A Case of Primary Hepatic Malignant Paraganglioma without Hypertension

Heuy Seong Lee(이희성),Hyung Geun Lee(이형근),Dong Do You(유동도),Jin Seok Heo(허진석),Seong Ho Choi(최성호),Dong Wook Choi(최동욱) 한국간담췌외과학회 2009 한국간담췌외과학회지 Vol.13 No.1

Paraganglioma is an unusual neoplasm that is embryologically derived from neural crest cells. The most common location of this neoplasm is the adrenal medulla, where these tumors are known as pheochromocytoma. It is extremely rare that paragangliomas occur in the liver. There are only 7 reports of primary hepatic paraganglioma. A 56-year-old man was referred to XX Medical Center. Hypertension was not found. He had suffered from jaundice, headache and weight loss for the 4 previous weeks, but hypertension was not present. The total bilirubin was 7.7 mg/dl and the CA19-9 level was 56.3 U/dl. The tumor was diagnosed as intrahepatic cholangiocarcinoma on the computed tomography image. After biliary drainage via endoscopic nasobiliary drainage, surgical exploration was carried out; right trisectionectomy with caudate lobectomy, portal vein resection and anastomosis were then done. The final pathological diagnosis was primary hepatic malignant paraganglioma of the intrahepatic duct. There has been no evidence of recurrence on the follow up CT images during the 24 month follow up period.

Purification and Properties of the Major Isozymic Form of NAD-linked ${\alpha}$-Glycerophosphate Dehydrogenase from Rat Kidney

이동욱,이희성,조성희,Lee, Dong-Wook,Lee, Hee-Sung,Cho, Sung-Hye 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.3

흰쥐 신장의 NAD 의존성 ${\alpha}$-glycerophosphate 탈수소 효소는 4종의 isozyme으로 존재하였고 그들의 등전점은 pH6.9, 6.6, 6.4 및 6.2였다. 이들중 등전점 6.6인 major isozyme을 blue dextran-Sepharose 4B, DEAE-cellulose, Sephadex G-100 chromatography를 통하여 1,078배 정제하였다. Major isozyme의 분자량은 62,000이고, 반응 최적온도와 pH는 각각 55도 및 10.0이었고, 최적온도에서 쉽게 불활성화 되었다. 이 효소는 일가 및 이가 양이온의 첨가에 의해 활성화 되었으며 p-HMB와 iodoacetamide에 의해 활성이 크게 억제되었고, glycerophosphate와 NAD에 대한 Km값은 각각 3.22 및 0.31 mM 이었다. 이들 결과로부터 이 효소의 isozyme pattern은 조직에 따라 다를지라도 major isozyme의 이화학적 성상은 서로 비슷함을 알 수 있었다. NAD-linked ${\alpha}$-glycerophosphate dehydrogenase(EC 1.1.1.8) in rat kidney existed as four different isozymic forms with an isoelectric point at pH 6.9, 6.6, 6.4 and 6.2, respectively. The major isozymic form(PI 6.6) was purified using several chromatographic procedures involving an ion exchange and two affinity chromatography steps. The 1,078 fold purified enzyme was homogeneous, nucleotide free protein. The molecular weight of the major isozyme was 62,000 daltons, the optimal pH and temperature for its catalytic activity were 10.0 and $55^{\circ}C$, respectively. At the optimal temperature this enzyme was rapidly inactivated$(t_{1/2}=1.5min)$. The major isozyme was activated by the addition of cations such as $K^+$, $Na^+$, $Mg^{++}$ or $Ca^{++}$, and was strongly inhibited by alkylating agents such as P-hydroxymercurybenzoate or iodoacetamide. Glycerophosphate oxidation reaction obeyed the Michaelis-Menton behavior with Km values of 3.22 and 0.31 mM for glycerophosphate and NAD, respectively. The data suggest that although the isozyme pattern of NAD-linked ${\alpha}$-glycerophosphate dehydrogenase is quite different by tissue or species of the animal the physico-chemical properties of the major isozymic form are very similar each other except the affinity for substrate and coenzyme.

소나무 꽃가루에서 분리한 Trehalase의 정제 및 성상에 관한 연구

이동욱,이희성,조성희,Lee, Dong-Wook,Lee, Hi-Sung,Cho, Sung-Hee 생화학분자생물학회 1981 한국생화학회지 Vol.14 No.2

