I2-imidazoline binding sites and monoamine oxidase activity in human postmortem brain from patients with Parkinson's disease
Identifieur interne : 001573 ( PascalFrancis/Checkpoint ); précédent : 001572; suivant : 001574I2-imidazoline binding sites and monoamine oxidase activity in human postmortem brain from patients with Parkinson's disease
Auteurs : C. Gargalidis-Moudanos [France] ; N. Pizzinat ; F. Javoy-Agid ; A. Remaury ; A. PariniSource :
- Neurochemistry international [ 0197-0186 ] ; 1997.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Homme.
English descriptors
- KwdEn :
Abstract
I2-imidazoline binding site (I2BS) has been identified with a regulatory site located on a subpopulation of monoamine oxidase (MAO)-A and -B. Previous studies showed a modification of MAO and I2BS in the elderly and in neurodegenerative processes such as Alzheimer's disease. In the present study. we studied the potential modification of I2 binding sites and monoamine oxidases in Parkinson's disease. Putamen and cerebral cortex were collected from 17 normal subjects (79±12 yr) and 16 patients (76 ± 9 yr) affected by Parkinson's disease. In mitochondrial preparations, radioligand binding studies with [3H]idazoxan showed that putamen and frontal cortex express equivalent amount of I2BS. The density and affinity of I2BS were similar in normal subjects (putamen : Bmax = 207 ± 58 fmol/mg of protein, Kd = 10.1 ± 3.4 nM; cerebral cortex: Bmax = 193 ± 54 fmol/mg of protein. Kd=12.8±6.8 nM) and Parkinson's disease patients (putamen: Bmax = 193 ± 60 fmol/mg of proteins Kd = 9.8 ± 4.6 nM: cerebral cortex: Bmax = 199 ± 49 fmol/mg of protein, Kd = 15.9 ± 8.1 nM). The activity of total monoamine oxidase and monoamine oxidase B, measured by [14C]tyramine and ['4C]phenylethylamine oxidations respectively, were higher in putamen than in cerebral cortex. No differences have been detected in the enzyme activity between normal and pathological subjects. These data suggest that, although MAO and I2BS may play a role in the development of Parkinson's disease, they are not altered in the chronic phase of this disease.
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-imidazoline binding sites and monoamine oxidase activity in human postmortem brain from patients with Parkinson's disease</title>
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-imidazoline binding sites and monoamine oxidase activity in human postmortem brain from patients with Parkinson's disease</title>
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<term>Enzymatic activity</term>
<term>Human</term>
<term>Imidazoline I2 receptor</term>
<term>Imidazoline receptor</term>
<term>Parkinson disease</term>
<term>Putamen</term>
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<keywords scheme="Pascal" xml:lang="fr"><term>Encéphale</term>
<term>Récepteur imidazoline</term>
<term>Site fixation</term>
<term>Amine oxidase (flavin-containing)</term>
<term>Activité enzymatique</term>
<term>Putamen</term>
<term>Cortex cérébral</term>
<term>Parkinson maladie</term>
<term>Homme</term>
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<front><div type="abstract" xml:lang="en">I<sub>2</sub>
-imidazoline binding site (I<sub>2</sub>
BS) has been identified with a regulatory site located on a subpopulation of monoamine oxidase (MAO)-A and -B. Previous studies showed a modification of MAO and I<sub>2</sub>
BS in the elderly and in neurodegenerative processes such as Alzheimer's disease. In the present study. we studied the potential modification of I<sub>2</sub>
binding sites and monoamine oxidases in Parkinson's disease. Putamen and cerebral cortex were collected from 17 normal subjects (79±12 yr) and 16 patients (76 ± 9 yr) affected by Parkinson's disease. In mitochondrial preparations, radioligand binding studies with [<sup>3</sup>
H]idazoxan showed that putamen and frontal cortex express equivalent amount of I<sub>2</sub>
BS. The density and affinity of I<sub>2</sub>
BS were similar in normal subjects (putamen : B<sub>max</sub>
= 207 ± 58 fmol/mg of protein, K<sub>d</sub>
= 10.1 ± 3.4 nM; cerebral cortex: B<sub>max</sub>
= 193 ± 54 fmol/mg of protein. K<sub>d</sub>
=12.8±6.8 nM) and Parkinson's disease patients (putamen: B<sub>max</sub>
= 193 ± 60 fmol/mg of proteins K<sub>d</sub>
= 9.8 ± 4.6 nM: cerebral cortex: B<sub>max</sub>
= 199 ± 49 fmol/mg of protein, K<sub>d</sub>
= 15.9 ± 8.1 nM). The activity of total monoamine oxidase and monoamine oxidase B, measured by [<sup>14</sup>
C]tyramine and ['4C]phenylethylamine oxidations respectively, were higher in putamen than in cerebral cortex. No differences have been detected in the enzyme activity between normal and pathological subjects. These data suggest that, although MAO and I<sub>2</sub>
BS may play a role in the development of Parkinson's disease, they are not altered in the chronic phase of this disease.</div>
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= 9.8 ± 4.6 nM: cerebral cortex: B<sub>max</sub>
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