ArticleBiophysical journal2002
Force spectroscopy of the leukocyte function-associated antigen-1/intercellular adhesion molecule-1 interaction.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.
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Who cites it
107 citing papers in PubMed, 272 citations in OpenAlex.
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- Single-Molecule Force Probing of RGD-Binding Integrins on Pancreatic Cancer Cells.ACS applied materials & interfaces · 2022Article
- Supported Lipid Bilayers and the Study of Two-Dimensional Binding Kinetics.Frontiers in molecular biosciences · 2022Review
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- Biomechanical characterization of SARS-CoV-2 spike RBD and human ACE2 protein-protein interaction.Biophysical journal · 2021Article
- Review: Cantilever-Based Sensors for High Speed Atomic Force Microscopy.Sensors (Basel, Switzerland) · 2020Review
- The bioenergetics of integrin-based adhesion, from single molecule dynamics to stability of macromolecular complexes.Computational and structural biotechnology journal · 2020Review
- Nucleolin mediates the binding of cancer cells to L-selectin under conditions of lymphodynamic shear stress.American journal of physiology. Cell physiology · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Calcium-Mediated Biophysical Binding of Cryptosporidium parvum Oocysts to Surfaces Is Sensitive to Oocyst Age.Applied and environmental microbiology · 2019Article
- Enhancing cancer cell adhesion with clay nanoparticles for countering metastasis.Scientific reports · 2019Article
- Biomechanical characterization of TIM protein-mediated Ebola virus-host cell adhesion.Scientific reports · 2019Article
- Integrin α4β7 switches its ligand specificity via distinct conformer-specific activation.The Journal of cell biology · 2018Article
47 more citing papers are in PubMed but not listed here.
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3 authors at 1 institution in 1 country.
Funding
Abstract
Interactions between leukocyte function-associated antigen-1 (LFA-1) with its cognate ligand, intercellular adhesion molecule-1 (ICAM-1) play a crucial role in leukocyte adhesion. Because the cell and its adhesive components are subject to external perturbation from the surrounding flow of blood, it is important to understand the binding properties of the LFA-1/ICAM-1 interaction in both steady state and in the presence of an external pulling force. Here we report on atomic force microscopy (AFM) measurements of the unbinding of LFA-1 from ICAM-1. The single molecule measurements revealed the energy landscape corresponding to the dissociation of the LFA-1/ICAM-1 complex and provided the basis for defining the energetic determinants of the complex at equilibrium and under the influence of an external force. The AFM force measurements were performed in an experimental system consisting of an LFA-1-expressing T cell hybridoma, 3A9, attached to the end of the AFM cantilever and an apposing surface expressing ICAM-1. In measurements covering three orders of magnitude change in force loading rate, the LFA-1/ICAM-1 force spectrum (i.e., unbinding force versus loading rate) revealed a fast and a slow loading regime that characterized a steep inner activation barrier and a wide outer activation barrier, respectively. The addition of Mg(2+), a cofactor that stabilizes the LFA-1/ICAM-1 interaction, elevated the unbinding force of the complex in the slow loading regime. In contrast, the presence of EDTA suppressed the inner barrier of the LFA-1/ICAM-1 complex. These results suggest that the equilibrium dissociation constant of the LFA-1/ICAM-1 interaction is regulated by the energetics of the outer activation barrier of the complex, while the ability of the complex to resist a pulling force is determined by the divalent cation-dependent inner activation barrier.
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