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Journal of Neuroscience, Vol 8, 2438-2446, Copyright © 1988 by Society for Neuroscience
Neuropeptide Y modulates neurotransmitter release and Ca2+ currents in rat sensory neurons
MW Walker, DA Ewald, TM Perney and RJ Miller
Department of Pharmacological and Physiological Sciences, University of Chicago, Illinois 60637.
Using 125I-labeled neuropeptide Y (NPY) and peptide YY (PYY), we
demonstrated the existence of specific receptors for these peptides on rat
dorsal root ganglion (DRG) cells grown in primary culture. Scatchard
analysis of membrane homogenates indicated that the peptides bound to 2
populations of sites, with approximate affinities of 0.08 and 6.5 nM. Only
low levels of binding were detected on sympathetic neurons cultured from
the same animals or on a variety of neuronal clonal cell lines. The binding
of 125I-NPY and 125I-PYY to DRG cell membranes was considerably reduced by
the nonhydrolyzable analog of GTP, Gpp(NH)p. The major effect of Gpp(NH)p
was to reduce the number of lower-affinity NPY binding sites without
altering the number of high- affinity binding sites. NPY potently inhibited
Ca2+ currents recorded under voltage clamp in rat DRG cells. Both the
transient and sustained portions of the Ca2+ current were inhibited. The
inhibitory effects of NPY were completely blocked following treatment of
the cells with pertussis toxin. Depolarization elicited a large influx of
Ca2+ into DRG neurons as assessed using fura-2-based
microspectrofluorimetry. This influx of Ca2+ could be partially inhibited
by NPY. Furthermore, NPY effectively inhibited the depolarization-induced
release of substance P from DRG cells in vitro. Thus, NPY may be an
important regulator of sensory neuron function in vivo.
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