• Title/Summary/Keyword: glucose isomerase

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Potential Role of Bacterial Infection in Autoimmune Diseases: A New Aspect of Molecular Mimicry

  • Alam, Jehan;Kim, Yong Chul;Choi, Youngnim
    • IMMUNE NETWORK
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    • v.14 no.1
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    • pp.7-13
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    • 2014
  • Molecular mimicry is an attractive mechanism for triggering autoimmunity. In this review, we explore the potential role of evolutionary conserved bacterial proteins in the production of autoantibodies with focus on granulomatosis with polyangiitis (GPA) and rheumatoid arthritis (RA). Seven autoantigens characterized in GPA and RA were BLASTed against a bacterial protein database. Of the seven autoantigens, proteinase 3, type II collagen, binding immunoglobulin protein, glucose-6-phosphate isomerase, ${\alpha}$-enolase, and heterogeneous nuclear ribonuclear protein have well-conserved bacterial orthologs. Importantly, those bacterial orthologs are also found in human-associated bacteria. The wide distribution of the highly conserved stress proteins or enzymes among the members of the normal flora and common infectious microorganisms raises a new question on how cross-reactive autoantibodies are not produced during the immune response to these bacteria in most healthy people. Understanding the mechanisms that deselect auto-reactive B cell clones during the germinal center reaction to homologous foreign antigens may provide a novel strategy to treat autoimmune diseases.

Purification and Characterization of a Regulatory Protein XyIR in the D-Xylose Operon from Escherichia coli

  • Shin, Jae-Ho;Roh, Dong-Hyun;Heo, Gun-Young;Joo, Gil-Jae;Rhee, In-Koo
    • Journal of Microbiology and Biotechnology
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    • v.11 no.6
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    • pp.1002-1010
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    • 2001
  • The D-xylose operon in Escherichia coli is known to be regulated by a transcriptional activator protein, XyIR, which is responsible for the expression of both xylAB and xylFGH gene clusters. The XyIR was purified to homogeneity by using the maltose binding protein fusion expression and purification systems involving two chromatography steps. The purified XyIR protein was composed of two subunits of 45 kDa, which was determined by both sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration. The purified XyIR was specifically bounded to the xylA promoter, regardless of adding xylose to the reaction mixture, but binding of XylR was specifically bounded to the xylA promoter, regardless of adding xylose to the reaction mixture, but binding of XylR to the xylA promoter was enhanced by adding xylose. The enhanced binding ability of XyIR in the presence of xylose was not diminished by adding glucose. The presumed XyIR binding site is located between 120 bp to 100 bp upstream the xylA initiation codon.

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Systemetic Study on the Family Pectinidae (Bivalvia) in Korea. Allozyme Variability (한국산 가리비과(Pectinidae: Bivalvia) 패류의 계통분류학적 연구. 동이원소)

  • 김재진;박갑만
    • The Korean Journal of Malacology
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    • v.15 no.1
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    • pp.63-69
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    • 1999
  • Electrophoretic analysis was carried out to elucidate genetic relationships of four Korean scallops, Patinopecten yessoensis, chlamys ferreri ferreri, Chlamys swifti and Amusium japonicum japonicum, and of a Chinese population of C. ferreri ferreri purchased form a market. Glucose phosphate isomerase banding pattern was highly varied among eight loci. Three populations of C. ferreri ferreri were more closely clustered in a dendrogram within the range of Nei's genetic similarity values of 0.730-0.830. P. yessoenensis and Chlamys swifti were clustered with genetic similarity value of 0.647. These two clusters were lineated at the value of 0.598. A. japonicum japonicum was clustered with other three species at value of 0.541.

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Isozyme Variability in Two Species of Freshwater Viviparid Snails in Korea : Cipangopaludina chinensis malleata and C. Japonica (한국산 논우렁이과 ( Family Viviparidae ) 2종에서의 동위효소 변이)

  • 정평림;정영헌;박준우;정기헌
    • The Korean Journal of Malacology
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    • v.14 no.1
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    • pp.33-40
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    • 1998
  • A horizontal starch gel electrophoresis for enzyme proteins extracted from 2 species of Korean viviparid snails; Cipangopaludina chinensis malleata and C. japonica was carried out in order to elucidate their genetic relationships. A total of 10 enzymes were employed in three different kinds of buffer systems. Two loci from each enzyme of alcohol dehydrogenase, esterase, glucose phosphate isomerase, isocitrate dehydrogenase, iditol dehydrogenase, malate dehydrogenase and peptidase(VL); and only one locus dach from two enzymes, glycerlo-3-phosphate dehydrogenase and phosphoglucomutase were detected; but, four loci from peptidase(LGG) were observed. Most of loci in two viviparid species showed homozygous monomorphic banding patterns and some of them were specific as genetic markers between two different species. However, EST-1, MDH-1, PEP(VL)-1loci showed polymorphic banding patterns. Foru populations of C. chinensis malleata were more closely clustered in a dendrogram within the range of genetic identity values of 0.928-1.00, and these clusters were lineated with C. japonica at the value of 0.355. In summarizing the above results, two viviparid snail species dmployed in this study mostly showed monomorphic enzyme protein banding patterns, and genetic differences specific between two species.

