Proceedings: An abnormality of secondary energy resources in epileptogenic human brain.
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Biomedical subjects
Publications and source records attributed to A L Sherwin.
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A specific antiserum against skeletal muscle creatine phosphokinase has been obtained by immunizing chickens with purified rabbit skeletal muscle creatine phosphokinase. The antiserum was organ- rather than species-specific and reacted equally well with creatine phosphokinase from rabbit, guinea pig, and human skeletal muscle. Immunological specificity was verified by double immunodiffusion in agar gel where the precipitin line exhibited creatine phosphokinase activity. In solution the antiserum inhibited the enzymatic activity of creatine phosphokinase. By means of the immunofluorescent technique, creatine phosphokinase was localized in the intermyofibrillar space of normal human skeletal muscle fibers in cryostat sections. A higher concentration of the enzyme was found in fibers which have primarily an anaerobic enzyme profile (type II fibers) as determined by conventional histochemical reactions.
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We measured the activities of the cholinergic marker synthetic and catabolic enzymes choline acetyltransferase (ChAT) and acetylcholinesterase (AChE) in surgical specimens obtained from 38 patients immediately following anterior temporal lobectomy for intractable epilepsy. Samples from patients with actively spiking lateral temporal cortex were compared to non-spiking lateral temporal cortex obtained from patients in whom the epileptic discharges were confined to the hippocampus. Mean activities of ChAT and AChE were increased by 25% (P less than 0.01) and 30% (P less than 0.025) respectively in the spiking vs. non-spiking cortex. We suggest that the above-normal activity of these cholinergic marker enzymes may reflect sprouting of cholinergic nerve terminals in spontaneously spiking cortex of some patients and/or increased acetylcholine metabolism secondary to the stimulatory effect of the ongoing epileptic discharge.
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The cholecystokinin (CCK) content of temporal cortex, obtained at neurosurgery from 22 patients with temporal lobe epilepsy, was measured by a specific radioimmunoassay. Tissue immunoreactivity was identified as authentic sulfated CCK-8 by reverse phase high performance liquid chromatography. Several samples were also analyzed by RNA blot hybridization for preproCCK mRNA. The CCK content of cortical tissue from which active epileptic spiking was recorded at the time of surgery (11 patients) was significantly decreased (20% lower) in comparison to tissue samples from a second group of 11 patients in whom the lateral temporal cortex was electrographically free of epileptiform spikes. These data suggest that the decrease may be due to continuous release of CCK as a result of abnormal neuronal firing within the focus. This hypothesis may also be consistent with our observation of a slight increase (67%) in preproCCK mRNA in the actively spiking group compared to the non-spiking cortical samples.
Plasma diatrizoate concentrations during computed cranial tomography were measured by UV spectrophotometry in 14 patients. A loading dose of 0.82 mg diatrizoate/kg followed by a stead infusion of 0.01 mg/kg was required to attain and maintain plasma concentrations of approximately 400 mg/100 ml. Lowering the beam energy resulted in a substantial increase in the EMI numbers of diatrizoate and significant improvement in the delineation of contrast containing lesions. A contrast index estimating the volume of pixel containing diatrizoate was calculated for five diagnosed lesions and this factor appears to be related to vascularity and extravasation.