Abstract:
:The origin of afferent somatostatin-containing fibers terminating in medial and ventral parts of the striatum has been investigated by performing various neurochemical and surgical lesions in the rat. Lesions of the anterior hypothalamus, amygdala, and the hippocampal commissure as well as lesions with 6-hydroxydopamine and 5,7-dihydroxytryptamine failed to decrease striatal somatostatin levels. However, thermal coagulation of the globus pallidus or knife-cut lesions performed ventrally to the striatum resulted in significant decreases in striatal somatostatin content. Analysis of the topographical distribution of somatostatin within the striatum after thermal lesions of the globus pallidus as well as after kainic acid-induced seizures revealed a preferential loss of the peptide in medial and ventral portions of the striatum, the site of terminating afferent somatostatin nerve fibers. The data suggest that the striatal afferent somatostatin-containing neurons may originate in the area of the globus pallidus.
journal_name
J Neurochemjournal_title
Journal of neurochemistryauthors
Widmann R,Mensdorff-Pouilly N,Pfaller K,Sperk Gdoi
10.1111/j.1471-4159.1987.tb05748.xsubject
Has Abstractpub_date
1987-06-01 00:00:00pages
1857-61issue
6eissn
0022-3042issn
1471-4159journal_volume
48pub_type
杂志文章abstract::Rat brain succinyl-CoA:3-oxo-acid CoA-transferase (3-oxo-acid CoA-transferase, EC 2.8.3.5), the first committed enzyme in the oxidation of ketone bodies in mitochondria, was purified to apparent homogeneity as judged by polyacrylamide gel electrophoresis. The enzyme has an apparent molecular weight of 90,000 as determ...
journal_title:Journal of neurochemistry
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pub_type: 杂志文章
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pub_type: 杂志文章,评审
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pub_type: 杂志文章
doi:10.1111/j.1471-4159.1983.tb08098.x
更新日期:1983-04-01 00:00:00
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journal_title:Journal of neurochemistry
pub_type: 杂志文章
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更新日期:1991-04-01 00:00:00
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pub_type: 杂志文章
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更新日期:1988-04-01 00:00:00
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journal_title:Journal of neurochemistry
pub_type: 杂志文章
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更新日期:1987-07-01 00:00:00
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journal_title:Journal of neurochemistry
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更新日期:2011-12-01 00:00:00
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