실험적 망상적혈구 증다증에 있어서 산화환원 효소활성의 변동 I : Ⅱ. Glucose 6-phosphate dehydrogenase

박주홍,이근배 朝鮮大學校 附設 醫學硏究所 1991 The Medical Journal of Chosun University Vol.15 No.1

토끼에 Phenylhydrazine을 주사한 후 시일이 경과하는 동안에 채혈한 혈액의 적혈구에서 glucose-6-phosphate dehydrogenase(D-glucose-6-phosphate : oxidoreductase, EC 1. 1. 1. 49)의 총 활성도의 변동과 세포질 및 mitochondria에 함유된 glucose-6-phosphate(G-6-P) dehydrogenase의 활성도의 변화를 관찰하여 다음과 같은 결과를 얻었다. G-6-P dehydrogenase의 활성도의 측정은 Komberg 및 Horecker의 방법에 따랐다. 1. 정상흰쥐 적혈구중의 망상적혈구의 수는 약 2.9%였다. 2. 정상 적혈구의 G-6_P dehydrogenase의 활성도는 약 3.8unit/㎖ RBC였으며 세포질 분획에는 약 99.0%가 mitochondria 분획에 약 1.0%가 분포되어 있었다. 3. Phenylhydrazine 주사후 5~6일이 경과하면 망상적혈구의 수는 최고치에 달하는 바 약 35배의 증가를 보였다. 이때 적혈구내의 G-6-P dehydrogenase의 총 활성도도 최고치에 달하는바, 정상치의 약 1.4배의 증가를 보였다. 총 활성도의 약 97.5%가 세포질 분획에, 약 2.5%가 mitochondria 분획에 증명되었다. 4. 망상적혈구증다증의 유발기에 있어서 G-6-P dehydrogenase의 총 활성도의 증가는 주로 세포질 분획내의 이 효소의 증가에 기인하였다.(Ks=0.0208, Kd=0.0042, t1/2=165.0 hours). 5. Mitochondria 분획내의 isozyme도 정상치의 최고 약 22.1배 증가하였다.(Ks=0.0013, Kd=0.0010, t1/2=69.3 hours). 6. 이 효소의 합성 및 분해속도 상수는 세포질 분획에 있어서는, Ks=0.0123, Kd=0.0464, t1/2=56.3 hours이며 mitochondria 분획에 있어서는, Ks=0.0003, Kd=0.0146, t1/2=47.5 hours 이었다. The activity of glucose 6-phosphate dehydrog-enase(D-glucose 6-phosphate : NADP 1-oxidoreductase, EC 1, 1, 1, 49) isozymes in rat red blood cells were studied during phenylhydrazine-induced reticulocytosis and recovery period from it. Glucose 6-phosphate dehydrogenase activity was assayed by the method of Kornberg and Horecker. The results obtained were as follows: 1. Red blood cells of normal rabbit contained about 2.9% of reticulocytes. 2. Total activity of G-6-P dehydrogenase in normal rat erythrocyte was 3.8 units and the relative activity of cytosolic and mitochondrial isozymes were 99.3% and 0.07% respectively. 3. The reticulocyte count in phenylhydrazine-treated rabbit increased to about 38 times on Day 4, Total G-6-P dehydrogenase activity reached maximal on Day 4, showing about 5.1 units which is about 1.3 fold higher than normal value. The increase in the total G-6-P dehydrogenase activity during induction of reticulocytosis was mostly due to the increase in the activity of cytosolic isozyme (Ks= 0.0208 : Kd=0.0042 ; t1/2=165.0 hours), and partly due to the increse in the activity of the mitochondrial isozyme (Ks=0.0013 ; Kd= 0.0100: t1/2=69.3 hours). 4. The rate constants following recovery from phenylhydrazine treatment were: Ks=0.04 64 : Kd=0.0123 ; t1/2=56.3 hours for cytosolic isozyme and Ks=0.0003 : Kd=0.0146 : t1/2=47.5 hours for mitochondrial isozyme.

