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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 299-313 |
| Number of pages | 15 |
| Journal | Brain Research |
| Volume | 130 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jul 15 1977 |
Fingerprint
ASJC Scopus subject areas
- Developmental Biology
- Molecular Biology
- Clinical Neurology
- Neuroscience(all)
Cite this
Neurotensin, a central nervous system peptide : apparent receptor binding in brain membranes. / Uhl, George R.; Bennett, James P.; Snyder, Solomon H.
In: Brain Research, Vol. 130, No. 2, 15.07.1977, p. 299-313.Research output: Contribution to journal › Article
}
TY - JOUR
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
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.
UR - http://www.scopus.com/inward/record.url?scp=0017741018&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017741018&partnerID=8YFLogxK
U2 - 10.1016/0006-8993(77)90277-3
DO - 10.1016/0006-8993(77)90277-3
M3 - Article
C2 - 884526
AN - SCOPUS:0017741018
VL - 130
SP - 299
EP - 313
JO - Brain Research
JF - Brain Research
SN - 0006-8993
IS - 2
ER -