ArticleBiophysical journal1996
Kinetics and locus of failure of receptor-ligand-mediated adhesion between latex spheres. I. Protein-carbohydrate bond.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 33 citations in OpenAlex.
- Application of Population Dynamics to Study Heterotypic Cell Aggregations in the Near-Wall Region of a Shear Flow.Cellular and molecular bioengineering · 2010Article
- Two-dimensional kinetics of beta 2-integrin and ICAM-1 bindings between neutrophils and melanoma cells in a shear flow.American journal of physiology. Cell physiology · 2008Article
- Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: the GPIb(alpha)-vWF tether bond.Biophysical journal · 2002Article
- Dynamics of neutrophil aggregation in couette flow revealed by videomicroscopy: effect of shear rate on two-body collision efficiency and doublet lifetime.Biophysical journal · 2001Article
- Outer membrane monolayer domains from two-dimensional surface scanning resistance measurements.Biophysical journal · 2000Article
- Time and force dependence of the rupture of glycoprotein IIb-IIIa-fibrinogen bonds between latex spheres.Biophysical journal · 2000Article
- A direct comparison of selectin-mediated transient, adhesive events using high temporal resolution.Biophysical journal · 1999Article
- Probabilistic modeling of shear-induced formation and breakage of doublets cross-linked by receptor-ligand bonds.Biophysical journal · 1999Article
- An automatic braking system that stabilizes leukocyte rolling by an increase in selectin bond number with shear.The Journal of cell biology · 1999Article
- Measuring two-dimensional receptor-ligand binding kinetics by micropipette.Biophysical journal · 1998Article
- Experimental study of the interaction range and association rate of surface-attached cadherin 11.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Micropipet-based pico force transducer: in depth analysis and experimental verification.Biophysical journal · 1998Article
- Kinetics and locus of failure of receptor-ligand-mediated adhesion between latex spheres. II. Protein-protein bond.Biophysical journal · 1996Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We previously described the use of a counter-rotating cone and plate rheoscope to measure the time and force dependence of break-up of doublets of sphered, swollen, and fixed red cells (SSRC) cross-linked by monoclonal IgM antibody. It has been shown that doublet break-up can occur by extraction of receptors from the membrane, rather than by antibody-antigen bond break-up, and is a stochastic process. We therefore prepared 4.62-microns carboxyl modified latex spheres with a covalently coupled synthetic blood group B antigen trisaccharide. Using a two-step carbodiimide process, ethylene diamine was covalently linked to the carboxyl modified latex spheres, and the trisaccharide, having an eight carbon spacer modified to bear a terminal carboxyl group, was linked to the ethylene diamine. Using these antigen spheres we carried out studies in Couette flow, in a transparent cone and plate rheoscope, of the shear-induced break-up of doublets cross-linked by monoclonal IgM anti-B antibody in 19% and 15% Dextran 40. As previously found with SSRC, over a range of normal force from 55 to 175 pN, there was a distribution in times to break-up. However, the fraction of antigen sphere doublets broken up, which increased from 0.08 to 0.43 at 75 pM IgM, and from 0.06 to 0.20 at 150 pM IgM, was significantly lower than that for the SSRC, where the fraction broken up at 150 pM IgM increased from 0.10 to 0.47. Thus, significantly higher forces were required to achieve the same degree of break-up for doublets of antigen-linked spheres than for SSRC. Computer simulation using a stochastic model of break-up showed that the differences between antigen sphere and SSRC doublet break-up were due to a change in bond character (the range and depth of the bond energy minimum) rather than to an increase in the number of bonds linking antigen-sphere doublets. This supports the notion that antibody-antigen bonds are ruptured in the case of antigen spheres, whereas antigen is able to be extracted from the membrane of SSRC, although changes of receptor substrate from cell to latex and the possibility of latex strand extraction from the microspheres are potential complicating factors.
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