Go to the main menu
Skip to content
Go to bottom
REFERENCE LINKING PLATFORM OF KOREA S&T JOURNALS
> Journal Vol & Issue
Journal Basic Information
Journal DOI :
Korean Society for Biochemistry and Molecular Biology
Editor in Chief :
Volume & Issues
Volume 44, Issue 12 - Dec 2011
Volume 44, Issue 11 - Nov 2011
Volume 44, Issue 10 - Oct 2011
Volume 44, Issue 9 - Sep 2011
Volume 44, Issue 8 - Aug 2011
Volume 44, Issue 7 - Jul 2011
Volume 44, Issue 6 - Jun 2011
Volume 44, Issue 5 - May 2011
Volume 44, Issue 4 - Apr 2011
Volume 44, Issue 3 - Mar 2011
Volume 44, Issue 2 - Feb 2011
Volume 44, Issue 1 - Jan 2011
Selecting the target year
The role of peroxidases in the pathogenesis of atherosclerosis
Park, Jong-Gil ; Oh, Goo-Taeg ;
BMB Reports , volume 44, issue 8, 2011, Pages 497~505
DOI : 10.5483/BMBRep.2011.44.8.497
Reactive oxygen species (ROS), which include superoxide anions and peroxides, induce oxidative stress, contributing to the initiation and progression of cardiovascular diseases involving atherosclerosis. The endogenous and exogenous factors hypercholesterolemia, hyperglycemia, hypertension, and shear stress induce various enzyme systems such as nicotinamide adenine dinucleotide (phosphate) oxidase, xanthine oxidase, and lipoxygenase in vascular and immune cells, which generate ROS. Besides inducing oxidative stress, ROS mediate signaling pathways involved in monocyte adhesion and infiltration, platelet activation, and smooth muscle cell migration. A number of antioxidant enzymes (e.g., superoxide dismutases, catalase, glutathione peroxidases, and peroxiredoxins) regulate ROS in vascular and immune cells. Atherosclerosis results from a local imbalance between ROS production and these antioxidant enzymes. In this review, we will discuss 1) oxidative stress and atherosclerosis, 2) ROS-dependent atherogenic signaling in endothelial cells, macrophages, and vascular smooth muscle cells, 3) roles of peroxidases in atherosclerosis, and 4) antioxidant drugs and therapeutic perspectives.
The functions of mTOR in ischemic diseases
Hwang, Seo-Kyoung ; Kim, Hyung-Hwan ;
BMB Reports , volume 44, issue 8, 2011, Pages 506~511
DOI : 10.5483/BMBRep.2011.44.8.506
Mammalian Target of Rapamycin (mTOR) is a serine/threonine kinase and that forms two multiprotein complexes known as the mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). mTOR regulates cell growth, proliferation and survival. mTORC1 is composed of the mTOR catalytic subunit and three associated proteins: raptor, mLST8/
and PRAS40. mTORC2 contains mTOR, rictor, mLST8/
, mSin1, and protor. Here, we discuss mTOR as a promising anti-ischemic agent. It is believed that mTORC2 lies down-stream of Akt and acts as a direct activator of Akt. The different functions of mTOR can be explained by the existence of two distinct mTOR complexes containing unique interacting proteins. The loss of TSC2, which is upstream of mTOR, activates S6K1, promotes cell growth and survival, activates mTOR kinase activities, inhibits mTORC1 and mTORC2 via mTOR inhibitors, and suppresses S6K1 and Akt. Although mTOR signaling pathways are often activated in human diseases, such as cancer, mTOR signaling pathways are deactivated in ischemic diseases. From Drosophila to humans, mTOR is necessary for Ser473 phosphorylation of Akt, and the regulation of Akt-mTOR signaling pathways may have a potential role in ischemic disease. This review evaluates the potential functions of mTOR in ischemic diseases. A novel mTOR-interacting protein deregulates over-expression in ischemic disease, representing a new mechanism for controlling mTOR signaling pathways and potential therapeutic strategies for ischemic diseases.
Establishment and characterization of an immortalized human dermal papilla cell line
Shin, Seung-Hyun ; Park, Sang-Yoon ; Kim, Moon-Kyu ; Kim, Jung-Chul ; Sung, Young-Kwan ;
BMB Reports , volume 44, issue 8, 2011, Pages 512~516
DOI : 10.5483/BMBRep.2011.44.8.512
Establishment of immortalized human dermal papilla cells (DPCs) retaining the characteristics of DPCs would be a great help for hair researchers. We recently established a simian virus 40T (SV40T)-transformed human DP cell line (SV40TDPC). However, the cell line senesced around passage 25 and ceased proliferation. In this study, we introduced the human telomerase reverse transcriptase (hTERT) gene into SV40T-DPC and established an immortalized human DP cell line. The cell line, SV40T-hTERT-DPC, did not induce tumors when inoculated into nude mice. SV40T-hTERT-DPC maintained morphology of early passage DPCs, expressed markers of DPCs, and retained responses to Wnt/
-catenin and bone morphogenic protein (BMP) signaling pathways known to be required for hair-inducing activity of DPCs. The data strongly suggest that SV40T-hTERT-DPC retains many characteristics of human DPCs in vivo without malignant transformation.
