Analysis of ligand-receptor interactions in cells by atomic force microscopy.
Atomic force microscopy (AFM) increasingly has been used to analyse "receptor" function, either by using purified proteins ("molecular recognition microscopy") or, more recently, in situ in living cells. The latter approach has been enabled by the use of a modified commercial AFM, linked to a confocal microscope, which has allowed adhesion forces between ligands and receptors in cells to be measured and mapped, and downstream cellular responses analysed. We review the application of AFM to cell biology and, in particular, to the study of ligand-receptor interactions and draw examples from our own work and that of others to show the utility of AFM, including for the exploration of cell surface functionalities. We also identify shortcomings of AFM in comparison to "standard" methods, such as receptor auto-radiography or immuno-detection, that are widely applied in cell biology and pharmacological analysis.
Horton
Michael
M
Department of Medicine, University College London, London WC IE 6JJ, UK. m.horton@ucl.ac.uk
Charras
Guillaume
G
Lehenkari
Petri
P
D000818:Animals; D001665:Binding Sites; D002116:Calcitonin / Q000378:metabolism; D006801:Humans; D016023:Integrins / Q000378:metabolism; D008024:Ligands; D018625:Microscopy, Atomic Force / Q000379:methods*; D009842:Oligopeptides / Q000378:metabolism; D010010:Osteoclasts / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000032:analysis*; D014660:Vasoactive Intestinal Peptide / Q000378:metabolism
D016023:Integrins; D008024:Ligands; D009842:Oligopeptides; D011956:Receptors, Cell Surface; D014660:Vasoactive Intestinal Peptide; C047981:arginyl-glycyl-aspartic acid; D002116:Calcitonin