Articles
<![CDATA[Altered expressions of endothelial junction protein of placental capillaries in premature infants with intraventricular hemorrhage ]]>
<![CDATA[Ekawati, Maria]]>;
<![CDATA[Mujihartini, Ninik]]>;
<![CDATA[Jusuf, Ahmad A.]]>;
<![CDATA[Dharmasetiawani, Nani]]>;
<![CDATA[Jusman, Sri W.A.]]>;
<![CDATA[Sadikin, Mohamad]]>
<![CDATA[ Medical Journal of Indonesia Vol 25, No 3 (2016): September ]]>
Publisher : <![CDATA[Faculty of Medicine Universitas Indonesia ]]>
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DOI: 10.13181/mji.v25i3.1287
<![CDATA[Background: Placental hypoxia may lead to oxidative stress, which inflicts damage to capillary protein junction. The aim of this study was to evaluate altered expression of endothelial junction protein of capillaries in hypoxia condition and to observe its correlation with the incidence of intraventricular hemorrhage in premature infants.Methods: A cross-sectional study was conducted by using placental tissues of premature infants as amodel of capillary integrity (29 hypoxic and 29 non-hypoxic). Hypoxia inducible factor (HIF)-1α was measured to define placental tissue response to hypoxia; malondialdehyde (MDA) and glutathione (GSH) served as markers of oxidative stress. The expressions of junctional proteins, N-cadherin and occludin were analyzed by immunohistochemistry. Intraventricular hemorrhage (IVH) was detected by cranial ultrasound at the third day. Unpaired t test, Mann-Whitney, and Chi-square tests were used to analyze the data.Results: The HIF-1α and MDA levels were slightly, but not significantly, higher in hypoxia group {13.64±8.70 pg/mg protein and 10.31 pmol/mg tissue (ranged 1.92–93.61), respectively} compared to non- hypoxia group {10.65±5.35 pg/mg protein and 9.77 pmol/mg tissue (ranged 2.42–93.31)}. GSH levels were not different in both groups (38.14 (ranged 9.44–118.91) and 38.47(ranged 16.49–126.76) ng/mg protein, respectively. mRNA expression of N-cadherin (0.13) and occludin (0.096) were significantly lower in hypoxia comparedto non-hypoxia group (p=0,001), while protein expression of N-cadherin (3.4; 75.9; 6.9; 13.8%) and occludin (20.7; 3.4; 69.0; 3.4; 6.9%) in hypoxia group was not associated with IVH (p=0.783 and p=0.743).Conclusion: Hypoxia altered expression of endothelial junction protein in placental capillaries, but no association with intraventricular hemorrhage was observed.]]>
<![CDATA[Expressions of stemness markers in keloid tissue ]]>
<![CDATA[Ningsih, Sri S.]]>;
<![CDATA[Sari, Dewi H.]]>;
<![CDATA[Antarianto, Radiana D.]]>;
<![CDATA[Hardiany, Novi S.]]>;
<![CDATA[Sadikin, Mohamad]]>;
<![CDATA[Wanandi, Septelia I.]]>;
<![CDATA[Jusman, Sri W.A.]]>
<![CDATA[ Medical Journal of Indonesia Vol 27, No 3 (2018): September ]]>
Publisher : <![CDATA[Faculty of Medicine Universitas Indonesia ]]>
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DOI: 10.13181/mji.v27i3.1920
<![CDATA[Background: Keloid is an abnormal wound healing process that extends beyond the site of injury. Keloid and tumor’s shared similarity of recurrence suggesting a shared underlying mechanism that involves stemness. Octamer-binding transcription factor-4 (Oct-4) and aldehyde dehydrogenase-1 (ALDH1) are stem cell stemness markers. This study aimed to analyze Oct-4 and ALDH1 expressions in keloid tissues.Methods: Samples were obtained from keloid tissue excisions from three keloid patients and post-circumcision preputial skin from three healthy donors (normal control) in accordance with the local ethical committee regulation. Total RNA was isolated using TriPure Isolation kit (Ameritech), and expressions of Oct4 and ALDH1 mRNA in keloid and preputial skin were determined by quantitative reverse transcription–polymerase chain reaction (qRT-PCR) using Livak method.Results: The qRT-PCR analysis revealed the expressions of Oct4 and ALDH1 in keloid and preputial skin tissues. Keloid tissues exhibited lower expression levels of Oct-4 and ALDH1 than the preputial skin. The difference was statistically insignificant.Conclusion: Keloid tissues express Oct-4 and ALDH1 as stemness markers, and the stemness characteristics of keloid might be similar to a normal skin.]]>
