ABSTRACT
BACKGROUND: The purpose of this study was to evaluate the effectiveness of multiple hippocampal transections (MHT) in the treatment of drug-resistant mesial temporal lobe epilepsy. METHODS: Six patients underwent MHT at Burdenko Neurosurgery Center in 2018. The age of the patients varied from 18 to 43 years. All patients suffered from refractory epilepsy caused by focal lesions of the mesial temporal complex or temporal pole in dominant side. Postoperative pathology revealed neuronal-glial tumors in two patients, focal cortical dysplasia (FCD) of the temporal pole - in two patients, cavernous angioma - in one patient, and encephalocele of the preuncal area - in one patient. RESULTS: All patients underwent surgery satisfactorily. There were no postoperative complications except for homonymous superior quadrantanopia. This kind of visual field loss was noted in four cases out of six. During the follow-up period five patients out of six had Engel Class I outcome (83.3%). In one case, seizures developed after 1 month in a patient with FCD in the uncus (Engel IVA). After surgery, three out of six patients developed significant nominative aphasia. Two patients relative to the preoperative level demonstrated improvement in delayed verbal memory after MHT. Two patients showed a decrease level in delayed verbal memory. In preoperative period, visual memory was below the normal in one patient. Delayed visual memory in two cases impaired compared to the preoperative level. CONCLUSION: MHT can be considered as an effective method of drug-resistant mesial temporal lobe epilepsy caused by tumors of the medial temporal complex. At the same time, MHT makes it possible to preserve memory in patients with structurally preserved hippocampus. However, MHT do not guarantee the preservation of memory after surgery.
ABSTRACT
Translocation of the tRNA x mRNA complex through the bacterial ribosome is driven by the multidomain guanosine triphosphatase elongation factor G (EF-G). We have used isothermal titration calorimetry to characterize the binding of GDP and GTP to free EF-G at 4 degrees C, 20 degrees C, and 37 degrees C. The binding affinity of EF-G is higher to GDP than to GTP at 4 degrees C, but lower at 37 degrees C. The binding enthalpy and entropy change little with temperature in the case of GDP binding but change greatly in the case of GTP binding. These observations are compatible with a large decrease in the solvent-accessible hydrophobic surface area of EF-G on GTP, but not GDP, binding. The explanation we propose is the locking of the switch 1 and switch 2 peptide loops in the G domain of EF-G to the gamma-phosphate of GTP. From these data, in conjunction with previously reported structural data on guanine nucleotide-bound EF-G, we suggest that EF-G enters the pretranslocation ribosome as an "activity chimera," with the G domain activated by the presence of GTP but the overall factor conformation in the inactive form typical of a GDP-bound multidomain guanosine triphosphatase. We propose that the active overall conformation of EF-G is attained only in complex with the ribosome in its "ratcheted state," with hybrid tRNA binding sites.
