전형적인 DISIDA scan 소견의 Rotor 증후군 1예

황의태,염동한,권지혜,임종주,최창수,김태현,김학철 圓光大學校 醫科學硏究所 2008 圓光醫科學 Vol.23 No.2

만성의 비용혈성 직접형 고빌리루빈혈증은 Rotor 증후군과 Dubin-Johnson 증후군의 특징적인 소견으로, Rotor 증후군은 드문 양성 유전성 질환이며, Dubin-Johnson 증후군과 감별을 필요로 한다. 본 저자들은 황달을 주소로 내원한 26세 남자 환자에서 고빌리루빈혈증에 대한 검사를 시행하여 담도폐쇄 소견없이 간담도 스캔상 전형적인 Rotor 증후군의 소견 즉, 강한 심장 배후방사능이 지속되면서, 간담도계의 조영은 지연 촬영에서도 관찰되지 않으며 신장으로의 배설이 계속 관찰되는 특징적인 소견과 정상 간조직 검사 결과로 Rotor 증후군으로 진단한 1예를 경험하였기에 문헌 고찰과 함께 보고하는 바이다. Chronic nonhemolytic conjugated hyperbilirubinemia characterizes both Rotor and Dubin-Johnson syndromes. Rotor syndrome is a rare, benign familial disorder and needs to be differentiated from Dubin-Johnson syndrome. Cholescintigraphy is a simple and informative procedure for the diagnosis, which can differentiate Rotor syndrome from Dubin-Johnson syndrome. A 26-year-old man was admitted due to asymptomatic persistent jaundice. Physical examination revealed icteric sclera without hepatosplenomegaly. Laboratory findings showed increased serum bilirubin with direct bilirubinemia. Markedly decreased hepatic uptake and poor visualization of the gallbladder and biliary tract were shown in ^(99m)Tc-DISIDA scan. Histology of the liver showed no diagnostic abnormality without pigmentation. But, we report a case of Rotor syndrome that showed characteristic cholescintigraphic findings with normal urinary total coproporphyrin excretion.

열공형과 비열공형 피질하 혈관성 치매에서 위험인자의 차이에 관한 비교 연구

배희준,정지향,유경호,나덕렬,김상윤,최경규,양동원,손의주,이상도,김재우,박경원,김응규,이재홍,박미영,한일우,함동석,최문성,하충건,최성혜,이애영,이병철,한설희 대한치매학회 2003 Dementia and Neurocognitive Disorders Vol.2 No.2

Backgrounds and Objectives: Vascular dementia is a group of dementing disoders arising from various stroke syndrome. Among these. subcortical ischemic vascular dementia (SIVD) is regarded as a relatively distinct clinical entity. However, MRI patterns of SIVD are not homogenous. In some patients, lacunes are dominant, and in others, subcortical white matter changes are. This study was designed to compare risk factor profiles between SIVD with and without multiple lacunes. Methods: We divided 47 subjects (22 males, mean age. 68 years) recruited from VADAPET (Multicenter Trial For Evaluation Of The Changes In the PET Images Of Subcortical Vascular Dementia Patient) study into two groups one with more than 5 lacunes in deep gray matter (lacune group) and the other with 5 or less(non-lacune group) Clinical characteristics and laboratory findings of two groups were compared. Results: Nineteen of 47 patients (40%) belonged to the lacune group. The lacune and non-lacune groups d d not differ in the following variables: age, hypertension, diabetes mellitus, hyperlipidemia heart disease, history of stroke or TIA, history of trauma or major surgery, family history of hypertension stroke, or dementia, age at diagnosis of dementia, body mass index, white blood cell count, ESR, CRP, fibrinogen, hemoglobin A1C, total cholesterol. LDL cholesterol creatinine, proteinuria, glucosuria, and microhematuria. However, male sex, smoking alcohol. hemoglobin, and HDL cholesterol were possibly associated more with lacune group SIVD than with non-lacune group (p<0 1) Multivariate analyses revealed that smoking, hemoglobin, and HDL cholesterol were independent predictors of SIVD with multiple lacunes Conclusion: Our study suggests that SIVD with multiple lacunes may be significantly different in smoking habits hemoglobin, and HDL cholesterol from SIVD without multiple lacunes.