5-Fluorouracil이 생쥐 신장조직이 Lactate dehydrogenase와 Glucose-6-phosphate dehydrogenase 활성에 미치는 영향에 관한 조직화학적인 연구

배기원 인제대학교 1983 仁濟醫學 Vol.4 No.1

항암화학요법제의 기본약제로 널리 사용되고 있는 5 -fluorouracil의 투여에 따른 생쥐 신장의 lactate dehydrogenase와 glucose-6-phosphate dehydrogenase 활성변화를 관찰한 결과 투여시간 경과에 따라 현저한 효소환성의 저하를 나타내었다. This experiment was carried out to investigate the effect of 6-fluorouracil on lactate dehydrogenase and glucose-6-phosphate dehydrogenase in mice kidney. The experimental animals were administrated with 5-fluorouracil by intraperitoneal injection and oral administration with single dose of 0.5 mg per individual during four dayg. The activities of lactate dehydrogenase and glucose-6-phosphate dehydrogenase were observed by Chayen's method and Abe's method for histochemical study. The following results were obtained: 1.The lactate dehydrogenase activities began to be decreased from the second day and appeared lower activities at the third and fourth day after the intraperitoneal injection of 5-fluorouracil. In the oral administration, the lactate dehydrogenase activities began to be decreased the third day and appeared lower activities at the fourth day. 2.The activities of glucose-6-phosphate dehydrogenase began to be decreased from the second day and these activities maintained at the third and fourth day after the intraperitoneal injection of 5-fluorouracil. In the oraloadministration, the activities were decreased at the third and fourth day. 3.The decrease of the glucose-6-phosphate dehydrogenase and lactate dehydrogenase activities was marked at the proximal and distal convoluted tubule and the outer zone of medulla.

Mitomycin C가 생쥐 신장조직의 Lactate dehydrogenase와 Glucose-6-phosphate dehydrogenase활성에 미치는 영향에 관한 조직화학적 연구

배기원,양영철 인제대학교 1986 仁濟醫學 Vol.7 No.1

Mitomycin C의 투여로 생쥐 신장의 lactate dehydrogenase와 glucose-6-phosphate dehydrogenase 활성은 투여 시간의 경과에 따라 현저히 저하하였다. This experiment was carried out to investigate the effect of mitomycin C on lactate dehydrogenase and glucose-6-phosphate dehydrogenase in mice kidney. The experimental animals were administered with mitomycin 2mg/kg per individual by intraperitoneal injection during five days. The activities of lactate dehydrogenase and glucose-6-phosphate dehydrogenase were observed by Chayen's method and Abe's method for histochemical study. The following results were obtained: 1.The lactate dehydrogenase activities began to be decreased from the second day. This decrease maintaianed by th fifth and was marked at the proximal and distal tubule, and the outer zone of the medulla. 2.The glucose-6-phosphate dehydrogenase activities began to be decreased from the second day and appeared lower activities at the fourth and fifth day. This decrease was marked at the proximal and distal tubules.

철 화합물을 이용한 당 탈수소화 효소-혈당센서의 연구

최영봉,이정민,김세영,김혁한,Choi, Young-Bong,Lee, Jung-Min,Kim, Samantha Saeyoung,Kim, Hyug-Han 한국전기화학회 2014 한국전기화학회지 Vol.17 No.1

