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Imaging Molecular Adhesion in Cell Rolling by Adhesion Footprint Assay
Published on: September 27, 2021
Molecular stiffness of selectins.
Krishna K Sarangapani1, Bryan T Marshall, Rodger P McEver
1Coulter Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
The Journal of Biological Chemistry
|January 11, 2011
Summary
Selectins, crucial for leukocyte adhesion during inflammation, exhibit varying stiffness related to their structure. P-selectin functions as a dimer, unlike L- and E-selectins, impacting molecular interactions.
Area of Science:
- Biophysics
- Cellular Biology
- Immunology
Background:
- Selectin-ligand interactions are vital for leukocyte adhesion to vascular surfaces during inflammation.
- The mechanical properties of these molecules may influence their biological function.
- Atomic force microscopy (AFM) offers a method to probe molecular mechanics.
Purpose of the Study:
- To characterize the molecular stiffness and mechanical properties of L-, E-, and P-selectins.
- To investigate the multimericity and binding behavior of purified selectins.
- To determine the molecular length of endoglycan-Ig.
Main Methods:
- Mechanical measurements using atomic force microscopy (AFM).
- Analysis of selectins complexed with ligands and antibodies.
- Reconstitution of purified membrane selectins into lipid bilayers.
Main Results:
- Stiffness of L-, E-, and P-selectins (4.2, 1.4, 0.85 pN/nm) inversely correlated with consensus repeats.
- P-selectin formed dimeric bonds with ligands, while L- and E-selectins formed monomeric bonds.
- Endoglycan-Ig molecular length was determined to be 51 ± 12 nm.
Conclusions:
- Molecular stiffness of selectins is linked to their structural repeats and influences their function.
- P-selectin's dimeric nature affects its binding capacity compared to monomeric L- and E-selectins.
- AFM is a powerful tool for characterizing molecular mechanics, multimericity, and length.
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