<![CDATA[Expression and specific activities of carbamoyl phosphate synthetase 1 in chronic hypoxic rats ]]>
<![CDATA[Nikmah, Uly A.]]>;
<![CDATA[Prijanti, Ani R.]]>;
<![CDATA[Jusman, Sri W.A.]]>;
<![CDATA[Sadikin, Mohamad]]>
<![CDATA[ Medical Journal of Indonesia Vol 25, No 1 (2016): March ]]>
Publisher : <![CDATA[Faculty of Medicine Universitas Indonesia ]]>
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DOI: 10.13181/mji.v25i1.1213
<![CDATA[Background: Urea biosynthesis is a very important process in the liver which needs ATP, CO2 and functional mitochondria or aerobic condition. Liver can adapt to hypoxic condition, generally and locally. This study aimed to analyze the effect of chronic hypoxia on liver urea biosynthesis as indicated by the level and specific activity of mRNA of carbamoyl phosphate synthetase 1 (CPS1), a key enzyme in urea biosynthesis in hypoxic rats.Methods: 20 male Sprague-Dawley rats were placed in hypoxic chamber supplied by a mixture of 10% O2 and 90% N2. Five rats were sacrificed at 1, 3, 5, and 7 days after exposure. Liver homogenates were analyzed for HIF-1 (hypoxia inducible factor-1) by ELISA, CPS1 mRNA by real time RT-PCR and CPS1 enzymatic specific activities by Pierson method. Data were analyzed by ANOVA test and Pearson correlation.Results: The HIF-1 in liver increased significantly, as well as CPS1 mRNA and CPS1 enzymatic activities (p<0.05). There was a strong correlation (r=0.618; p<0.01) between the level of CPS1 mRNA and CPS1 enzymatic activities, moderate correlation between HIF-1 and CPS1 mRNA (r=0.419; p<0.05) but no correlation between HIF-1 and CPS1 enzymatic activities. The study indicated that urea biosynthesis in liver was affected by hypoxia and partially under HIF-1 regulation. The study also found increase of urea and NH3 biosynthesis related to proteolysis as indicated by the decrease of total body weight and liver weight.Conclusion: There was an increase in the expression and specific activities of CPS1 in urea biosynthesis as a result of increasing proteolysis in chronic hypoxic condition.]]>
<![CDATA[Myocardial damage after continuous aerobic and anaerobic exercise in rats ]]>
<![CDATA[Flora, Rostika]]>;
<![CDATA[Ferdinal, Frans]]>;
<![CDATA[Hernowo, Bethy S.]]>;
<![CDATA[Wanandi, Septelia I.]]>;
<![CDATA[Sadikin, Mohamad]]>;
<![CDATA[Freisleben, Hans-Joachim]]>
<![CDATA[ Medical Journal of Indonesia Vol 22, No 4 (2013): November ]]>
Publisher : <![CDATA[Faculty of Medicine Universitas Indonesia ]]>
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DOI: 10.13181/mji.v22i4.601
<![CDATA[Background: Regular physical activity is highly recommended in preventive, curative, and rehabilitative programs in order to promote health, especially cardiovascular health. However, physical activity can also cause sudden death. In athletes, sudden death may occur during sport competitions, with myocardial infarction as the most common etiology. It is suspected that continuous training without any rest-day play a role in cardiac muscle damage and sudden death during competition. Our study was aimed to learn about cardiac muscle adaptation on continuous aerobic and anaerobic physical activity without any rest-day. Methods: The specimens in our study were cardiac muscle tissue obtained from rats that had performed aerobic and anaerobic physical activity on treadmill for 1, 3, 7, and 10 days without any rest-day. Blood gas analysis and hematological assessment were used as parameters of systemic adaptation to hypoxia during physical activity. Moreover, histopathology of cardiac muscle tissue was performed as parameter for cardiac muscle damage.Results: The results showed that aerobic and anaerobic physical activity caused a systemic hypoxic condition and triggered adaptation responses. Cardiac muscle damage occurred on the 10th day in both treatment groups, with more severe damage observed in the group with anaerobic physical activity. The tissue protein level in the anaerobic group increased progressively on the 10th day.Conclusion: Physical activity may result in hypoxia and systemic adaptation. Aerobic and anaerobic physical activities performed for 10 days without any rest-day may cause cardiac muscle damage. (Med J Indones. 2013;22:209-14. doi: 10.13181/mji.v22i4.601)Keywords: Cardiac muscle, cardiac muscle damage, histopathology, physical activity]]>