산화/환원 매개체는 혈당 센서의 구성에서 전극과 효소 반응의 전자 전달 매개체로서 중요한 역할을 담당한다. 본 연구에서는 기존의 산화/환원 매개체보다 전자 전달 반응이 용이하며, 높은 민감도를 위해 페레이트에 아닐린을 결합시켜, 1차 아민기를 갖는 $Fe(CN)_5$-aminopyridine를 합성하였다. 합성된 $Fe(CN)_5$-aminopyridine 는 순환 전압 전류 법과 분광학적 방법을 이용하여 합성 결과를 확인하였다. 합성된 물질과 포도당을 측정하기 위한 당 탈 수소 효소를 ITO 전극위에 고정시켜 효소전극을 제작하였고, 또한 신호 증폭을 위하여 금 나노 입자를 함께 고정시켰다. 금 나노 입자가 고정된 효소 전극은 그렇지 않은 전극에 비해 약 2배 가량의 전류 밀도가 증가함을 확인하였다. 만들어진 효소 전극에서 포도당의 농도 별 산화 촉매 전류를 순환 전압 전류 법으로 측정한 결과 0.4 V (vs. Ag/AgCl)에서 전기적 신호가 발생되었으며, 포도당 0~10 mM의 농도 범위에서 전기적 신호가 선형 증가함을 확인할 수 있었다. Redox complexes to transport electrons from enzyme to electrodes are very important part in glucose sensor. Pentacyanoferrate-bound aniline ($Fe(CN)_5$-aminopyridine), was prepared as a potential redox mediator in a glucose dehydrogenase (GDH)-glucose sensor. The synthesized pyridyl-$NH_2$ to pentacyanoferrate was characterized by the electrochemical and spectroscopic methods. A amperometric enzyme-linked electrode was developed based on GDH, which catalyses the oxidation of glucose. Glucose was detected using GDH that was co-immobilized with an $Fe(CN)_5$-aminopyridine and gold nano-particles (AuNPs) on ITO electrodes. The $Fe(CN)_5$-aminopyridine and AuNPs immobilized onto ITO electrodes provided about a two times higher electrochemical response compared to that of a bare ITO electrode. As glucose was catalyzed by wired GDH, the electrical signal was monitored at 0.4 V versus Ag/AgCl by cyclic voltammetry. The anode currents was linearly increased in proportion to the glucose concentration over the 0~10 mM range.

출생 첫날 출현한 황달과 용혈성 빈혈로 내원한 Glucose-6-Phosphate Dehydrogenase 결핍증

김경모 ( Kyung Mo Kim ),이정현 ( Jung Hyun Lee ),전정식 ( Chung Sik Chun ) 대한주산의학회 2006 Perinatology Vol.17 No.1

The most devastating clinical consequence of G-6-PD deficiency is neonatal hyperbilirubinemia which can be severe and result in kernicterus or even death, although glucose-6-phosphate dehydrogenase deficiency is responsible for two clinical syndromes, an episodic hemolytic anemia induced by infections or certain drugs and spontaneous chronic nonspherocytic hemolytic anemia. In the pathogenesis of neonatal hyperbilirubinemia associated with G-6-PD deficiency, decreased elimination of bilirubin has been suspected to be a key factor, because these neonates usually do not develop frank anemia even in the presence of severe hyperbilirubinemia. But, we experienced a glucose-6-phosphate dehydrogenase deficient male patient who showed jaundice and severe hemolytic anemia appearing within the first 24 hour of life. The patient had resolution of symptoms after phototherapy and transfusion. We report this case with a brief review of the related literatures.

Vincristine이 생쥐 신장의 효소활성에 미치는 영향에 관한 조직화학적 연구

양영철 인제대학교 1986 仁濟醫學 Vol.7 No.2

미정맥으로 투여한 vincristine은 생쥐의 근위곡 요세관 상피의 효소활성에 크게 영향을 미쳐 투여 1일 후에는 cytochrome oxidase, lacatate dehyrogenase, glucose-6-phosphate dehydrogenase의 활성이 감소되기 시작하였고 투여 4일 후에는 효소 활성 저하가 현저하였으며, 이때부터 alkaline phosphatase 활성은 저하되기 시작하였고 acid phosphatase의 활성은 증가하기 시작하였다. This experiment was carried out to investigate the effect of vincristine upon renal enzymes in mice. The laboratory animals were administered with single dose of vincristine 0.1mg/kg by the intravenous injection. Histochemical studies observed the activities of cytochrome oxidise, alkaline phosphatase, acid phosphatase, lactate dehydrogenase and glucose-6-phophate dehydrogenase . The following results were obtained: 1.The activities of cytochrome oxidase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase began to be decreased from the 1st day in the proximal tubules. After the 4th day, these decreased were salient and at the 9th day these activities were slightly resilient in the proximal tubules. 2.From the 4th day, the alkaline phosphatase activity began to be decreased and the acid phosphatase activity to be increased, these activities were maintained at the 15th day.

