Altered striatal dopaminergic metabolism 36 hours after unilateral trauma to the human mesencephalon
- 1 February 1987
- journal article
- research article
- Published by Wolters Kluwer Health in Neurology
- Vol. 37 (2), 322
- https://doi.org/10.1212/wnl.37.2.322
Abstract
Markers of dopaminergic synaptic activity and choline acetyltransferase (CAT) were measured in the putamen and caudate nucleus of a patient who lived 36 hours after a unilateral mechanical lesion of the mesencephalon. After cessation of impulse flow along the nigrostriatal tract, dopamine was elevated, dihydroxyphenylacetic acid was diminished, and CAT and tyrosine hydroxylase activity were enhanced in the putamen ipsilateral to the lesion. [3H]-spiperone binding indicated an increase in D2-dopamine receptor density in the caudate nucleus. These findings indicate that the changed predicted from experimental neurochemical models occur in human nigrostriatal systems.This publication has 8 references indexed in Scilit:
- Determination of tyrosine, tryptophan and their metabolic derivitives by liquid chromatography-electrochemical detection: Application to post mortem samples from patients with Parkinson's and Alzheimer's diseaseLife Sciences, 1985
- THE AUTORECEPTOR CONTROL OF DOPAMINE SYNTHESIS - AN INVITRO AND INVIVO COMPARISON OF DOPAMINE AGONISTS1982
- Supersensitivity time course of dopamine antagonist binding after nigrostriatal denervation: Evidence for early and drastic changes in the rat corpus striatumBrain Research, 1981
- GLUCOSE METABOLISM AND ACETYLCHOLINE SYNTHESIS IN RELATION TO NEURONAL ACTIVITY IN ALZHEIMER'S DISEASEThe Lancet, 1980
- Nigrostriatal lesions enhance striatal 3H-apomorphine and 3H-spiroperidol bindingEuropean Journal of Pharmacology, 1979
- Enhanced dopamine metabolism after small lesions in the midbrain of the ratLife Sciences, 1978
- Biochemical differentiation of amphetamine vs methylphenidate and nomifensine in ratsJournal of Pharmacy and Pharmacology, 1977
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951