소나무 꽃가루를 파쇄하여 Hogeboom (1968)의 방법으로 세포의 각 분획을 분리하였다. 그리고 trehalase의 활성도를 측정하고 세포질 분획의 trehalase 를 ammonium sulfate에 의한 침전, DEAE-cellulose 및 Sephadex G-200 column chromatography를 행하여 정제하였으며 그 성상을 관찰하여 다음과 같은 결론을 얻었다. 1. 소나무 꽃가루에 있는 trehalase 는 cytosol에 약 80% 그리고 mitochondria에 약 4%, nuclei 에 약 10% 함유되어 있었다. 2. 소나무 꽃가루의 세포질 분획에서 이 효소를 81배 정제하였으며, 기질로는 trehalose에 대해서만 활성을 나타냈다. 3. 이 효소활성의 최적 pH 는 5.4였으며, 최적온도는 $60^{\circ}C$였다. 4. 이 효소의 기질에 대한 Km값은 $2.56{\times}10^{-3}M$이었다. 5. 반응 생성물이 glucose임을 paper chromatography에 의해 확인하였다. 6. 양이온이 이 효소에 미치는 영향은 $Na^+$이 $1{\times}10^{-4}{\sim}1{\times}10^{-3}M$농도에서 효소활성도를 약 14~17% 증가시켰으나, 농도의 증가에 따라 억제 현상이 증가되었다. 또 $Mg^{++}$ 경우에도 $1{\times}10^{-5}M{\sim}1{\times}10^{-4}M$ 농도에서 활성도가 27~15% 증가되었으나 농도의 증가에 따라 현저한 억제현상을 보였다. 7. $K^+$, $Ca^{++}$의 경우에는 같은 농도 범위에서 효소활성에 변화가 없었다. 8. 이 효소의 분자량은 약 70,000이었다. Trehalose, the alpha-1,1 linked disaccharide of glucose, occurs widely in nature. This sugar has been isolated from bacteria, yeast, fungi and a number of invertebrates, where it functions as reserve carbohydrate. Trehalase(${\alpha},{\alpha}$-trehalose 1-D-glucohydrolase, EC 3.2.1.28.) responsible for the hydrolysis of trehalose was isolated from pine pollen(Pinus densiflora Siebold) and purified 81 times by DEAE-cellulose column and Sephadex G-200 column chromatography. The activity of trehalase was measured by method of Lapp and Mason. The enzyme activity in pine pollen was detected 80.46% in cytosolic fraction, 4.09% in mitochondria) fraction and 10.33% in nucleic fraction. The pH optimum for enzymatic activity was found to be 5.4 and optimal temperature was $60^{\circ}C$ and the Km value for trehalose was estimated to be about $2. 56{\times}10^{-3}M$. The product of reaction was identited as D-glucose by paper chromatographic method. The trehalase activity was activated as much as 14∼17% by $1{\times}10^{-4}M{\sim}1{\times}10^{-3}M$ concentration of $Na^+$, and 27~15% by $1{\times}10^{-5}M{\sim}1{\times}10^{-4}M$ of $Mg^{++}$, and the other cations($K^+$, $Ca^{++}$) were tested for their abillity to replace $Mg^{++}$, but none was effective. The molecular weight of trehalase was estimated to be approximately 70,000 by Sephadex G-200 gel filtration.

소나무 꽃가루에서 분리한 Trehalase 의 정제 및 성상에 관한 연구

이동욱,이희성,조성희 ( Dong Wook Lee,Hi Sung Lee,Sung Hee Cho ) 생화학분자생물학회 1981 BMB Reports Vol.14 No.2

Trehalose, the alpha-1, 1 linked disaccharide of glucose, occurs widely in nature. This sugar has been isolated from bacteria, yeast, fungi and a number of invertebrates, where it functions as reserve carbohydrate. Trehalase(α,α-trehalose 1-D-glucohydrolase, EC 3. 2. 1. 28. ) responsible for the hydrolysis of trehalose was isolated from pine pollen(Pinus densiflora Siebold) and purified 81 times by DEAE-cellulose column and Sephadex G-200 column chromatography. The activity of trehalase was measured by method of Lapp and Mason. The enzyme activity in pine pollen was detected 80.46% in cytosolic fraction, 4.09% in mitochondria) fraction and 10.33% in nucleic fraction. The pH optimum for enzymatic activity was found to be 5.4 and optimal temperature was 60℃ and the Km value for trehalose was estimated to be about 2. 56 × 10^(-3)M. The product of reaction was identited as D-glucose by paper chromatographic method. The trehalase activity was activated as much as 14∼17% by 1 × 10^(-4)M∼1 × 10^(-3)M concentration of Na^+, and 27∼15% by 1 × 10^(-5)∼1 × 10^(-4)M of Mg^(++), and the other cations(K+, Ca++) were tested for their abillity to replace Mg^(++), but none was effective. The molecular weight of trehalase was estimated to be approximately 70,000 by Sephadex G-200 gel filtration.