황백 에탄올 추출물의 혈당강하작용

김옥경 한국응용과학기술학회 2020 한국응용과학기술학회지 Vol.37 No.4

Streptozotocin(STZ)을 45mg/kg.b.w의 용량으로 흰쥐의 미정맥에 투여 한 후 당뇨병이 유발된 당뇨 흰쥐에게 1일 1회 7일간 1,000mg/kg,b.w의 용량으로 황백에탄올 추출물을 투여 후 glucose 함량과 당대사에 관여하는 효소인 glucose-6-phosphatase(G-6-Pase), glucose-6-phosphate dehydrogenase(G-6-PDH, glucokinase(GK)활성과 glycogen 함량을 측정한 결과 황백 에탄올 추출물 투여군이 glucose 함량과 G-6-Pase 활성의 유의적인 감소를 나타내었으며 glycogen 함량과 G-6-PDH, GK의 활성은 유의적인 증가를 나타내었다. 이와 같이 황백 에탄올 추출물이 혈당강하 효과를 가졌다. This study was performed to investigate the antidiabetic effect of ethanol extract of Phelladrindron Amurense Rupr (P.A) in Streptozotocin(STZ) induced diabetic rats. Diabetes was induced by intravenous injection of STZ at a dose of 45㎎/㎏,b.w. dissolved in citrate buffer. The ethanol extract of P. A was orally administrated once a day for 7 days at a dose of 1,000㎎/㎏. The content of serum glucose, was significantly decreased in P.A treated group compared to the those of STZ-control group. The content of hepatic glycogen and activities of glucokinase(GK) and glucose-6-phosphate dehydrogenase(G-6-PDH) were significantly increased(p<0.05), and activity of glucose-6-phoshatase(G-6-Pase) was significantly decreased(p<0.05) in P.A treated group compared to those of STZ-control group, These results indicated that ethanol extract of P.A have antidiabetic effect in STZ-induced diabetic rats.

Glucose-6-phosphate dehydrogenase deficiency does not increase the susceptibility of sperm to oxidative stress induced by H₂O₂

Roshankhah, Shiva,Rostami-Far, Zahra,Shaveisi-Zadeh, Farhad,Movafagh, Abolfazl,Bakhtiari, Mitra,Shaveisi-Zadeh, Jila The Korean Society for Reproductive Medicine 2016 Clinical and Experimental Reproductive Medicine Vol.43 No.4

Objective: Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common human enzyme defect. G6PD plays a key role in the pentose phosphate pathway, which is a major source of nicotinamide adenine dinucleotide phosphate (NADPH). NADPH provides the reducing equivalents for oxidation-reduction reductions involved in protecting against the toxicity of reactive oxygen species such as $H_2O_2$. We hypothesized that G6PD deficiency may reduce the amount of NADPH in sperms, thereby inhibiting the detoxification of $H_2O_2$, which could potentially affect their motility and viability, resulting in an increased susceptibility to infertility. Methods: Semen samples were obtained from four males with G6PD deficiency and eight healthy males as a control. In both groups, motile sperms were isolated from the seminal fluid and incubated with 0, 10, 20, 40, 60, 80, and $120{\mu}M$ concentrations of $H_2O_2$. After 1 hour incubation at $37^{\circ}C$, sperms were evaluated for motility and viability. Results: Incubation of sperms with 10 and $20{\mu}M\;H_2O_2$ led to very little decrease in motility and viability, but motility decreased notably in both groups in 40, 60, and $80{\mu}M\;H_2O_2$, and viability decreased in both groups in 40, 60, 80, and $120{\mu}M\;H_2O_2$. However, no statistically significant differences were found between the G6PD-deficient group and controls. Conclusion: G6PD deficiency does not increase the susceptibility of sperm to oxidative stress induced by $H_2O_2$, and the reducing equivalents necessary for protection against $H_2O_2$ are most likely produced by other pathways. Therefore, G6PD deficiency cannot be considered as major risk factor for male infertility.