Niclosamide induces mitochondria fragmentation and promotes both apoptotic and autophagic cell death
Park, So-Jung ; Shin, Ji-Hyun ; Kang, Hee ; Hwang, Jung-Jin ; Cho, Dong-Hyung ;
BMB Reports , volume 44, issue 8, 2011, Pages 517~522
DOI : 10.5483/BMBRep.2011.44.8.517
Mitochondrial dynamics not only involves mitochondrial morphology but also mitochondrial biogenesis, mitochondrial distribution, and cell death. To identify specific regulators to mitochondria dynamics, we screened a chemical library and identified niclosamide as a potent inducer of mitochondria fission. Niclosamide promoted mitochondrial fragmentation but this was blocked by down-regulation of Drp1. Niclosamide treatment resulted in the disruption of mitochondria membrane potential and reduction of ATP levels. Moreover, niclosamide led to apoptotic cell death by caspase-3 activation. Interestingly, niclosamide also increased autophagic activity. Inhibition of autophagy suppressed niclosamide-induced cell death. Therefore, our findings suggest that niclosamide induces mitochondria fragmentation and may contribute to apoptotic and autophagic cell death.
Downregulation of ARFGEF1 and CAMK2B by promoter hypermethylation in breast cancer cells
Kim, Ju-Hee ; Kim, Tae-Woo ; Kim, Sun-Jung ;
BMB Reports , volume 44, issue 8, 2011, Pages 523~528
DOI : 10.5483/BMBRep.2011.44.8.523
To identify novel genes that are regulated by promoter methylation, a combinational approach involving in silico mining followed by molecular assay was performed. From the expression microarray data registered in the European bioinformatics institute (EBI), genes showing downregulation in breast cancer cells were initially screened and then selected by e-Northern analysis using the Unigene database. A series of these in silico methods identified CAMK2B and ARFGEF1 as candidates, and the two genes were revealed to be hypermethylated in breast cancer cell lines and hypomethylated in normal breast cell lines. Additionally, cancer cell lines showed downregulated expression of these genes. Furthermore, treatment of the cancer cell lines with a demethylation agent, 5-Aza-2`-deoxycytidine, recovered expression of CAMK2B and ARFGEF1, implying that hypermethyaltion silenced gene activity in cancer cells. Taken together, promoter methylations of CAMK2B and ARFGEF1 are novel epigenetic markers identified in breast cancer cell lines and can be utilized for the application to clinical cancer tissues.
Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase
Yoon, In-Soo ; Chung, Ji-Hyung ; Hahm, Soo-Hyun ; Park, Min-Ju ; Lee, You-Ri ; Ko, Sung-Il ; Kang, Lin-Woo ; Kim, Tae-Sung ; Kim, Joon ; Han, Ye-Sun ;
BMB Reports , volume 44, issue 8, 2011, Pages 529~534
DOI : 10.5483/BMBRep.2011.44.8.529
Ribosomal protein S3 (rpS3) is a multifunctional protein involved in translation, DNA repair, and apoptosis. The relationship between rpS3 and cyclin-dependent kinases (Cdks) involved in cell cycle regulation is not yet known. Here, we show that rpS3 is phosphorylated by Cdk1 in G2/M phase. Co-immunoprecipitation and GST pull-down assays revealed that Cdk1 interacted with rpS3. An in vitro kinase assay showed that Cdk1 phosphorylated rpS3 protein. Phosphorylation of rpS3 increased in nocodazole-arrested mitotic cells; however, treatment with Cdk1 inhibitor or Cdk1 siRNA significantly attenuated this phosphorylation event. The phosphorylation of a mutant form of rpS3, T221A, was significantly reduced compared with wild-type rpS3. Decreased phosphorylation and nuclear accumulation of T221A was much more pronounced in G2/M phase. These results suggest that the phosphorylation of rpS3 by Cdk1 occurs at Thr221 during G2/M phase and, moreover, that this event is important for nuclear accumulation of rpS3.
Epigenetic characterization of the PBEF and TIMP-2 genes in the developing placentae of normal mice
Kim, Hong-Rye ; Han, Rong-Xun ; Diao, Yun-Fei ; Park, Chang-Sik ; Jin, Dong-Il ;
BMB Reports , volume 44, issue 8, 2011, Pages 535~540
DOI : 10.5483/BMBRep.2011.44.8.535
Reprogramming errors, which appear frequently in cloned animals, are reflected by aberrant gene expression. We previously reported the aberrant expression of TIMP-2 and PBEF in cloned placenta and differential expression of PBEF genes during pregnancy. To examine the epigenetic modifications that regulate dynamic gene expression in developing placentae, we herein analyzed the mRNA and protein expression levels of PBEF and TIMP-2 in the placentae of normal mice during pregnancy and then examined potential correlations with epigenetic modifications. DNA methylation pattern analysis revealed no difference, but ChIP assays using antibodies against H3-K9/K14 and H4-K5 histone acetylation revealed that the H3-K9/K14 acetylation levels, but not the H4-K5 acetylation levels, of the TIMP-2 and PBEF loci were significantly correlated with their gene expression levels during placentation in normal mice. These results suggest that epigenetic changes may regulate gene expression level in the developing placentae of normal mice and that inappropriate epigenetic reprogramming might be one cause of the abnormal placentae seen in cloned animals.
