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알코올 사용 장애 환자에서 알코올 사용의 심각도에 따른 불안 및 우울 증상과의 연관성
천은진,이준엽,구본훈,문보영,정진영,정성훈 대한생물치료정신의학회 2011 생물치료정신의학 Vol.17 No.2
Objectives:The purpose of this study was to examine the relationships of anxiety& depressive symptoms according to the severity of alcohol use in patients with alcohol use disorder. Methods:A total of 85 patients with alcohol use disorders were enrolled in this study. The severity of alcohol use was measured by the Korean version of alcohol use disorders identification test(AUDIT-K)& National Alcohol Screening test(NAST). Anxiety and depressive symptoms were measured by using the Beck Anxiety Inventory(BAI) and the Beck Depression Inventory(BDI), respectively. Pearson’s correlation test was applied to correlate among the severity of alcohol use, anxiety and depressive symptoms. Results:The mean scores of AUDIT-K, NAST, BAI and BDI were 22.22(±8.28), 6.24(±3.25), 18.64(±13.08), and 22.05(±10.13), respectively. Pearson’s correlation test showed that between the score of AUDIT-K and NAST, BAI or BDI, there were positively significant correlations(r=.534, p<.01 r=.231, p<.05 r=.334, p<.01), respectively. And in cases of≥26 score of AUDIT-K, there were much more positive correlations with BAI(r=.425, p<.05). Conclusion:The results of this study demonstrated that patients with alcohol use disorders have high co-morbid anxiety and depressive disorders. Overall, the greater severity of alcohol use may be associated with more anxiety and depressive symptoms. However, it is suggested that in the patients with severe alcohol use, correlation appeared to be positive only for anxiety symptoms.
이상준,박진용,임태형,윤영호,권순대,남창욱,허규찬,박근용,구본식,김상표,장종억 啓明大學校 醫科大學 1997 계명의대학술지 Vol.16 No.3
저자들은 인슐린 비의존형 당뇨병 환자에서 통증성 구강내 미란 및 전신성 수포성 미란을 동반한 심상성 천포창 1예를 경험하였기에 문헌고찰과 함께 보고하는 바이다. Various skin conditions such as diabetic dermopathy, necrobiosis lipoidica diabeticorum, bullosis diabeticorum, granuloma annulare occur frequently in diabetes, although common lesions may be associated by chance. Pemphigus vulgaris(PV) is a blistering skin disease seen predominantly in elderly patients. This disorder is characterized by the loss of cohesion between epidermal cells with the resultant formation of intraepidermal blisters. These blisters rupture easily, leaving denuded areases that may crust and enlarge peripherally. In half or more of patients, lesions begin in the mouth: approximately 90% of patients have oromucosal involvement at some time during the course of their disease. But the relationship of this disorder with diabetes is not clear. We experienced a case of pemphigus vulgaris associated with NIDDM in 67 years old woman who was admitted due to painful oral ulcer and control of blood glucose, so we present this case with a review of literatures.
Regulatory mechanism of matrix metalloprotease-2 enzymatic activity by factor Xa and thrombin.
Koo, Bon-Hun,Park, Michael Y,Jeon, Ok-Hee,Kim, Doo-Sik American Society for Biochemistry and Molecular Bi 2009 The Journal of biological chemistry Vol.284 No.35
<P>Matrix metalloprotease (MMP)-2 plays a key role in many biological and pathological processes related to cell migration, invasion, and mitogenesis. MMP-2 is synthesized as a zymogen that is activated through either a conformational change or proteolysis of the propeptide. Several activating enzymes for pro-MMP-2 have been proposed, including metalloproteases and serine proteases. The mechanism of pro-MMP-2 activation by metalloproteases is well established, and the most studied activation mechanism involves cleavage of the propeptide by membrane type 1-MMP (MT1-MMP). In contrast, serine protease activation has not been thoroughly studied, although studies suggest that MT1-MMP may be involved in activation by thrombin and plasmin. Here, we demonstrate that factor Xa mediates MT1-MMP-independent processing of pro-MMP-2 in vascular smooth muscle cells and endothelial cells. Factor Xa and thrombin directly cleaved the propeptide on the carboxyl terminal sides of the Arg(98) and Arg(101) residues, whereas plasmin only cleaved the propeptide downstream of Arg(101). Moreover, processed MMP-2 showed enzymatic activity that was enhanced by intermolecular autoproteolytic processing at the Asn(109)-Tyr peptide bond. In addition to its role in activation, factor Xa rapidly degraded MMP-2, thereby restricting excessive MMP-2 activity. Thrombin also degraded MMP-2, but the degradation was reduced greatly under cell-associated conditions, resulting in an increase in processed MMP-2. Overall, factor Xa and thrombin regulate MMP-2 enzymatic activity through its activation and degradation. Thus, the net enzymatic activity results from a balance between MMP-2 activation and degradation.</P>
Effect of Ovarian Extract on Oocyte Maturation and Early Embryonic Development in Pigs
