Theory for ligand rebinding at cell membrane surfaces

Biophysical Journal

Volumn 74, Issue 3, 1998, Pages 1215-1228

  Lagerholm, B Christoffer ^a   Thompson, Nancy L ^a  

^a University of North Carolina at Chapel Hill   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND;

ARTICLE; CELL MEMBRANE; CELL SURFACE; LIGAND BINDING; MATHEMATICAL ANALYSIS; PROTEIN PROTEIN INTERACTION;

EID: 0031910469     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77836-1     Document Type: Article

References (42)

1. Abramowitz, M., and I. A. Stegun. 1974. Handbook of Mathematical Functions. Dover Publications, New York. 295ff, 355ff, 1019ff.
2. Adam, G., and M. Delbrück. 1968. Reduction of dimensionality in biological diffusion processes. In Structural Chemistry and Molecular Biology. A. Rich and N. Davison, editors. W. H. Freeman, San Francisco. 198-215.
3. Axelrod, D., and M. D. Wang. 1994. Reduction-of-dimensionality kinetics at reaction-limited cell surface receptors. Biophys. J. 66:588-600.
4. Balgi, G., D. E. Leckband, and J. M. Nitsche. 1995 Transport effects on the kinetics of protein-surface binding. Biophys. J. 68:2251-2260.
5. Berg, H. C., and E. M. Purcell. 1977. Physics of chemoreception. Biophys. J. 20:193-219.
6. Berg, O., and P. H. von Hippel. 1985. Diffusion-controlled macromoleular interactions. Annu. Rev. Biophys. Biophys. Chem. 14:131-160.
7. Burghardt, T. P., and D. Axelrod. 1981. Total internal reflection/ fluorescence photobleaching recovery study of serum albumin adsorption dynamics. Biophys. J. 33:455-467.
8. Conibear, P. B., and C. R. Bagshaw. 1996. Measurement of nucleotide exchange kinetics with isolated synthetic myosin filaments using flash photolysis. FEBS Lett. 380:13-16.
9. DeLisi, C., and F. W. Wiegel. 1981. Effect of nonspecific forces and finite receptor number on rate constants of ligand-cell bound receptor interactions. Proc. Natl. Acad. Sci. USA. 78:5569-5572.
10. Duschl, C., A. Sévin-Landais, and H. Vogel. 1996. Surface engineering: optimization of antigen presentation in self-assembled monolayers. Biophys. J. 70:1985-1995.
11. Erickson, J., B. Goldstein, D. Holowka, and B. Baird 1987. The effect of receptor density on the forward rate constant for binding of ligands to cell surface receptors. Biophys. J. 52:657-662.
12. Erickson, J. W., R. G. Posner, B. Goldstein, D. Holowka, and B. Baird. 1991. Bivalent ligand dissociation kinetics from receptor-bound immunoglobulin E: evidence for a time-dependent increase in ligand rebinding at the cell surface. Biochemistry. 30:2357-2363.
13. Forsten, K. E., and D. A. Lauffenburger. 1994. Probability of autocrine ligand capture by cell-surface receptors: implications for ligand secretion measurements. J. Comp. Biol. 1:15-23.
14. Funatsu, T., Y. Harada, M. Tokunaga, K. Saito, and T. Yanagida. 1995. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature. 374:555-559.
15. Geurts, B. J. 1989. Diffusion limited immunochemical sensing. Bull. Math. Biol. 51:359-379.
16. Goldstein, B., R. G. Posner, D. C. Torney, J. Erickson, D. Holowka, and B. Baird. 1989. Competition between solution and cell surface receptors for ligand. Dissociation of hapten bound to surface antibody in the presence of solution antibody. Biophys. J. 56:955-966.
17. Goldstein, B., and M. Dembo. 1995. Approximating the effects of diffusion on reversible reactions at the cell surface: ligand-receptor kinetics. Biophys. J. 68:1222-1230.
18. Hsieh, H. V., and N. L. Thompson. 1994. Theory for measuring bivalent surface binding kinetics using total internal reflection with fluorescence photobleaching recovery. Biophys. J. 66:898-911.
19. Hsieh, H. V., and N. L. Thompson. 1995. Dissociation kinetics between a mouse Fc receptor (FcγRII) and IgG: measurement by total internal reflection with fluorescence photobleaching recovery. Biochemistry. 34: 12481-12488.
