• The Korean Journal of Nuclear Medicine
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• v.35 no.3
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• pp.131-141
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• 2001

Purpose: We evaluated the sensitivity of the F-18 FDG PET by visual assessment and statistical parametric mapping (SPM) analysis for the localization of the epileptogenic zones in frontal lobe epilepsy. Materials and Methods: Twenty-four patients with frontal lobe epilepsy were examined. All patients exhibited improvements after surgical resection (Engel class I or II). Upon pathological examination, 18 patients revealed cortical dysplasia, 4 patients revealed tumor, and 2 patients revealed cortical scar. The hypometabolic lesions were found in F-18 FDG PET by visual assessment and SPM analysis. On SPM analysis, cutoff threshold was changed. Results: MRI showed structural lesions in 12 patients and normal results in the remaining 12. F-18 FDG PET correctly localized epileptogenic zones in 13 patients (54%) by visual assessment. Sensitivity of F-18 FDG PET in MR-negative patients (50%) was similar to that in MR-positive patients (67%). On SPM analysis, sensitivity decreased according to the decrease of p value. Using uncorrected p value of 0.05 as threshold, sensitivity of SPM analysis was 53%, which was not statistically different from that of visual assessment. Conclusion: F-18 FDG PET was sensitive in finding epileptogenic zones by revealing hypometabolic areas even in MR-negative patients with frontal lobe epilepsy as well as in MR-positive patients. SPM analysis showed comparable sensitivity to visual assessment and could be used as an aid in the diagnosis of epileptogenic zones in frontal lobe epilepsy.

• Journal of Life Science
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• v.21 no.7
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• pp.1032-1038
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• 2011

Recently identified Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP) consists of an ion channel-like transmembrane domain (VSD) and a phosphatase-like domain. Ci-VSP senses the change of membrane potential by its VSD and works as a phosphoinositide phosphatase by its phosphatase domain. In this study, we present the construction of His-tagged phosphatase-like domain of Ci-VSP, its recombinant expression and purification, and its enzymatic activity behavior in order to examine the biochemical behavior of phosphatase domain of Ci-VSP without interference. We found that Ci-VSP(248-576)-His can be eluted with an elution buffer containing 25 mM NaCl and 100 mM imidazole during His-tag purification. In addition, we found the proper measurement condition for kinetics study of Ci-VSP(248-576)-His against p-nitrophenyl phosphate (pNPP). We measured the kinetic constant of Ci-VSP(248-576)-His at $37^{\circ}C$, pH 5.0 or 5.5, under 30 min of reaction time, and less than $2.0\;{\mu}g$ of protein amount. With these conditions, we acquired that Ci-VSP(248-576)-His has $K_m$ of $354{\pm}0.143\;{\mu}M$, $V_{max}$ of $0.0607{\pm}0.0137\;{\mu}mol$/min/mg and $k_{cat}$ of $0.359{\pm}0.009751\;min^{-1}$ for pNPP dephosphorylation. Therefore, we produced a pure form of Ci-VSP(248-576)-His, and this showed a higher activity against pNPP. This purified protein will provide the road to a structural investigation on an interesting protein, Ci-VSP.