Szigethy E, Wenk G L, Beaudet A
Montreal Neurological Institute, McGill University, Quebec, Canada.
Peptides. 1988 Nov-Dec;9(6):1227-34. doi: 10.1016/0196-9781(88)90186-6.
We have previously shown by combined radioautography and acetylcholinesterase histochemistry that the distribution of 125I-neurotensin (NT) binding sites was in register with that of cholinergic neurons in the rat nucleus basalis magnocellularis (NBM). The present study utilized three experimental approaches to elaborate on the type and cellular localization of NT binding sites in the NBM. Competition studies using levocabastine, a selective blocker of the low affinity NT binding component, revealed that most of the 125I-NT binding sites labeled in the NBM are of the levocabastine-insensitive high affinity type, known to correspond to the physiologically active receptor. Ibotenic acid-induced lesions of the NBM produced a marked reduction in both cholinesterase reactivity and cellular 125I-NT binding suggesting that most of the labeled sites are associated with the cholinergic neurons themselves rather than with an afferent input to those cells. Finally, examination of the high resolution radioautographic distribution of 125I-NT binding sites in semithin sections revealed that a proportion of 125I-NT-labeled receptors is associated with the plasma membrane of magnocellular perikarya and proximal processes, thereby providing an anatomical substrate for a local action of NT in the NBM.