FSCB phosphorylation in mouse spermatozoa capacitation
Liu, Shun-Li ; Ni, Bing ; Wang, Xiang-Wei ; Huo, Wen-Qian ; Zhang, Jun ; Tian, Zhi-Qiang ; Huang, Ze-Min ; Tian, Yi ; Tang, Jun ; Zheng, Yan-Hua ; Jin, Feng-Shuo ; Li, Yan-Feng ;
BMB Reports , volume 44, issue 8, 2011, Pages 541~546
DOI : 10.5483/BMBRep.2011.44.8.541
It is generally accepted that spermatozoa capacitation is associated with protein kinase A-mediated tyrosine phosphorylation. In our previous study, we identified the fibrous sheath CABYR binding protein (FSCB), which was phosphorylated by PKA. However, the phosphorylation status of FSCB protein during spermatozoa capacitation should be further investigated. To this aim, in this study, we found that phosphorylation of this 270-kDa protein occurred as early as 1 min after mouse spermatozoa capacitation, which increased over time and remained stable after 60 min. Immunoprecipitation assays demonstrated that the tyrosine and Ser/Thr phosphorylation of FSCB occurred during spermatozoa capacitation. The extent of phosphorylation and was closely associated with the PKA activity and spermatozoa motility characteristics. FSCB phosphorylation could be induced by PKA agonist DB-cAMP, but was blocked by PKA antagonist H-89.Therefore, FSCB contributes to spermatozoa capacitation in a tyrosine-phosphorylated format, which may help in further elucidating the molecular mechanism of spermatozoa capacitation.
Suppression of MED19 expression by shRNA induces inhibition of cell proliferation and tumorigenesis in human prostate cancer cells
Cui, Xingang ; Xu, Danfeng ; Lv, Chao ; Qu, Fajun ; He, Jin ; Chen, Ming ; Liu, Yushan ; Gao, Yi ; Che, Jianping ; Yao, Yacheng ; Yu, Hongyu ;
BMB Reports , volume 44, issue 8, 2011, Pages 547~552
DOI : 10.5483/BMBRep.2011.44.8.547
MED19 is a member of the Mediator that plays a key role in the activation and repression of signal transduction or the regulation of transcription in carcinomas. To tested the functional role of MED19 in human prostate cancer, we downregulated MED19 expression in prostate cancer cells (PC-3 and DU145) by lentivirus-mediated short hairpin (shRNA), and analyzed the effect of inhibition of MED19 on prostate cancer cell proliferation and tumorigenesis. The in vitro prostate cancer cell proliferation, colony formation, and in vivo tumor growth in nude mice xenografts was significantly reduced after the downregulation of MED19. Knockdown of MED19 caused S-phase arrest and induced apoptosis via modulation of Bid and Caspase 7. It was suggested that MED19 serves as a novel proliferation regulator that promotes growth of prostate cancer cells.
NF-Y binds to both G1- and G2-specific cyclin promoters; a possible role in linking CDK2/Cyclin A to CDK1/Cyclin B
Chae, Hee-Don ; Kim, Jung-Bin ; Shin, Deug-Y. ;
BMB Reports , volume 44, issue 8, 2011, Pages 553~557
DOI : 10.5483/BMBRep.2011.44.8.553
We previously reported that CDK2/Cyclin A can phosphorylate and activate the transcription factor NF-Y. In this study, we investigated a potential regulatory role for NF-Y in the transcription of Cyclin A and other cell cycle regulatory genes. Gel-shift assays demonstrate that NF-Y binds to CCAAT sequences in the Cyclin A promoter, as well as to those in the promoters of cell cycle G2 regulators such as CDC2, Cyclin B and CDC25C. Furthermore, expression of Cyclin A increases NF-Y`s affinity for CCAAT sequences in the CDC2 promoter; however, Cyclin A`s induction of CDC2 transcription is antagonized by p21, an inhibitor of CDK2/Cyclin A. These results suggest a model wherein NF-Y binds to and activates transcription from the Cyclin A promoter, increasing cellular levels of Cyclin A/CDK2 and potentiating NF-Y`s capacity for transcriptional transactivation, and imply a positive feedback loop between NF-Y and Cyclin A/CDK2. Our findings are additionally indicative of a role for Cyclin A in activating Cyclin B/CDK1 through promoting NF-Y dependent transcription of Cyclin B and CDC2; NF-Y mediated crosstalk may therefore help to orchestrate cell-cycle progression.