Neurotensin, a central nervous system peptide: apparent receptor binding in brain membranes

George R. Uhl; James P. Bennett; Solomon H. Snyder

doi:10.1016/0006-8993(77)90277-3

Neurotensin, a central nervous system peptide: apparent receptor binding in brain membranes

George R. Uhl, James P. Bennett, Solomon H. Snyder

School of Medicine

Research output: Contribution to journal › Article › peer-review

171 Scopus citations

Abstract

Neurotensin, a tridecapeptide recently isolated from bovine hypothalami, has potent pharmacologic effects in several peripheral systems and a regional distribution in rat brain suggestive of a specialized function. ¹²⁵I-neurotensin binds to membrane preparations from rat brain saturably, reversibly, and with high affinity (apparent K_{D = 3 nM}) under conditions that minimize degradation of the polypeptide. This binding is displaced by neurotensin sequence fragments with relative potencies generally paralleling their potencies in peripheral systems. ¹²⁵I-neurotensin binding is highest in specific thalamic, cerebral cortical, and hypothalamic areas of rat and calf brain. White matter, brain stem and cerebellar regions have substantially lower amounts of binding. Characteristics of this binding suggest an association with a physiologically relevant neurotensin receptor.

Original language	English (US)
Pages (from-to)	299-313
Number of pages	15
Journal	Brain research
Volume	130
Issue number	2
DOIs	https://doi.org/10.1016/0006-8993(77)90277-3
State	Published - Jul 15 1977

ASJC Scopus subject areas

General Neuroscience
Molecular Biology
Clinical Neurology
Developmental Biology

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@article{e1bb623d8fdf4bc28aa69afc22193e72,

title = "Neurotensin, a central nervous system peptide: apparent receptor binding in brain membranes",

abstract = "Neurotensin, a tridecapeptide recently isolated from bovine hypothalami, has potent pharmacologic effects in several peripheral systems and a regional distribution in rat brain suggestive of a specialized function. 125I-neurotensin binds to membrane preparations from rat brain saturably, reversibly, and with high affinity (apparent KD = 3 nM) under conditions that minimize degradation of the polypeptide. This binding is displaced by neurotensin sequence fragments with relative potencies generally paralleling their potencies in peripheral systems. 125I-neurotensin binding is highest in specific thalamic, cerebral cortical, and hypothalamic areas of rat and calf brain. White matter, brain stem and cerebellar regions have substantially lower amounts of binding. Characteristics of this binding suggest an association with a physiologically relevant neurotensin receptor.",

author = "Uhl, {George R.} and Bennett, {James P.} and Snyder, {Solomon H.}",

note = "Funding Information: This research was supported by USPHS Research Grant DA-00266, a Research Scientist Development Award, MH-33128 (S.H.S.) and a USPHS Training Grant I-T01-GM-02191 (G.R.U.). We wish to thank Dr. Morley Hollenberg for bringing neurotensin to our atten- Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1977",

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doi = "10.1016/0006-8993(77)90277-3",

language = "English (US)",

volume = "130",

pages = "299--313",

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T1 - Neurotensin, a central nervous system peptide

T2 - apparent receptor binding in brain membranes

AU - Uhl, George R.

AU - Bennett, James P.

AU - Snyder, Solomon H.

N1 - Funding Information: This research was supported by USPHS Research Grant DA-00266, a Research Scientist Development Award, MH-33128 (S.H.S.) and a USPHS Training Grant I-T01-GM-02191 (G.R.U.). We wish to thank Dr. Morley Hollenberg for bringing neurotensin to our atten- Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1977/7/15

Y1 - 1977/7/15

N2 - Neurotensin, a tridecapeptide recently isolated from bovine hypothalami, has potent pharmacologic effects in several peripheral systems and a regional distribution in rat brain suggestive of a specialized function. 125I-neurotensin binds to membrane preparations from rat brain saturably, reversibly, and with high affinity (apparent KD = 3 nM) under conditions that minimize degradation of the polypeptide. This binding is displaced by neurotensin sequence fragments with relative potencies generally paralleling their potencies in peripheral systems. 125I-neurotensin binding is highest in specific thalamic, cerebral cortical, and hypothalamic areas of rat and calf brain. White matter, brain stem and cerebellar regions have substantially lower amounts of binding. Characteristics of this binding suggest an association with a physiologically relevant neurotensin receptor.

AB - Neurotensin, a tridecapeptide recently isolated from bovine hypothalami, has potent pharmacologic effects in several peripheral systems and a regional distribution in rat brain suggestive of a specialized function. 125I-neurotensin binds to membrane preparations from rat brain saturably, reversibly, and with high affinity (apparent KD = 3 nM) under conditions that minimize degradation of the polypeptide. This binding is displaced by neurotensin sequence fragments with relative potencies generally paralleling their potencies in peripheral systems. 125I-neurotensin binding is highest in specific thalamic, cerebral cortical, and hypothalamic areas of rat and calf brain. White matter, brain stem and cerebellar regions have substantially lower amounts of binding. Characteristics of this binding suggest an association with a physiologically relevant neurotensin receptor.

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JO - Brain research

JF - Brain research

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ER -

Neurotensin, a central nervous system peptide: apparent receptor binding in brain membranes

Abstract

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