Uhl G R, Bennett J P, Snyder S H
Brain Res. 1977 Jul 15;130(2):299-313. doi: 10.1016/0006-8993(77)90277-3.
Neurotensin, a tridecapeptide recently isolated from bovine hypothalamia, 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 revelant neurotensin receptor.