<![CDATA[The suppression of manganese superoxide dismutase decreased the survival of human glioblastoma multiforme T98G cells ]]>
<![CDATA[Hardiany, Novi S.]]>;
<![CDATA[Sadikin, Mohamad]]>;
<![CDATA[Siregar, Nurjati]]>;
<![CDATA[Wanandi, Septelia I.]]>
<![CDATA[ Medical Journal of Indonesia Vol 26, No 1 (2017): March ]]>
Publisher : <![CDATA[Faculty of Medicine Universitas Indonesia ]]>
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DOI: 10.13181/mji.v26i1.1511
<![CDATA[Background: Glioblastoma multiforme (GBM) is a primary malignant brain tumor which has poor prognosis. High incidence of oxidative stress-based therapy resistance could be related to the high antioxidant status of GBM cells. Our previous study has reported that manganese superoxide dismutase (MnSOD) antioxidant expression was significantly higher in high grade glioma than in low grade. The aim of this study was to analyze the impact of MnSOD suppression toward GBM cell survival.Methods: This study is an experimental study using human glioblastoma multiforme T98G cell line. Suppression of MnSOD expression was performed using in vitro transfection MnSOD-siRNA. The MnSOD expression was analyzed by measuring the mRNA using real time RT-PCR, protein using ELISA technique, and specific activity of enzyme using inhibition of xantine oxidase. Concentration of reactive oxygen species (ROS) intracellular was determined by measuring superoxide radical and hydrogen peroxide. Cell survival was analyzed by measuring viability, proliferation, and cell apoptosis.Results: In vitro transfection of MnSOD-siRNA suppressed the mRNA, protein, and specific activity of MnSOD. This treatment significantly increased the concentration of superoxide radical; however, it did not influence the concentration of hydrogen peroxide. Moreover, viability MnSOD-suppressing cell significantly decreased, accompanied by increase of cell apoptosis without affecting cell proliferation.Conclusion: The suppression of MnSOD expression leads to decrease glioblastoma multiforme cell survival, which was associated to the increase of cell apoptotic.]]>
<![CDATA[Avidin inhibits PHA-induced human peripheral blood mononuclear cell proliferation ]]>
<![CDATA[Firakania, Cicia]]>;
<![CDATA[Mansur, Indra G.]]>;
<![CDATA[Jusman, Sri W.A.]]>;
<![CDATA[Sadikin, Mohamad]]>
<![CDATA[ Medical Journal of Indonesia Vol 25, No 1 (2016): March ]]>
Publisher : <![CDATA[Faculty of Medicine Universitas Indonesia ]]>
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DOI: 10.13181/mji.v25i1.1264
<![CDATA[Background: Cell proliferation occurs not only in normal but also in cancer cells. Most of cell proliferation inhibition can be done by inhibiting the DNA synthesis, notably by intervening the formation of purine or pyrimidine. In purine de novo synthesis, it was assumed that biotin plays a role as a coenzyme in carboxylation reaction, one of the pivotal steps in the purine de novo pathways. The aim of this study was to see the avidin potency to bind biotin and inhibit mitosis.Methods: Peripheral blood mononuclear cell (PBMC) was cultured in RPMI-1640 medium and stimulated by phytohemagglutinin (PHA) in the presence or absence of interleukin-2 (IL-2), with or without avidin. The effect of avidin addition was observed at 24, 48, and 72 hours for cell proliferation, viability, and cell cycle. Statistical analysis was done by one-way ANOVA.Results: Avidin inhibited cell proliferation and viability in culture under stimulation by PHA with and without IL-2. Cell cycle analysis showed that avidin arrested the progression of PBMC after 72 hours of culture. Most cells were found in G0/G1 phase.Conclusion: Inhibition of biotin utilization by avidin binding can halt cell proliferation.]]>
<![CDATA[Relative hypoxia and oxidative stress in spleen lymphocytes of immunized Balb/c mice as indicated by HIF-1α, HIF-2α, Nrf2 expression, and glutathione peroxidase activity ]]>
