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REFERENCE LINKING PLATFORM OF KOREA S&T JOURNALS
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Korean Society for Biochemistry and Molecular Biology
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Volume & Issues
Volume 41, Issue 12 - Dec 2008
Volume 41, Issue 11 - Nov 2008
Volume 41, Issue 10 - Oct 2008
Volume 41, Issue 9 - Sep 2008
Volume 41, Issue 8 - Aug 2008
Volume 41, Issue 7 - Jul 2008
Volume 41, Issue 6 - Jun 2008
Volume 41, Issue 5 - May 2008
Volume 41, Issue 4 - Apr 2008
Volume 41, Issue 3 - Mar 2008
Volume 41, Issue 2 - Feb 2008
Volume 41, Issue 1 - Jan 2008
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Innate immune response in insects: recognition of bacterial peptidoglycan and amplification of its recognition signal
Kim, Chan-Hee ; Park, Ji-Won ; Ha, Nam-Chul ; Kang, Hee-Jung ; Lee, Bok-Luel ;
BMB Reports , volume 41, issue 2, 2008, Pages 93~101
DOI : 10.5483/BMBRep.2008.41.2.093
The major cell wall components of bacteria are lipopolysaccharide, peptidoglycan, and teichoic acid. These molecules are known to trigger strong innate immune responses in the host. The molecular mechanisms by which the host recognizes the peptidoglycan of Gram-positive bacteria and amplifies this peptidoglycan recognition signals to mount an immune response remain largely unclear. Recent, elegant genetic and biochemical studies are revealing details of the molecular recognition mechanism and the signalling pathways triggered by bacterial peptidoglycan. Here we review recent progress in elucidating the molecular details of peptidoglycan recognition and its signalling pathways in insects. We also attempt to evaluate the importance of this issue for understanding innate immunity.
CLIP-domain serine proteases in Drosophila innate immunity
Jang, In-Hwan ; Nam, Hyuck-Jin ; Lee, Won-Jae ;
BMB Reports , volume 41, issue 2, 2008, Pages 102~107
DOI : 10.5483/BMBRep.2008.41.2.102
Extracellular proteases play an important role in a wide range of host physiological events, such as food digestion, extracellular matrix degradation, coagulation and immunity. Among the large extracellular protease family, serine proteases that contain a "paper clip"-like domain and are therefore referred to as CLIP-domain serine protease (clip-SP), have been found to be involved in unique biological processes, such as immunity and development. Despite the increasing amount of biochemical information available regarding the structure and function of clip-SPs, their in vivo physiological significance is not well known due to a lack of genetic studies. Recently, Drosophila has been shown to be a powerful genetic model system for the dissection of biological functions of the clip-SPs at the organism level. Here, the current knowledge regarding Drosophila clip-SPs has been summarized and future research directions to evaluate the role that clip-SPs play in Drosophila immunity are discussed.
Proteomic analysis of heat-stable proteins in Escherichia coli
Kwon, Soon-Bok ; Jung, Yun-A ; Lim, Dong-Bin ;
BMB Reports , volume 41, issue 2, 2008, Pages 108~111
DOI : 10.5483/BMBRep.2008.41.2.108
Some proteins of E. coli are stable at temperatures significantly higher than
, the maximum temperature at which the organism can grow. The heat stability of such proteins would be a property which is inherent to their structures, or it might be acquired by evolution for their specialized functions. In this study, we describe the identification of 17 heat-stable proteins from E. coli. Approximately one-third of these proteins were recognized as having functions in the protection of other proteins against denaturation. These included chaperonin (GroEL and GroES), molecular chaperones (DnaK and FkpA) and peptidyl prolyl isomerases (trigger factor and FkpA). Another common feature was that five of these proteins (GroEL, GroES, Ahpc, RibH and ferritin) have been shown to form a macromolecular structure. These results indicated that the heat stability of certain proteins may have evolved for their specialized functions, allowing them to cope with harsh environments, including high temperatures.
Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli
Wang, Qian ; Pi, Yan ; Hou, Rong ; Jiang, Keji ; Huang, Zhuoshi ; Hsieh, Ming-shiun ; Sun, Xiaofen ; Tang, Kexuan ;
BMB Reports , volume 41, issue 2, 2008, Pages 112~118
DOI : 10.5483/BMBRep.2008.41.2.112
Camptothecin is an anti-cancer monoterpene indole alkaloid. The gene encoding 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (designated as CaHDR), the last catalytic enzyme of the MEP pathway for terpenoid biosynthesis, was isolated from camptothecin-producing Camptotheca acuminata. The full-length cDNA of CaHDR was 1686 bp encoding 459 amino acids. Comparison of the cDNA and genomic DNA of CaHDR revealed that there was no intron in genomic CaHDR. Southern blot analysis indicated that CaHDR belonged to a low-copy gene family. RT-PCR analysis revealed that CaHDR expressed constitutively in all tested plant organs with the highest expression level in flowers, and the expression of CaHDR could be induced by 100
methyl-jasmonate (MeJA), but not by 100 mg/L salicylic acid (SA) in the callus of C. acuminata. The complementation of CaHDR in Escherichia coli ispH mutant MG1655 demonstrated its function.
Cytotoxic activity and probable apoptotic effect of Sph2, a sphigomyelinase hemolysin from Leptospira interrogans strain Lai
Zhang, Yi-xuan ; Geng, Yan ; Yang, Jun-wei ; Guo, Xiao-kui ; Zhao, Guo-ping ;
BMB Reports , volume 41, issue 2, 2008, Pages 119~125
DOI : 10.5483/BMBRep.2008.41.2.119
Our previous work confirmed that Sph2/LA1029 was a sphigomyelinase-like hemolyisn of Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai. Characteristics of both hemolytic and cytotoxic activities of Sph2 were reported in this paper. Sph2 was a heat-labile neutral hemolysin and had similar hemolytic behavior as the typical sphingomyelinase C of Staphylococcus aureus upon sheep erythrocytes. The cytotoxic activity of Sph2 was shown in mammalian cells such as BALB/C mouse lymphocytes and macrophages, as well as human L-02 liver cells. Transmission electron microscopic observation showed that the Sph2 treated BALB/C mouse lymphocytes were swollen and ruptured with membrane breakage. They also demonstrated condensed chromatin as a high-density area. Cytoskeleton changes were observed via fluorescence confocal microscope in Sph2 treated BALB/C mouse lymphocytes and macrophages, where both cytokine IL-
and IL-6 were induced. In addition, typical apoptotic morphological features were observed in Sph2 treated L-02 cells via transmission electron microscope and the percentage of apoptotic cells did increase after the Sph2 treatment detected by flow cytometry. Therefore, Sph2 was likely an apoptosis-inducing factor of human L-02 liver cells.
Detection for folding of the thrombin binding aptamer using label-free electrochemical methods
Cho, Min-Seon ; Kim, Yeon-Wha ; Han, Se-Young ; Min, Kyung-In ; Rahman, Md. Aminur ; Shim, Yoon-Bo ; Ban, Chang-Ill ;
BMB Reports , volume 41, issue 2, 2008, Pages 126~131
DOI : 10.5483/BMBRep.2008.41.2.126
The folding of aptamer immobilized on an Au electrode was successfully detected using label-free electrochemical methods. A thrombin binding DNA aptamer was used as a model system in the presence of various monovalent cations. Impedance spectra showed that the extent to which monovalent cations assist in folding of aptamer is ordered as
. Our XPS analysis also showed that
caused a conformational change of the aptamer in which it forms a stable complex with these monovalent ions. Impedance results for the interaction between aptamer and thrombin indicated that thrombin interacts more with folded aptamer than with unfolded aptamer. The EQCM technique provided a quantitative analysis of these results. In particular, the present impedance results showed that thrombin participates a folding of aptamer to some extent, and XPS analysis confirmed that thrombin stabilizes and induces the folding of aptamer.
AtbZIP16 and AtbZIP68, two new members of GBFs, can interact with other G group bZIPs in Arabidopsis thaliana
Shen, Huaishun ; Cao, Kaiming ; Wang, Xiping ;
BMB Reports , volume 41, issue 2, 2008, Pages 132~138
DOI : 10.5483/BMBRep.2008.41.2.132
AtbZIP16 and AtbZIP68 are two putative G group bZIP transcription factors in Arabidopsis thaliana, the other three members of G group bZIPs are GBF1-3 which can bind G-box. Members of G group have conservative protein structure: highly homological basic region and a proline-rich domain in the N-terminal region. Here, we report that AtbZIP16 and AtbZIP68 could bind cis elements with ACGT core, such as G-box, Hex, C-box and As-1, but with different binding affinities which from high to low were G-box > Hex > C-box > As-1; AtbZIP16 and AtbZIP68 could form homodimer and form heterodimer with other members of G group; N-terminal proline rich domain of AtbZIP16 had transactivation activity in yeast cells while that of AtbZIP68 did not; AtbZIP16 and AtbZIP68 GFP fusion protein localized in the nucleus of onion epidermal cells. These results indicated that AtbZIP16 and AtbZIP68 were two new members of GBFs. In Arabidopsis, AtbZIP16 and AtbZIP68 may also participate in light-responsive process in which GBF1-3 are involved.
