1-2 molecular attachments were nearly the same for all of the agglutinin, i.e., 1-2 x 10(-6) dyn. Hence, microfluorometric tests were carried out to determine if labeled agglutinins and/or labeled surface molecules were transferred between surfaces after separation of large areas of adhesive contact. The results showed that the attachments failed because receptors were extracted from the membrane.

Indexed as

HemagglutininsABO Blood-Group SystemAnimalsAntibodies, MonoclonalErythrocyte DeformabilityErythrocyte MembraneErythrocytesGlycophorinsHelix, SnailsHumansImmune SeraLectinsMathematicsModels, BiologicalABO Blood-Group SystemAntibodies, MonoclonalGlycophorinsHelix lectinHemagglutininsImmune SeraLectins

Identifiers

PMID2065188
PMCPMC1281249
OpenAlexW2151431807

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.