Abstract
The distribution of high affinity 125I-neurotensin (NT) binding sites were investigated in the amygdaloid complex of adult humans by means of dry film and emulsion autoradiography. Autoradiograms were analysed quantitatively using [ 125I] standards and an image analyser system, and data obtained were converted to nCi of ligand bound per mg tissue. High densities of 125I-NT binding sites were found in the following amygdaloid structures: the dorsal part of the accessory basal nucleus, the medial part of the cortical nucleus, the lateral subdivision of the central nucleus, the paralaminar nucleus, the amygdalohippocampal transition area and the rostral portions of the anterior amygdaloid area. The ventral part of the accessory basal nucleus, the intercalated cell groups and the remaining parts of the anterior amygdaloid area showed moderate density of NT binding sites, while the medial, basal and lateral amygdaloid nuclei, the lateral part of the cortical nucleus, the medial subdivision of the central nucleus, as well basal and lateral amygdaloid nuclei, the lateral part of the cortical nucleus, the medial subdivision of the central nucleus, as well as the corticoamygdaloid transition area exhibited low densities of 125I-NT binding sites. At microscopic level, silver grains appeared more or less evenly distributed over both neuronal perikarya and the surrounding neuropil. In comparison to NT-immunoreactivity, NT receptors showed mismatching distribution throughout most parts of the amygdala, with the exception of the lateral subdivision of the central nucleus, where NT-immunoreactive perikarya and nerve fibers as well as 125I-NT binding sites were found in high density.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.