Guinea pig cysteinyl leukotriene receptor 2 (gpCysLT2) mediates cell proliferation and intracellular calcium mobilization by LTC4 and LTD4
Ito, Yoshiyuki ; Hirano, Minoru ; Umemoto, Noriko ; Zang, Liqing ; Wang, Zhipeng ; Oka, Takehiko ; Shimada, Yasuhito ; Nishimura, Yuhei ; Kurokawa, Ichiro ; Mizutani, Hitoshi ; Tanaka, Toshio ;
BMB Reports , volume 41, issue 2, 2008, Pages 139~145
DOI : 10.5483/BMBRep.2008.41.2.139
We cloned and pharmacologically characterized the guinea pig cysteinyl leukotriene (CysLT) 2 receptor (gpCysLT2). gpCysLT2 consists of 317 amino acids with 75.3%, 75.2%, 73.3% identity to those of humans, mice and rats, respectively. The gpCysLT2 gene is highly expressed in the lung, moderately in eosinophils, skin, spleen, stomach, colon, and modestly in the small intestine. CysLTs accelerated the proliferation of gpCysLT2-expressing HEK293. Leukotriene C4 (LTC4) and Leukotriene D4 (LTD4) enhanced the cell proliferation higher than Bay-u9773, a CysLT2 selective partial agonist and a nonselective antagonist for CysLT receptors. Bay-u9773 did not antagonize the cell proliferation by LTC4 and LTD4. Despite the equipotency of the mitogenic effect among these chemicals, calcium mobilization (CM) levels were variable (LTC4 > LTD4 >> Bay-u9773), and Bay-u9773 antagonized the CM by LTC4. Moreover, the Gi/o inhibitor pertussis toxin perfectly inhibited agonist-induced cell proliferation. These results reveal that cell proliferation via CysLT2 signaling was mediated by Gi/o signaling but independent of calcium mobilization.
Expression profile identifies novel genes involved in neuronal differentiation
Kim, Jung-Hee ; Lee, Tae-Young ; Yoo, Kyung-Hyun ; Lee, Hyo-Soo ; Cho, Sun-A ; Park, Jong-Hoon ;
BMB Reports , volume 41, issue 2, 2008, Pages 146~152
DOI : 10.5483/BMBRep.2008.41.2.146
In the presence of NGF, PC12 cells extend neuronal processes, cease cell division, become electrically excitable, and undergo several biochemical changes that are detectable in developing sympathetic neurons. We investigated the expression pattern of the apoptosis-related genes at each stage of neuronal differentiation using a cDNA microarray containing 320 apoptosis-related rat genes. By comparing the expression patterns through time-series analysis, we identified candidate genes that appear to regulate neuronal differentiation. Among the candidate genes, HO2 was selected by real-time PCR and Western blot analysis. To identify the roles of selected genes in the stages of neuronal differentiation, transfection of HO2 siRNA in PC12 cells was performed. Down-regulation of HO2 expression causes a reduction in neuronal differentiation in PC12 cells. Our results suggest that the HO2 gene could be related to the regulation of neuronal differentiation levels.
Increased expression of the F
ATP synthase in response to iron in heart mitochondria
Kim, Mi-Sun ; Kim, Jin-Sun ; Cheon, Choong-Ill ; Cho, Dae-Ho ; Park, Jong-Hoon ; Kim, Keun-Il ; Lee, Kyo-Young ; Song, Eun-Sook ;
BMB Reports , volume 41, issue 2, 2008, Pages 153~157
DOI : 10.5483/BMBRep.2008.41.2.153
The objective of the present study was to identify mitochondrial components associated with the damage caused by iron to the rat heart. Decreased cell viability was assessed by increased presence of lactate dehydrogenase (LDH) in serum. To assess the functional integrity of mitochondria, Reactive Oxygen Species (ROS), the Respiratory Control Ratio (RCR), ATP and chelatable iron content were measured in the heart. Chelatable iron increased 15-fold in the mitochondria and ROS increased by 59%. Deterioration of mitochondrial function in the presence of iron was demonstrated by low RCR (46% decrease) and low ATP content (96% decrease). Using two dimensional gel electrophoresis (2DE), we identified alterations in 21 mitochondrial proteins triggered by iron overload. Significantly, expression of the
, and d subunits of
ATP synthase increased along with the loss of ATP. This suggests that the
ATP synthase participates in iron metabolism.