Seul-Gi Yang(Seul-Gi Yang),Jae-Hun Choi(Jae-Hun Choi),Young-Seo Jo(Young-Seo Jo),Ye-Won Kim(Ye-Won Kim),Dong-Mok Lee(Dong-Mok Lee),Hyo-Jin Park(Hyo-Jin Park),Deog-Bon Koo(Deog-Bon Koo) 한국동물보건학회 2022 한국동물보건학회지 Vol.1 No.2
Various factors in the ovary are known to regulate oocyte maturation and hormone secretory functions; however, the effect of ovarian extract (OE) on oocyte maturation and embryonic development in pigs remains unknown. In this study, we first evaluated whether OE supplementation in the in vitro maturation (IVM) medium alters the oocyte maturation capacity by affecting glucose/amino acid metabolites, meiotic maturation, cumulus cell (CC) expansion, and antioxidants. Various OE concentrations (50, 100, 200, 500, and 5000 μg/mL) were included in the IVM medium. Only the oocytes treated with 100 μg/mL OE exhibited an improved meiotic maturation rate when compared with that of the other groups (non-treated group, 78.6 ± 3.0% vs. 100 μg/mL OE-treated group, 81.6 ± 4.3%); however, the difference was not significant. To observe the changes in glucose and amino acid metabolism in the OE-treated oocytes, we measured the amounts of diverse constituents (glucose, lactate, glutamine, and ammonia) in the IVM medium containing OE. Lactate and ammonia levels in the OE-treated group after 44 h of IVM were higher (p < 0.01) than those in the non-treated group. In addition, the expression of the CC expansion factors (Has2 and Tnfaip6) significantly increased (p < 0.05), whereas the mRNA expression levels of antioxidative enzymes (Sod1, Cat, and Gpx1) significantly diminished (p < 0.05) in the OE-treated group. Moreover, mature oocytes treated with 100 μg/mL OE demonstrated increased subsequent embryonic development rates after 144 h of IVM. Thus, the addition of OE in IVM mediums may improve oocyte maturation capacity which could enhance antioxidative enzyme activation, energy metabolism, and expression of the CC expansion factors in porcine oocytes.
Koo, Bon‐,Hun,Kim, Hee‐,Hyun,Park, Michael Y.,Jeon, Ok‐,Hee,Kim, Doo‐,Sik Blackwell Publishing Ltd 2009 FEBS JOURNAL Vol.276 No.21
<P>Matrix metalloprotease‐2 is implicated in many biological processes and degrades extracellular and non‐extracellular matrix molecules. Matrix metalloprotease‐2 maintains a latent state through a cysteine–zinc ion pairing which, when disrupted, results in full enzyme activation. This pairing can be disrupted by a conformational change or cleavage within the propeptide. The best known activation mechanism for pro‐matrix metalloprotease‐2 occurs via cleavage of the propeptide by membrane type‐1 matrix metalloprotease. However, significant residual activation of pro‐matrix metalloprotease‐2 is seen in membrane type‐1 matrix metalloprotease knockout mice and in fibroblasts treated with metalloprotease inhibitors. These findings indicate the presence of a membrane type‐1 matrix metalloprotease‐independent activation mechanism for pro‐matrix metalloprotease‐2 <I>in vivo</I>, which prompted us to explore an alternative activation mechanism for pro‐matrix metalloprotese‐2. In this study, we demonstrate membrane type‐1 matrix metalloprotease‐independent propeptide processing of matrix metalloprotease‐2 in HEK293F and various tumor cell lines, and show that proprotein convertases can mediate the processing intracellularly as well as extracellularly. Furthermore, processed matrix metalloprotease‐2 exhibits enzymatic activity that is enhanced by intermolecular autolytic cleavage. Thus, our experimental data, taken together with the broad expression of proprotein convertases, suggest that the proprotein convertase‐mediated processing may be a general activation mechanism for pro‐matrix metalloprotease‐2 <I>in vivo</I>.</P>
Threshold Voltage Control of Pentacene Thin-Film Transistor with Dual-Gate Structure
Koo, Jae-Bon,Ku, Chan-Hoe,Lim, Sang-Chul,Lee, Jung-Hun,Kim, Seong-Hyun,Lim, Jung-Wook,Yun, Sun-Jin,Yang, Yong-Suk,Suh, Kyung-Soo The Korean Infomation Display Society 2006 Journal of information display Vol.7 No.3
This paper presents a comprehensive study on threshold voltage $(V_{th})$ control of organic thin-film transistors (OTFTs) with dual-gate structure. The fabrication of dual-gate pentacene OTFTs using plasma-enhanced atomic layer deposited (PEALD) 150 nm thick $Al_{2}O_{3}$ as a bottom gate dielectric and 300 nm thick parylene or PEALD 200 nm thick $Al_{2}O_{3}$ as both a top gate dielectric and a passivation layer was investigated. The $V_{th}$ of OTFT with 300 nm thick parylene as a top gate dielectric was changed from 4.7 V to 1.3 V and that with PEALD 200 nm thick $Al_{2}O_{3}$ as a top gate dielectric was changed from 1.95 V to -9.8 V when the voltage bias of top gate electrode was changed from -10 V to 10 V. The change of $V_{th}$ of OTFT with dual-gate structure was successfully investigated by an analysis of electrostatic potential.