흰쥐 신장의 NAD 의존성 α - glycerophosphate 탈수소 효소의 정제 및 성상

이동욱,이희성 ( Dong Wook Lee,Hee Sung Lee,Sung Hye Cho ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.3

NAD-linked α-glycerophosphate dehydrogenase(EC 1.1.1.8) in rat kidney existed as four different isozymic forms with an isoelectric point at pH 6.9, 6.6, 6.4 and 6.2, respectively. The major isozymic form(PI 6.6) was purified using several chromatographic procedures involving an ion exchange and two affinity chromatography steps. The 1,078 fold purified enzyme was homogeneous, nucleotide free protein. The molecular weight of the major isozyme was 62,000 daltons, the optimal pH and temperature for its catalytic activity were 10.0 and 55℃, respectively. At the optimal temperature this enzyme was rapidly inactivated(t_(1/2) = 1.5 min). The major isozyme was activated by the addition of cations such as K^+, Na^+, Mg^(++) or Ca^(++), and was strongly inhibited by alkylating agents such as P-hydroxymercurybenzoate or iodoacetamide. Glycerophosphate oxidation reaction obeyed the Michaelis-Menton behavior with Km values of 3.22 and 0.31 mM for glycerophosphate and NAD, respectively. The data suggest that although the isozyme pattern of NAD-linked α-glycerophosphate dehydrogenase is quite different by tissue or species of the animal the physico-chemical properties of the major isozymic form are very similar each other except the affinity for substrate and coenzyme.

매우 얇은 치조골에서 치조능 분할 확장술을 통한 임플란트 치료

김신근(Sin-Guen Kim),이희성(Hee-Sung Lee),박종욱(Jong-Wook Park),남종훈(Jong-Hoon Nam),복성철Sung-Cheol Bok),박기남(Ki-Nam Park),최동주(Dong-Ju Choi) 대한구강악안면외과학회 2011 대한구강악안면외과학회지 Vol.37 No.3

For implant treatment there must be sufficient bone to house the implant body. At least 5mm wide residual bone is needed and usually a 6mm width is preferred by clinicians. However, surgeons sometimes find patients with a narrow ridge, which makes it difficult to place an implant. Therefore, many clinicians perform bone graft or a ridge splitting technique to overcome these poor conditions. The time and cost can be reduced using the ridge splitting technique with immediate implant placement. Recently, many studies reported reliable consequences of ridge splitting technique. This paper reports a successful of implant placement with a ridge splitting technique in a very thin alveolar ridge.

간질(Fasciola hepatica)의 Branched Chain 아미노산 Aminotransferase의 정제 및 성상

이중호(Jung Ho Lee),이동욱(Dong Wook Lee),이희성(Hi Sung Lee),송철용(Chul Yong Song) 대한기생충학열대의학회 1983 The Korean Journal of Parasitology Vol.21 No.1

Detergent가 NAD의존성 α-glycerophosphate 탈수소효소에 미치는 영향

박수언,이동욱,이희성 중앙대학교 의과대학 의과학연구소 1984 中央醫大誌 Vol.9 No.3

The physical properties and the effects of detergent on the activities of purified NAD-linked a-glycerophosphate dehydrogenase(EC 1.1.1.8, GPDH) from kidney, liver and skeletal muscle of the rat were studied. The activity of this enzyme was measured by the method of White and Kaplan. The enzyme activity of liver (9.65 units/g tissue) was higher than those of other organs, but the highest value of the specific activity was shown in skeletal muscle as 0.058 unit/㎎ protein. These enzymes were purified approximately 167, 286 and 216-fold from kidney, liver and skeletal muscle, respectively, by ammonium sulfate saturation and blue dextran Sepharose column chromatography. These enzymes were composed of two isozymes which have different isoelectric points. Isoelectric points of the two isozymes were 6.5 and 6.7, and the molecular weights were 62,000 and 60,000 daltons. The UV spectrums of the purified enzymes from three organs of the rat showed very simillar pattern. But the representative compounds from three classes of detergents showed different effects on these enzymes. The enzyme of the skeletal muscle was activated by all of the detergents which were studied expect for Triton X-100, whereas the enzymes of the kidney and the liver were not activated or strongly inhibited by all of the detergents. In conclusion, the purified a-glycerophosphate dehydrogenases from the three organs of the rat were the homogeneous proteins out of consideration for physical properties. But the differences in the interaction between enzymes and detergents revealed that there are unsimilarities in the three dimentional structure between the skeletal muscle and those of other two organs inspite of similarities between the enzyme of kidney and that of liver.