Hepatitis B virus X protein enhances NFκB activity through cooperating with VBP1
Kim, Sang-Yong ; Kim, Jin-Chul ; Kim, Jeong-Ki ; Kim, Hye-Jin ; Lee, Hee-Min ; Choi, Mi-Sun ; Maeng, Pil-Jae ; Ahn, Jeong-Keun ;
BMB Reports , volume 41, issue 2, 2008, Pages 158~163
DOI : 10.5483/BMBRep.2008.41.2.158
Hepatitis B virus X protein (HBx) is essential for hepatitis B virus infection and exerts a pleiotropic effect on various cellular machineries. HBx has been also demonstrated as an indirect transcriptional transactivator of various different viral and cellular promoters. In addition, HBx is involved in the development of various liver diseases including hepatocellular carcinoma. However the mechanism of HBx in hepatocellular carcinogenesis remains largely unknown. In this study, to identify possible new cellular proteins interacting with HBx, we carried out yeast two-hybrid assay. We obtained several possible cellular partners including VBP1, a binding factor for VHL tumor suppressor protein. The direct physical interaction between HBx and VBP1 in vitro and in vivo was confirmed by immunoprecipitation assay. In addition, we found that VBP1 facilitates HBx-induced
activation and cell proliferation. These results implicate the important role of HBx in the development of hepatocellular carcinoma through its interaction with VBP1.
Protective effect of p53 in vascular smooth muscle cells against nitric oxide-induced apoptosis is mediated by up-regulation of heme oxygenase-2
Kim, Young-Myeong ; Choi, Byung-Min ; Kim, Yong-Seok ; Kwon, Young-Guen ; Kibbe, Melina R. ; Billiar, Timothy R. ; Tzeng, Edith ;
BMB Reports , volume 41, issue 2, 2008, Pages 164~169
DOI : 10.5483/BMBRep.2008.41.2.164
The tumor suppressor gene p53 regulates apoptotic cell death and the cell cycle. In this study, we investigated the role of p53 in nitric oxide (NO)-induced apoptosis in vascular smooth muscle cells (VSMCs). We found that the NO donor S-nitroso-N-acetyl-penicillamine (SNAP) increased apoptotic cell death in p53-deficient VSMCs compared with wild-type cells. The heme oxygen-ase (HO) inhibitor tin protoporphyrin IX reduced the resistance of wild-type VSMCs to SNAP-induced cell death. SNAP promoted HO-1 expression in both cell types. HO-2 protein was increased only in wild-type VSMCs following SNAP treatment; however, similar levels of HO-2 mRNA were detected in both cell types. SNAP significantly increased the levels of non-heme-iron and dinitrosyl iron-sulfur clusters in wild-type VSMCs compared with p53-deficient VSMCs. Moreover, pretreatment with FeSO4 and the carbon monoxide donor CORM-2, but not biliverdin, significantly protected p53-deficient cells from SNAP-induced cell death compared with normal cells. These results suggest that wild-type VSMCs are more resistant to NO-mediated apoptosis than p53-deficient VSMCs through p53-dependent up-regulation of HO-2.
Protein transduction of an antioxidant enzyme: subcellular localization of superoxide dismutase fusion protein in cells
Kim, Dae-Won ; Kim, So-Young ; Lee, Hwa ; Lee, Yeum-Pyo ; Lee, Min-Jung ; Jeong, Min-Seop ; Jang, Sang-Ho ; Park, Jin-Seu ; Lee, Kil-Soo ; Kang, Tae-Cheon ; Won, Moo-Ho ; Cho, Sung-Woo ; Kwon, Oh-Shin ; Eum, Won-Sik ; Choi, Soo-Young ;
BMB Reports , volume 41, issue 2, 2008, Pages 170~175
DOI : 10.5483/BMBRep.2008.41.2.170
In protein therapy, it is important for exogenous protein to be delivered into the target subcellular localization. To transduce a therapeutic protein into its specific subcellular localization, we synthesized nuclear localization signal (NLS) and membrane translocation sequence signal (MTS) peptides and produced a genetic in-frame SOD fusion protein. The purified SOD fusion proteins were efficiently transduced into mammalian cells with enzymatic activities. Immunofluorescence and Western blot analysis revealed that the SOD fusion proteins successfully transduced into the nucleus and the cytosol in the cells. The viability of cells treated with paraquat was markedly increased by the transduced fusion proteins. Thus, our results suggest that these peptides should be useful for targeting the specific localization of therapeutic proteins in various human diseases.