High-affinity neurotensin binding sites in differentiated neuroblastoma N1E115 cells.

Abstract:

:This paper describes the interaction of neurotensin with mouse neuroblastoma N1E115 cells. Neurotensin binding sites are undetectable in nondifferentiated neuroblastoma cells. They appear during cell differentiation in the presence of a low serum concentration and dimethyl sulfoxide, and reach a maximal level after 50-60 h of incubation under these conditions. The binding of monoiodo[Trp11]neurotensin to homogenates of differentiated N1E115 cells is specific, saturable, and reversible. The interaction is characterized by a dissociation constant of 150 pM and a maximal binding capacity of 9 fmol/mg of protein at 0 degrees C, pH 7.5. These binding parameters, as well as the specificity toward a series of neurotensin analogues, are similar for neurotensin receptors in N1E115 cells and for the high-affinity binding sites that had been previously characterized in rat brain synaptic membranes by means of the same radiolabeled ligand. The presence of high-affinity binding sites for neurotensin in the neuroblastoma N1E115 provides a useful model to study the cellular responses that are generated by the association of neurotensin to its receptor in electrically excitable cells.

journal_name

J Neurochem

authors

Poustis C,Mazella J,Kitabgi P,Vincent JP

doi

10.1111/j.1471-4159.1984.tb12715.x

subject

Has Abstract

pub_date

1984-04-01 00:00:00

pages

1094-100

issue

4

eissn

0022-3042

issn

1471-4159

journal_volume

42

pub_type

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