Uncoupler를 투여한 흰쥐의 뇌와 간조직의 Superoxide Dismutase에 관한 연구

오창학,이동욱,이희성 중앙대학교 의과대학 의과학연구소 1985 中央醫大誌 Vol.10 No.3

The activities of superoxide dismutases, and the variation of superoxide radicals and hydrogen peroxide contents in the brain and liver tissues, and some of the classic signs of rats administered with either 2, 4-dinitrophenol or arsenate has been investigated. Superoxide dismutase activities were determined either by the method of McCord and Fridovich(1969) or by the method of Crapo et al, (1978). The contents of hydrogen peroxide was determined according to the method of Thruman et al, (1972). The experimental results were summarized as follows; 1. Body weights of animals administered with 2, 4-dinitrophenol and/or arsenate were decreased, but the rectal temperatures of animals treated rose above the normal when compared with those of control group. 2. Formation of superoxide radicals in the tissues of brain and liver of 2, 4-dinitrophenol treated animals was increased to each 1.5 and 1.3 times those of the control group. However, formation of superoxide radicals in the tissues of animals administered with arsenate was not changed in the brain tissues, but significantly decreased in the liver tissues. 3. The contents of hydrogen peroxide was slightly increased in both brain and liver tissues of animals administered with 2, 4-dinitrophenol, but no changes occured in those tissues of animals administered with arsenate. 4. The specific activity of total superoxide dismutase in the brain tissues of animals administered with 2,4-dinitrophenol was enhanced up to 1.7 times that of the control group, but when treated with arsenate, the specific activity was closed to that of the control group. 5. The specific activities of total superoxide dismutase in the liver tissues of animals treated with 2,4-dinitrophenol and/or arsenate were 4.68 and 3.77, respectively. 6. The activities of Mn-superoxide dismutase in the brain and liver tissues of animals treated with 2,4-dinitrophenol was increased to 2.2 and 2.0 times as higher as that of the control group, but no significant change in the activity of Cu,Zn-superoxide dismutase was observed, whereas in the case of arsenate treated animals, no changes in the specific activities of Cu,Zn- and Mn-superoxide dismutase was observed. These results indicated that an uncoupler 2,4-dinitrophenol which may act on all the sites of oxidative phosphorylation caused to increase the superoxide radicals in the cells, and this might occur at State 4. A parallel increment of the formation of superoxide radicals and Mn-superoxide dismutase activities would suggest that the enzyme, especially Mn-superoxide dismutase, must be an important factor to protect the mitochondria from the toxicity by superoxide radicals.

Phenylhydrazine으로 유발된 빈혈에 대한 방어기전으로서의 Superoxide Dismutase의 역할

이광재,권년수,이동욱,이희성 중앙대학교 의과대학 의과학연구소 1983 中央醫大誌 Vol.8 No.3

Cytotoxic superoxide radical(O_2^-) is a common intermediate of oxygen reduction in the respiring cells and therefore these cells should be protected against the cytotoxic effects of superoxide radicals. Superoxide dismutase(EC 1.15.1.1) is an enzyme that makes a defence against the toxicity of superoxide radical. At present time, three types of superoxide dismutase(SOD), copper and zinc-containing, manganese containing and iron containing enzyme, have been isolated from both eukaryotic and prokaryotic cells. In this study, we have carried out an experiment to establish the general patterns of cynthesis and degradation of SOD in rabbit that was induced hemolytic anemia by phenylhydrazine and normal, sequential measurements of activity of SOD in the cytosolic and mitochondrial fraction of normal and phenylhydrazine treated rabbits were conducted. The kinetic study of rabbit red blood cell(RBC) during cytodifferentiation provides a unique system which permitted a comparison of the isozymes' turnover rates in vivo. Also, in order to observe the role of SOD as protecting mechanism against O_2^- radicals in this experimental system, these data were treated according to kinetic method of the Kopelovich. The activity of SOD was measured by the method of McCord and Fridovich. The experimental results are summarized as follows; 1. The activity of cytosolic and mitochondrial SOD of normal rabbit RBC was 42 units and 1.5 units per ml RBC, respectively. 2. The reticulocyte counts of normal rabbit RBC was approximately 2.5% and administration of phenylhydrazine resulted in rapid and profound reticulocytosis, i.e., about 63.5% on day 6 and essentially 100% on day 7. 3. The hematocrit of normal rabbit blood was 36%, but after treatment of phenylhydrazine, it was decreased to 20.2% in the value on 4th day. 4. In the phenylhydrazine treated rabbit RBC, activity of cytosolic SOD was maximal on day 5, about 108 units per ml RBC which is about 2.6 fold higheh than the normal value. At induction period, rate constants of synthesis(K_s) and degradation(K_d) were 3.9312 and 0.0364, respectively, the half life was 19.04hrs. K_s and K_d following recovery from phenylhydrazine treatment were 0.5781 and 0.0141, respectively, and the half life was 49.0hrs. 5. The activity of mitochondrial SOD was maximal on day 5, about 5.5 fold higher than the normal value. During induction period, rate constants of synthesis and degradation were 0.1640 and 0.0200, respectively, and the half lief was 34.65 hrs K_s and K_d following recovery from phenylhydrazine treatment were 0.0384 and 0.0256, respectively, and the half life was 27.1 hrs.