Efficacy and Safety of Zolpidem for Focal Dystonia After Neurosurgical Treatments: A Retrospective Cohort Study.

Although there are several reports of the significant efficacy of zolpidem for treating dystonia, zolpidem is still considered an anecdotal treatment. Here, we evaluated the efficacy and safety of zolpidem for treating residual dystonia in patients who previously received various neurosurgical treatments majorly including deep brain stimulation and radiofrequency ablation. We retrospectively reviewed medical records from January 2021 to September 2021 to identify patients with dystonia who had been prescribed zolpidem after undergoing neurosurgery. Twenty patients were enrolled in this study, including those with blepharospasm (two), tongue dystonia (four), mouth dystonia (one), spasmodic dysphonia (two), cervical dystonia (six), focal hand dystonia (three), hemidystonia (two), blepharospasm with cervical dystonia (one), and mouth dystonia with cervical dystonia (one). Single doses of zolpidem ranged between 2.5 and 10 mg, while daily dosages ranged from 10 to 30 mg. The zolpidem dose prescribed was 5-10 mg, with single and daily doses of 7 ± 2.9 and 14.5 ± 6.0 mg, respectively. With zolpidem administration, the participants' Burke-Fahn-Marsden Dystonia Rating Scale-Movement Scale score significantly improved from 8.1 ± 6.7 to 3.7 ± 2.5 (50.6% improvement, p < 0.0001). Improvements in arm dystonia, blepharospasm, and spasmodic dysphonia were observed using the Arm Dystonia Disability Scale, Jankovic Rating Scale, and Voice Handicap Index, respectively. No improvements were observed in cervical dystonia on the Toronto Western Spasmodic Torticollis Rating Scale. Drowsiness, including three cases each of mild and moderate drowsiness, was the most frequent adverse effect (30%), which persisted for 2-3 h. Transient amnesia and rapid eye movement sleep behavior disorder occurred in two patients and one patient, respectively. Although our findings suggest that zolpidem can be a valuable treatment option for patients with residual dystonia after neurosurgical treatments, the beneficial effects for cervical dystonia were limited.

Aggressive internal and external decompression as a life-saving surgery in a deeply comatose patient with fixed dilated pupils after severe traumatic brain injury: A case report.

BACKGROUND: To maximize control of the intracranial pressure in deeply comatose patients with malignant cerebral swelling, combination of the surgical techniques for internal and external brain decompression may be reasonable, as demonstrated in the presented case. CASE DESCRIPTION: A 55-year-old man was admitted with Glasgow Coma Scale (GCS) score 4, maximally dilated pupils, and absence of the pupillary light and vestibulo-ocular reflexes. Head CT revealed massive acute subdural hematoma, prominent brain shift with subfalcine and transtentorial herniation, and diffuse subarachnoid hemorrhage. Large size decompressive craniectomy and evacuation of subdural hematoma were done, however, prominent swelling of the brain and its protrusion through the bone defect remained. Therefore, extensive temporal lobectomy and removal of the bulk of temporal muscle were additionally attained followed by lax duraplasty. Gradual recovery of the patient was noted from the 1st postoperative day, and on the 70th day, his GCS score was 4T4. Three months later, his condition corresponded to the Glasgow Outcome Scale score 3 (severe disability). CONCLUSION: Aggressive internal and external decompression with combination of large size craniectomy, extensive temporal lobectomy, removal of the bulk of temporal muscle, and lax duraplasty should be considered as possible life-saving option in cases of neurosurgical emergencies with malignant cerebral swelling.

Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-ß-d-glucosaminidase activity in Streptomyces coelicolor A3(2).

The dasD gene is located just downstream of the dasABC gene cluster, encoding components of an ABC transporter for uptake of a chitin-degradation product N,N'-diacetylchitobiose [(GlcNAc)(2) ] in Streptomyces coelicolor A3(2). To clarify the roles of the DasD protein in the degradation and assimilation of chitin, we obtained and characterized a recombinant DasD protein and a dasD-null mutant of S. coelicolor A3(2). The recombinant DasD protein produced in Escherichia coli showed N-acetyl-ß-d-glucosaminidase (GlcNAcase) activity and its optimum temperature and pH were 40 °C and 7, respectively. dasD transcription was strongly induced in the presence of chitin, weakly by chitosan, but not by cellulose or xylan in S. coelicolor A3(2). Immuno-blot analysis demonstrated that DasD is a cytoplasmic protein. The dasD-null mutant exhibited cellular GlcNAcase activity which was comparable with that of the parent strain M145. DasD, thus, did not seem to be a major GlcNAcase. Induced extracellular chitinase activity in the dasD-null mutant was, interestingly, higher than M145, in the presence of colloidal chitin or (GlcNAc)(2) . In contrast to M145, (GlcNAc)(2) temporally accumulated in the culture supernatant of the dasD-null mutant in the presence of colloidal chitin.

Enzymatic synthesis of 4-hydroxyphenyl beta-D-oligoxylosides and their notable tyrosinase inhibitory activity.

We have purified and characterized an oligoxylosyl transfer enzyme (OxtA) from Bacillus sp. strain KT12. In the present study, a N-terminally His-tagged recombinant form of the enzyme, OxtA(H)(E), was overproduced in Escherichia coli and applied to the reaction with xylan and hydroquinone to produce 4-hydroxyphenyl beta-D-oligoxylosides, beta-(Xyl)(n)-HQ (n=1-4), by one step reaction. The obtained beta-(Xyl)(n)-HQ inhibited mushroom tyrosinase, which catalyzes the oxidation of L-DOPA to L-DOPA quinine, and the IC(50) values of beta-Xyl-HQ, beta-(Xyl)(2)-HQ, beta-(Xyl)(3)-HQ, and beta-(Xyl)(4)-HQ were 3.0, 0.74, 0.48, and 0.18 mM respectively. beta-(Xyl)(4)-HQ showed 35-fold more potent inhibitory activity than beta-arbutin (4-hydroxyphenyl beta-D-glucopyranoside), of which the IC(50) value was measured to be 6.3 mM. Kinetic analysis revealed that beta-(Xyl)(2)-HQ, beta-(Xyl)(3)-HQ, and beta-(Xyl)(4)-HQ competitively inhibited the enzyme, and the corresponding K(i) values were calculated to be 0.20, 0.29, and 0.057 mM respectively.