<![CDATA[Praditi, Citra]]>;
<![CDATA[Prijanti, Ani R.]]>;
<![CDATA[Jusman, Sri W.A.]]>;
<![CDATA[Sadikin, Mohamad]]>
<![CDATA[ Medical Journal of Indonesia Vol 27, No 4 (2018): December ]]>
Publisher : <![CDATA[Faculty of Medicine Universitas Indonesia ]]>
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DOI: 10.13181/mji.v27i4.2152
<![CDATA[Background: Lymphocytes activated by immunization must increase their metabolism to meet the energy requirements for mitosis, differentiation, and protein synthesis, which may subject the cell to conditions of relative hypoxia and oxidative stress. This study was conducted to investigate the increase in the levels of transcription factors involved in both conditions.Methods: Male Balb/c mice were divided into the following four groups, each consisting of six animals: the control and three experimental groups. The experimental groups were immunized by injection of 0.2 ml of 2% sheep red blood cells (SRBC) suspended in phosphate-buffered saline (PBS). Lymphocytes were harvested from the spleens of each group at time intervals of 24-, 48-, and 72-h post-immunization. The buffy coat from splenocytes was separated using Ficoll Histopaque as the medium. The lymphocytes were separated from adherent cells by incubating the purified splenocytes in microtubes for 2-h. Cells were lysed by three freeze–thaw cycles (−80°C and 37°C) and used to analyze the levels of HIF-1α and HIF-2α (mRNA and protein), Nrf2 (protein), and glutathione peroxidase (GPx) activity.Results: The treatment caused an increase in GPx activity and HIF-1α protein concentration 24-h post-immunization, whereas the HIF-1α mRNA levels remained static. Elevated Nrf2 protein levels were detected within 48-h after treatment. Meanwhile, the HIF-2α mRNA and protein levels increased within72-h after immunization.Conclusion: Immunization with SRBC suspension induced relative hypoxia, elevated reactive oxygen species (ROS), and oxidative stress in the lymphocytes as indicated by the increase in both HIF-1α and HIF-2α protein and mRNA levels, GPx activity, and Nrf2 protein levels.]]>
<![CDATA[Efforts to overcome hypoxia condition in Balb/c mouse macrophages after intraperitoneal SRBC immunization ]]>
<![CDATA[Sarsanti, Pungguri Ayu Nega]]>;
<![CDATA[Sadikin, Mohamad]]>;
<![CDATA[Jusman, Sri Widia Azraki]]>
<![CDATA[ Medical Journal of Indonesia Vol 28, No 1 (2019): March ]]>
Publisher : <![CDATA[Faculty of Medicine Universitas Indonesia ]]>
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DOI: 10.13181/mji.v28i1.1961
<![CDATA[BACKGROUND Activated macrophages require increased oxygen to destroy foreign bodies, leading to an increase in the levels of reactive oxygen species (ROS). Therefore, macrophages would experience hypoxic and oxidative stress conditions at the same time. Thus, this study was aimed to evaluate the mechanism of the activated macrophages to overcoming this dual condition.METHODS The activated macrophages were harvested from the intraperitoneal cavities of 18 BALB/c mice immunized with 2% sheep red blood cells (SRBCs). The macrophage suspension was divided into four groups: control, 24, 48, and 72 hours after-immunization groups. The expressions of hypoxia-inducible factor (HIF)-1α, HIF-2α, and cytoglobin (Cygb), as markers for hypoxic condition, were measured by quantitative reverse transcription polymerase chain reaction (qRT-PCR) and enzyme-linked immunosorbent assay (ELISA), whereas peroxisome proliferator-activated receptor gamma coactivator (PGC-1α) protein as a marker for mitochondrial biogenesis and aerobic metabolism was measured with ELISA. The analysis of oxidative stress was conducted with the water-soluble tetrazolium salt test.RESULTS The HIF-1α mRNA expression was the highest at 24 hours, whereas the HIF-2α mRNA showed no increased expression during the observation. The Cygb mRNA decreased after 24 hours. The highest expressions of HIF-1α and HIF-2α proteins were detected at 72 hours, whereas the Cygb protein expression increased since 24 hours. The PGC-1α protein expression increased at 72 hours. The WST test showed the highest ROS level at 24 hours.CONCLUSIONS The macrophages were activated by SRBCs underwent dual hypoxia and oxidative stress condition simultaneously to overcome the foreign bodies. The macrophages overcame these stress conditions by increasing their aerobic metabolism.]]>