Glucose and Its Role in Generating Reactive Oxygen Species Required for Mouse Sperm Fertilizing Ability

Lin, S.C.,Chen, M.C.,Huang, A.J.,Salem, B.,Li, K.C.,Chou, K. Asian Australasian Association of Animal Productio 2000 Animal Bioscience Vol.13 No.6

Effects of xanthine (X), xanthine oxidase (XO), and catalase (C), $H_2O_2$, and carbohydrates on sperm capacitation, acrosome reaction, and fertilizing ability in vitro were examined. Glucose alone, but not fructose, supported the maximum rate of sperm capacitation and acrosome reaction. However, in the combination of X, XO, and C (XXOC) or $H_2O_2$, fructose alone also supported maximum capacitation, acrosome reaction, and fertilization. Either insufficient or excessive amounts of $H_2O_2$ decreased sperm capacitation and the acrosome reaction. In order to understand how glucose generates $H_2O_2$ or other reactive oxygen species in sperm cells, 6-aminonicotinamide, an inhibitor of the pentose-phosphate pathway (PPP), and apocynin, an inhibitor of NADPH oxidase, were added to sperm suspensions in glucose-containing medium. Results appeared that sperm capacitation, acrosome reaction, and fertilization were consequently inhibited by either one of these compounds. These inhibitory effects were nullified by addition of XXOC. These results support the hypothesis that glucose, in addition to being a substrate for glycolysis, facilitates sperm capacitation and the acrosome reaction by generating reactive oxygen species through G-6-P dehydrogenase and NADPH oxidase.

Case Reports : Hypohidrotic Ectodermal Dysplasia Associated with Glucose-6-Phosphate Dehydrogenase Deficiency

( Aylin Turel Ermertcan ),( Ali Yasar ),( Tuba Celebi Kayhan ),( Huseyin Gulen ),( Pelin Ertan ) 대한피부과학회 2011 Annals of Dermatology Vol.23 No.1S

Hypohidrotic ectodermal dysplasia (HED) is a syndrome characterized by hypodontia, hypotrichosis, and partial or total ecrine sweat gland deficiency. The most prevalent form of HED is inherited as an X linked pattern. Glucose-6-phosphate dehydrogenase (G-6-PD) deficiency is an X-linked recessive disease, which leads to hemolytic anemia and jaundice. It is expressed in males, while heterozygous females are usually clinically normal. A 12-year-old boy with the complaints of hair and eyebrow disturbances, teeth disfigurement, decreased sweating, and xerosis presented to the outpatient clinic. Dermatological examination revealed sparse hair and eyebrows, conical- shaped teeth, xerosis, syndactylia, transverse grooves, and discoloration of nails. Laboratory findings indicated anemia. His 3-year-old sister also had sparse hair and eyebrows, xerosis, and syndactylia. We learned that the patient had a previous history of neonatal jaundice and a diagnosis of G-6-PD deficiency. Although it has been shown that loci of ectodermal dysplasia and G-6-PD deficiency genes are near to one another, we did not find any case study reporting on occurrence of these two genetic diseases together. With the aspect of this rare and interesting case, the relationship between HED and G-6-PD deficiency was defined. (Ann Dermatol 23(S1) S8~S10, 2011)