Hsp72 : a natural inhibitor of the stress-activated signaling

Choi, Eui-Ju 이화여자대학교 세포신호전달연구센터 2003 고사리 세포신호전달 심포지움 Vol. No.5

Hsp72, a major inducible member of the heat shock protein family, has been shown to protect cells against many cellular stresses including heat shock and ischemia. In our present study, we observed that mild heat shock suppressed both c-Jun N-terminal kinase 1(JNK1) and p38 activity. Constitutively overexpressed Hsp72 also inhibited UV-induced JNK1 and p38 activation in NIH/3T3 cells. Both in vitro binding and kinase studies indicated that Hsp72 physically interacted with JNK1 and that the peptide-binding domain of Hsp72 might be involved in the binding and inhibition of JNK1. In vivo binding between endogenous Hsp72 and JNK1 protein in NIH/3T3 cells was confirmed by co-immunoprecipitation. Constitutively overexpressed Hsp72 also inhibited the JNK-dependent stimulation of c-Jun-mediated luciferase reporter activity and the apoptotic cell death induced by MEKK1 activation. Hsp72 antisense oligonucleotides blocked Hsp72 production in NIH/3T3 cells in response to mild heat shock and concomitantly abolished the suppressive effect of mild heat shock on UV-induced JNK activation and apoptosis. Taken together, our data strongly suggest that Hsp72 can modulate stress-activated signaling.

Cell Death Induced by the Stress-Activated Protein Kinase (SAPK) Pathway

Choi, Eui-Ju 이화여자대학교 세포신호전달연구센터 1999 고사리 세포신호전달 심포지움 Vol. No.1

The stress-activated protein kinase(SAPK), which is identical to the c-Jun N-terminal kinase(JNK) is a new member of the family of mammalian mitogen-activated protein(MAP) kinases that mediate intracellular signals originated from diverse extracellular stimuli, including growth factors, cytokines, or various stresses. SAPK is often activated through upstream protein kinases including SEK and MEKK1 in response to a variety of cellular stresses such as ionizing irradiation, alkylating chemicals, ultraviolet(UV) light, or metabolic inhibitors. It is noteworthy that many stresses that induce the stimulation of SAPK can eventually cause cell death. In fact, a blockade of the SAPK activation resulted in the prevention of cell death under varous conditions. These findings imply that SAPK may mediate an intracellular signaling pathway leading to cell death. In this context, we recently demonstrated that Bcl-2 disrupted a signaling cascade to SAPK which was activated by various apoptotic stresses and that overexpression of SAPK antagonized the death-protective function of Bcl-2. These findings imply that suppression of SAPK activation may be an important mechanism for the anti-apoptotic action of Bcl-2. Although SAPK is thought to play a role In cell death, a molecular mechanism by which the SAPK pathway mediates intracellular signals leading to cell death is not defined completely. To determine a mechanism for the regulation of the SAPK pathway may be prerequisite for understanding a role of SAPK in cell death. In this regard, we recently found several intracellular factors that can repress the SAPK signaling pathway. These findings imply that the inhibitory factors may suppress the stress-induced cell death that is mediated by the SAPK pathway.

Apoptosis Symposium : Anti-apoptotic function of a new protein CIIA

( Eui Ju Choi ) 한국생화학분자생물학회 (구 한국생화학회) 2004 생화학분자생물학회 춘계학술발표논문집 Vol.2004 No.-

Primary intraosseous squamous cell carcinoma mimicking periapical disease: a case report

Choi, Yoon-Joo,Oh, Song-Hee,Kang, Ju-Han,Choi, Hwa-Young,Kim, Gyu-Tae,Yu, Jae-Jung,Choi, Yong-Suk,Hwang, Eui-Hwan Korean Academy of Oral and Maxillofacial Radiology 2012 Imaging Science in Dentistry Vol.42 No.4

Primary intraosseous squamous cell carcinoma (PIOSCC) is a rare carcinoma, which arises within the jaws without connection to the oral mucosa and presumably develops from a remnant of odontogenic epithelium. We present a case of solid type PIOSCC in a 52-year-old male patient complaining of dull pain on his left lower molar. In this case, early stage PIOSCC mimicking a periapical lesion might lead to a one-year delay in treatment due to the misdiagnosis of osteomyelitis after extraction of the third molar. The clinical, radiological, and histologic features are described. In this case, there was initial radiographic evidence for PIOSCC mimicking a periapical lesion. Incautious radiographic interpretation and treatment procedures had delayed the correct diagnosis and resulted in extensive bony destruction during the patient's disease progression.