<![CDATA[Qualitative Study on Endothelial Cell–to–cell–junction Disassembly in Severe Burn Injury ]]>
<![CDATA[Moenadjat, Yefta]]>;
<![CDATA[Siregar, Nurjati C.]]>;
<![CDATA[Wanandi, Septelia I.]]>;
<![CDATA[Sadikin, Mohamad]]>
<![CDATA[ The New Ropanasuri Journal of Surgery ]]>
Publisher : <![CDATA[UI Scholars Hub ]]>
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<![CDATA[Introduction. Endothelial gap in severe burn injury remain a mystery. Capillary leaks possess its own characteristics, which is found in burned– and non–burned area. The gaps remain up to 10 post burned days or more. This is somehow representing the feature of systemic capillary leaks syndrome at the first date. VE–cadherin of adherens endothelial junction molecules known to be temporarily disassembled following thermal exposure, but there’s a question about reversibility. Question is also addressed to occludin of the tight junction molecules. We run a study to investigate these junction molecules. Method. We run an investigation to find out both molecules qualitatively descriptive on 30 burn patients enrolled, consist of 20 severe– and 10 of non–severe burn. Samples of moderate size vein taken from burned– and non–burned area were subjected to study of histomorphology and immunohistochemistry. Light microscopic study and polymerase chain reaction test were carried out to compare the features and its expression. Analysis is carried out to find the difference, specificity and sensitivity. Results. Samples took within the first 8 hours following ER presentation showed severely deteriorated endothelial lining and both ofVE–cadherin and occludin dissociation. This endothelial junction disassembly was found in both of burned– and non–burned area; both of severe– and non– severe burn as well. In burned area, mRNA expression of VE–cadherin found to be increased, as occludin decreased. In severe burned group, mRNA expression of VE–cadherin as well as occludin found to be increased. VE–cadherin synthesis was found to be earlier than occludin. Conclusion. Dissociation of both of endothelial cell–to–cell molecules junction show no differences between the two groups, and between burned– and non–burned areas.]]>
<![CDATA[Myoglobin Expression in Chelonia mydas Brain, Heart and Liver Tissues ]]>
<![CDATA[RINI PUSPITANINGRUM]]>;
<![CDATA[SEPTELIA INAWATI WANANDI]]>;
<![CDATA[RONDANG ROEMIATI SOEGIANTO]]>;
<![CDATA[MOHAMAD SADIKIN]]>;
<![CDATA[DARYL ROBERT WILLIAMS]]>;
<![CDATA[ANDREW ROBERT COSSINS]]>
<![CDATA[ HAYATI Journal of Biosciences Vol. 17 No. 3 (2010): September 2010 ]]>
Publisher : <![CDATA[Bogor Agricultural University, Indonesia ]]>
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DOI: 10.4308/hjb.17.3.110
<![CDATA[An understanding of the underpinning physiology and biochemistry of animals is essential to properly understand the impact of anthropogenic changes and natural catastrophes upon the conservation of endangered species. An observation on the tissue location of the key respiratory protein, myoglobin, now opens up new opportunities for understanding how hypoxia tolerance impacts on diving lifestyle in turtles. The respiratory protein, myoglobin has functions other than oxygen binding which are involved in hypoxia tolerance, including metabolism of reactive oxygen species and of the vascular function by metabolism of nitric oxide. Our work aims to determine whether myoglobin expression in the green turtle exists in multiple non muscle tissues and to confirm the hypothesis that reptiles also have a distributed myoglobin expression which is linked to the hypoxiatolerant trait. This initial work in turtle hatch Chelonia mydas confirms the presence of myoglobin transcriptin brain, heart and liver tissues. Furthermore, it will serve as a tool for completing the sequence and generating an in situ hybridization probe for verifying of cell location in expressing tissues.]]>
