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J. Biol. Chem., Vol. 269, Issue 45, 27840-27846, 11, 1994
J Philo, J Talvenheimo, J Wen, R Rosenfeld, A Welcher and T Arakawa
Interactions of three neurotrophin dimers, brain-derived neurotrophic
factor (BDNF), neurotrophin-3 (NT-3), and a NT-3.BDNF heterodimer with
extracellular, soluble TrkB and TrkC receptors were studied using native
gels, light scattering, and sedimentation equilibrium. These three
neurotrophins showed binding of two TrkB receptors per neurotrophin dimer,
with a tendency to dissociate into one TrkB per dimer for NT-3 and the
heterodimer, as determined by native gels, light scattering, and
sedimentation equilibrium. For TrkC, native gels suggested binding of NT-3,
heterodimer, and BDNF but not of nerve growth factor. Sedimentation
equilibrium revealed that all three neurotrophin molecules bind to TrkC at
two receptors per dimer but that BDNF binds much more weakly and that the
heterodimer has an intermediate binding strength. Light scattering/size
exclusion chromatography showed complexes with two TrkC receptors per NT-3
dimer and one TrkC per heterodimer but did not detect binding of BDNF to
TrkC. This latter result is not inconsistent with the sedimentation data,
because the weak binding of BDNF to TrkC may be easily dissociated by
nonspecific interactions of BDNF with the size exclusion column. The
relative binding constants for these neurotrophins and the soluble receptor
extracellular domains, as determined by sedimentation equilibrium, are
correlated with their biological activity. However, the magnitude of these
binding constants is insufficient by approximately 3 orders of magnitude to
promote receptor dimerization at physiologically active concentrations.
Interactions of neurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and the NT-3.BDNF heterodimer with the extracellular domains of the TrkB and TrkC receptors
Amgen Inc., Thousand Oaks, California 91320-1789.
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