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PMID: 2065188 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Biophysical journal ·Vol. 59 ·No. 4 ·1991-04-00 ·Pages 838-48

Evans E, Berk D, Leung A

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 Then, the deformable capsule is slowly withdrawn by displacement of the pipette.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.

MeSH Terms
ABO Blood-Group System/immunology Animals Antibodies, Monoclonal Erythrocyte Deformability Erythrocyte Membrane/immunology,physiology Erythrocytes/cytology,immunology,physiology Glycophorins/immunology Helix, Snails Hemagglutinins Humans Immune Sera Lectins Mathematics Models, Biological
Chemicals
ABO Blood-Group System Antibodies, Monoclonal Glycophorins Helix lectin Hemagglutinins Immune Sera Lectins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Evans E
Department of Pathology, University of British Columbia, Vancouver, Canada.
Berk D
Leung A
References (11)
11 references, click to expand
  1. Interaction forces between red cells agglutinated by antibody. II. Measurement of hydrodynamic force of breakup.
    Biophys J. 1986 Dec;50(6):1117-26 PMID: 3801572
  2. Studies on specificity and binding properties of the blood group A reactive hemagglutinin from Helix pomatia.
    Biochemistry. 1971 Apr 27;10(9):1684-92 PMID: 4931750
  3. Atomic force microscope.
    Phys Rev Lett. 1986 Mar 3;56(9):930-933 PMID: 10033323
  4. Detachment of agglutinin-bonded red blood cells. II. Mechanical energies to separate large contact areas.
    Biophys J. 1991 Apr;59(4):849-60 PMID: 2065189
  5. Models for the specific adhesion of cells to cells.
    Science. 1978 May 12;200(4342):618-27 PMID: 347575
  6. The reaction-limited kinetics of membrane-to-surface adhesion and detachment.
    Proc R Soc Lond B Biol Sci. 1988 Jun 22;234(1274):55-83 PMID: 2901109
  7. Monoclonal antibodies to human erythrocytes.
    Eur J Immunol. 1982 Mar;12(3):228-32 PMID: 6807697
  8. Interaction forces between red cells agglutinated by antibody. I. Theoretical.
    Biophys J. 1986 Dec;50(6):1109-16 PMID: 3801571
  9. Extensional flow of erythrocyte membrane from cell body to elastic tether. I. Analysis.
    Biophys J. 1982 Jul;39(1):71-81 PMID: 7104453
  10. The Wrb antigen, a receptor for Plasmodium falciparum malaria, is located on a helical region of the major membrane sialoglycoprotein of human red blood cells.
    Biochem J. 1983 Jan 1;209(1):273-6 PMID: 6342608
  11. Lateral mobility of band 3 in the human erythrocyte membrane studied by fluorescence photobleaching recovery: evidence for control by cytoskeletal interactions.
    Proc Natl Acad Sci U S A. 1980 May;77(5):2537-41 PMID: 6930650
Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1991-04-00
Pages
838-48
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1281249
Subset
IM
Grants
NHLBI NIH HHS · HL45099 · United States
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