SKIP : an Inhibitory Factor for Stress-Activated Protein Kinase

Choi, Eui-Ju 가톨릭 의과학연구원 1998 가톨릭 의과학연구원 국제학술대회 Vol.2 No.-

A variety of environmental stresses including DNA damaging agents induce the activation of stress-activated protein kinase/c-Jun N-terminal kinase(SAPK/JNK). Deviation from the normal regulation of stress-activated protein kinase pathway may result in cell death. In this study, we report the molecular cloning of a gene encoding a cellular factor, named SAPK-inhibitory protein (SKIP), which is capable of physically interacting with SAPK in vitro as well as in vivo. SKIP acts as an inhibitor specific for SAPK, but not for either ERK or p38 MAPK. In rat and mouse, the skip generates multiple transcription variants probably produced by alternative splicing. Northern analysis indicates that in both mouse and rat, the skip1 is expressed in brain and kidney and the skip2 is specifically expressed in brain. All the deduced protein products of the skip transcription variants appear to have a similar property in that they all inhibit the SAPK stimulation in intact cells. SKIP not only inhibis the stress-induced stimulation of SAPK, but also confers an anti-cell death effect. These findings suggest that SKIP may play an important role in a regulatory mechanism for the stress-induced cellular responses including cell death.

p21WAF1 AS AN INHIBITOR OF STRESS - ACTIVATED MAP KINASES

Eui Ju Choi 한국생화학분자생물학회 (구 한국생화학회) 1996 추계학술대회집 Vol.- No.-

Licochalcone A induces apoptosis through endoplasmic reticulum stress via a phospholipase Cγ1-, Ca(2+)-, and reactive oxygen species-dependent pathway in HepG2 human hepatocellular carcinoma cells.

Choi, A-Young,Choi, Ji Hyun,Hwang, Keun-Young,Jeong, Yeon Ju,Choe, Wonchae,Yoon, Kyung-Sik,Ha, Joohun,Kim, Sung Soo,Youn, Jang Hyun,Yeo, Eui-Ju,Kang, Insug Rapid Science Publishers ; Kluwer Academic Publish 2014 Apoptosis Vol.19 No.4

<P>Licochalcone A (LicA), an estrogenic flavonoid, induces apoptosis in multiple types of cancer cells. In this study, the molecular mechanisms underlying the anti-cancer effects of LicA were investigated in HepG2 human hepatocellular carcinoma cells. LicA induced apoptotic cell death, activation of caspase-4, -9, and -3, and expression of endoplasmic reticulum (ER) stress-associated proteins, including C/EBP homologous protein (CHOP). Inhibition of ER stress by CHOP knockdown or treatment with the ER stress inhibitors, salubrinal and 4-phenylbutyric acid, reduced LicA-induced cell death. LicA also induced reactive oxygen species (ROS) accumulation and the anti-oxidant N-acetylcysteine reduced LicA-induced cell death and CHOP expression. In addition, LicA increased the levels of cytosolic Ca(2+), which was blocked by 2-aminoethoxydiphenyl borate (an antagonist of inositol 1,4,5-trisphosphate receptor) and BAPTA-AM (an intracellular Ca(2+) chelator). 2-Aminoethoxydiphenyl borate and BAPTA-AM inhibited LicA-induced cell death. Interestingly, LicA induced phosphorylation of phospholipase Cγ1 (PLCγ1) and inhibition of PLCγ1 reduced cell death and ER stress. Moreover, the multi-targeted receptor tyrosine kinase inhibitors, sorafenib and sunitinib, reduced LicA-induced cell death, ER stress, and cytosolic Ca(2+) and ROS accumulation. Finally, LicA induced phosphorylation of vascular endothelial growth factor receptor 2 (VEGFR2) and c-Met receptor and inhibition of both receptors by co-transfection with VEGFR2 and c-Met siRNAs reversed LicA-induced cell death, Ca(2+) increase, and CHOP expression. Taken together, these findings suggest that induction of ER stress via a PLCγ1-, Ca(2+)-, and ROS-dependent pathway may be an important mechanism by which LicA induces apoptosis in HepG2 hepatocellular carcinoma cells.</P>

CIIA : a novel anti-apoptotic protein that antagonizes ASK1-and CAD-mediated signaling

Choi, Eui-Ju 이화여자대학교 세포신호전달연구센터 2004 고사리 세포신호전달 심포지움 Vol. No.6

Diverse stimuli initiate the activation of apoptotic signaling pathways that often causes nuclear DNA fragmentation. Here we report a new anti-apoptotic protein, CIIA(a CAD inhibitor that interacts with ASK1). CIIA, by binding to apoptosis signal-regulating kinase 1(ASKl), inhibits oligomerization-induced ASK1 activation. CIIA also associates with caspase-activated DNase(CAD) and inhibits the nuclease activity of CAD without affecting caspase-3-mediated ICAD cleavage. Overexpressed CIIA reduces H₂O₂ and TNF-α-induced apoptosis. CIIA antisense oligonucleotides, which abolish expression of endogenous CIIA in murine L929 cells, block the inhibitory effect of CIIA on ASK1 activation, DNA fragmentation, and apoptosis. These findings suggest that CIIA is an endogenous antagonist of both ASK1-and CAD-mediated signaling.