20. Huang, Z., K. H. Pearce, and N. L. Thompson. 1994. Translational diffusion of bovine prothrombin fragment 1 weakly bound to supported planar membranes: measurement by total internal reflection with fluorescence pattern photobleaching recovery. Biophys. J. 67:1754-1766.
21. Lánská, V., P. Lánský, and C. E. Smith. 1994. Synaptic transmission in a diffusion model for neural activity. J. Theor. Biol. 166:393-406.
22. Lauffenburger, D. A., K. E. Forsten, B. Will, and H. S. Wiley. 1995. Molecular/cell engineering approach to autocrine ligand control of cell function. Ann. Biomed. Eng. 23:208-215.
23. Lookene, A., O. Chevreuil, P. Østergaard, and G. Olivecrona. 1996. Interaction of lipoprotein lipase with heparin fragments and with heparin sulfate: stoichiometry, stabilization, and kinetics. Biochemistry. 35: 12155-12163.
24. Model, M. A., and G. M. Omann. 1995. Ligand-receptor interaction rates in the presence of convective mass transport. Biophys. J. 69:1712-1720.
25. Nieba, L., A. Krebber, and A. Plückthun. 1996. Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. Anal. Biochem. 234:155-165.
26. Northrup, S. H. 1988. Diffusion-controlled ligand binding to multiple competing cell-bound receptors. J. Phys. Chem. 92:5847-5850.
27. Northrup, S. H., M. S. Curvin, S. A. Allison, and J. A. McCammon. 1986. Optimization of Brownian dynamics methods for diffusion-influenced rate constant calculations. J. Chem. Phys. 84:2196-2203.
28. Nygren, H., and M. Stenberg. 1989. Immunochemistry at interfaces. Immunology. 66:321-327.
29. O'Shannessy, D. J., and D. J. Winzor. 1996. Interpretation of deviations from pseudo-first-order kinetic behavior in the characterization of ligand binding by biosensor technology. Anal. Biochem. 236:275-283.
30. Otis, T. S., Y. Wu, and L. O. Trussell. 1996. Delayed clearance of transmitter and the role of glutamate transporters at synapses with multiple release sites. J. Neurosci. 16:1634-1644.
31. Pearce, K. H., R. G. Hiskey, and N. L. Thompson. 1992. Surface binding kinetics of prothrombin fragment 1 on planar membranes measured by total internal reflection fluorescence microscopy. Biochemistry. 31: 5983-5995.
32. Pisarchick, M. L., D. Gesty, and N. L. Thompson. 1992. Binding kinetics of an anti-dinitrophenyl monoclonal Fab on supported phospholipid monolayers measured by total internal reflection with fluorescence photobleaching recovery. Biophys. J. 63:215-223.
33. Sadana, A., and A. Madagula. 1994. A fractal analysis of external diffusion-limited first-order kinetics for the binding of antigen by immobilized antibody. Biosens. Bioelectr. 9:45-55.
34. Schuck, P., and A. P. Minton. 1996. Analysis of mass transport-limited binding kinetics in evanescent wave biosensors. Anal. Biochem. 240: 262-272.
35. Shoup, D., and A. Szabo. 1982. Role of diffusion in ligand binding to macromolecules and cell-bound receptors. Biophys. J. 40:33-39.
36. Thompson, N. L. 1982. Surface binding rates of nonfluorescent molecules may be obtained by total internal reflection with fluorescence correlation spectroscopy. Biophys. J. 38:327-329.
37. Thompson, N. L., and D. Axelrod. 1983. Immunoglobulin surface binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy. Biophys. J. 43:103-114.
38. Thompson, N. L., T. P. Burghardt, and D. Axelrod. 1981. Measuring surface dynamics of biomolecules by total internal reflection fluorescence with photobleaching recovery or correlation spectroscopy. Biophys. J. 33:435-454.
39. Vale, R. D., T. Funatsu, D. W. Pierce, L. Romberg, Y. Harada, and T. Yanagida. 1996. Direct observation of single kinesin molecules moving along microtubules. Nature. 380:451-453.
40. Wang, D., S. Gou, and D. Axelrod. 1992. Reaction rate enhancement by surface diffusion of adsorbates. Biophys. Chem. 43:117-137.
41. Xu, X. H., and E. S. Yeung. 1997. Direct measurement of single-molecule diffusion and photodecomposition in free solution. Science. 275: 1106-1109.
42. Zwanzig, R. 1990. Diffusion-controlled ligand binding to spheres partially covered by receptors: an effective medium treatment. Proc. Natl. Acad. Sci. USA. 87:5856-5857.