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Journal of Neuroscience, Vol 8, 3337-3342, Copyright © 1988 by Society for Neuroscience
Binding characteristics of brain-derived neurotrophic factor to its receptors on neurons from the chick embryo
A Rodriguez-Tebar and YA Barde
Max-Planck-Institute for Psychiatry, Department of Neurochemistry, Martinsried, Federal Republic of Germany.
Brain-derived neurotrophic factor (BDNF), a protein known to support the
survival of embryonic sensory neurons and retinal ganglion cells, was
derivatized with 125I-Bolton-Hunter reagent and obtained in a biologically
active, radioactive form (125I-BDNF). Using dorsal root ganglion neurons
from chick embryos at 9 d of development, the basic physicochemical
parameters of the binding of 125I-BDNF with its receptors were established.
Two different classes of receptors were found, with dissociation constants
of 1.7 x 10(-11) M (high-affinity receptors) and 1.3 x 10(-9) M
(low-affinity receptors). Unlabeled BDNF competed with 125I-BDNF for
binding to the high-affinity receptors with an inhibition constant
essentially identical to the dissociation constant of the labeled protein:
1.2 x 10(-11) M. The association and dissociation rates from both types of
receptors were also determined, and the dissociation constants calculated
from these kinetic experiments were found to correspond to the results
obtained from steady-state binding. The number of high-affinity receptors
(a few hundred per cell soma) was 15 times lower than that of low-affinity
receptors. No high-affinity receptors were found on sympathetic neurons,
known not to respond to BDNF, although specific binding of 125I-BDNF to
these cells was detected at a high concentration of the radioligand. These
results are discussed and compared with those obtained with nerve growth
factor on the same neuronal populations.
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