Brain neurotransmitter receptors after long-term haloperidol: dopamine, acetylcholine, serotonin, alpha-noradrenergic and naloxone receptors.
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Biomedical subjects
Publications and source records attributed to P Muller.
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Spontaneous spinal extradural hematoma is an uncommon but reversible cause of acute paraplegia. Only 44 cases have been reported in the English literature. This paper adds two cases and analyzes the data in previous case reports to identify prognostic factors. Patients with a history of trauma or an incomplete myelographic block have a good prognosis. In most patients no cause of bleeding is found at operation.
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To investigate the extent of cholinergic involvement in opiate-induced catalepsy, the effects of three anticholinergic drugs were studied on morphine-induced catalepsy. Haloperidol-induced catalepsy was also examined. Maximum catalepsy in rats was obtained with 30 mg/kg morphine or 3 mg/kg haloperidol. The anticholinergic drugs atropine, benztropine, and scopolamine were unable to antagonize morphine-induced catalepsy, yet readily antagonized haloperidol-induced catalepsy. Low doses of apomorphine (7.5 mg/kg), on the other hand, readily antagonized morphine catalepsy, but 13-fold higher doses of apomorphine were needed to block haloperidol-induced catalepsy. The results are compatible with the idea that catalepsy can be mediated via the striatum or the amygdala; morphine-dopamine antagonism may occur in the amygdala, whereas morphine-dopamine-cholinergic interactions occur in the striatum.
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By single intraarticular injection of lectin from Lens culinaris in nosenitized rabbits acute and chronic arthritis was produced. By use of fluoresceinisothiocyanate-labelled lectin binding of lectin could be demonstrated in the connective tissue of joint capsule for 4 weeks. The morphological features of lectin-arthritis were described. The results are discussed with respect to the pathogenesis of the arthritis.
Treatment by urea of purified rat liver cystathionase (L-Cystathionine cysteine-lyase (deaminating), EC 4.4.1.1) provoked a similar alteration of two activities of the enzyme, namely cysteine desulfhydration and homoserine deamination. Since the decreases of the two activities were also comparable as a result of chymotrypsin digestion of the enzyme, these observations suggest that the two sites responsible for the one and the other activites are in close proximity. Studies of the effect of derivatives of substrates (S-carboxymethylcyste-ine, S-carboxyethylcysteine, S-carboxymethylhomocysteine and S-carboxyethylhomocysteine) on both activities were performed. All of them inhibited cysteine desulfhydration and homoserine deamination; in several cases, the type of inhibition was also determined. The results are in agreement with the hypothesis that each of the two sites of the active center has, at least, three binding points which "recognise" groupings of substrates or of inhibitors, and this led us to propose a model for the active center. Each site has an -NH-2 binding point, hence the active center has two -NH-2 binding points; therefore, as cystathionase consists of four subunits and contains four molecules of pyriodoxal phosphate, it might be of interest to determine whether the smallest active molecule is the dimer.
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