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Expression of Acid Stress-Induced Proteins of Streptococcus mutans Isolated from Korean Children with Caries (한국인 우식아동으로부터 분리한 Streptococcus mutans의 내산성 단백질의 발현)

  • Kang, Kyung-Hee;Nam, Jin-Sik;Jin, Ing-Nyol
    • Journal of the Korea Academia-Industrial cooperation Society
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    • v.10 no.7
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    • pp.1766-1772
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    • 2009
  • In this study, we are interested in comparing the protein profiles of acid-shocked and control cells of S. mutans isolated from Korean children with caries. The results of 2D gel electrophoresis showed that twelve proteins are up-regulated when the cells were grown under 20 mM lactic acid stress in the exponential phase. Up-proteins under acid stress were estimated a major key of the survival and proliferation of S. mutans in low pH environments. These proteins are estimated generally associated with three biochemical pathways: glycolysis, alternative acid production and branched-chain amino acid biosynthesis.

Detoxification Mechanism and Isoenzyme Pattern Changes against Cadmium in Rhizopus oryzae (Rhizopus oryzae의 카드뮴 해독기작과 이에 관련된 동위효소의 변화 양상)

  • Lee, Ki-Sung;Kim, Young-Ho;Park, Young-Sik;Park, Yong-Keun
    • The Korean Journal of Mycology
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    • v.23 no.1 s.72
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    • pp.86-91
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    • 1995
  • Isoenzymatic analysis related with cadmium adaptation and detoxifying mechanism were carried out upon Rhizopus oryzae. When cadmium was added into R. oryzae culture, activities of malate dehydrogenase (MDH) and glucose phosphate isomerase (GPI) related with carbohydrate metabolizing pathways were stimulated. Novel isoenzyme CAT-2 related with removing intracellular toxic peroxides, was induced lately and derepressed very highly. On the other hand, lactate-catabolizing enzymes such as lactate dehydrogenase (LDH) and alcohol dehydrogenase (ADH) were repressed. These results strongly suggest that, under cadmium stress, much of derepression of enzymes relating with central metabolism such as TCA cycle that produces high yield of energy and relating with removal of toxic peroxides should be necessary.

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Species-specific Expression of Rpia Transcript in Cumulus-oocyte-complex (난자-난구세포 복합체에서 발현하는 Rpia 유전자의 종 특이적 발현)

  • Kim, Yun-Sun;Yoon, Se-Jin;Kim, Eun-Young;Lee, Kyung-Ah
    • Clinical and Experimental Reproductive Medicine
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    • v.34 no.2
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    • pp.95-106
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    • 2007
  • Objective: We previously identified differentially expressed genes (DEGs) between germinal vesicle (GV) and metaphase II (MII) mouse oocyte. The present study was accomplished as a preliminary study to elucidate the role of ribose 5-phosphate isomerase A (Rpia), the essential enzyme of the pentose phosphate pathway (PPP), in oocyte maturation. We observed expression of Rpia in the mouse and porcine oocytes. Methods: Expression pattern of the 11 MII-selective DEGs in various tissues was evaluated using RT-PCR and selected 4 genes highly expressed in the ovary. According to the oocyte-selective expression profile, we selected Rpia as a target for this study. We identified the porcine Rpia sequence using EST clustering technique, since it is not yet registered in public databases. Results: The extended porcine Rpia nucleotide sequence was submitted and registered to GenBank (accession number EF213106). We prepared primers for porcine Rpia according to this sequence. In contrast to the oocyte-specific expression in the mouse, Rpia was expressed in porcine cumulus and granulosa cells as well as in oocytes. Conclusion: This is the first report on the characterization of the Rpia gene in the mouse and porcine ovarian cells. Results of the present study suggest that the mouse and porcine COCs employ different mechanism of glucose metabolism. Therefore, the different metabolic pathways during in vitro oocyte maturation (IVM) in different species may lead different maturation rates. It is required to study further regarding the role of Rpia in glucose metabolism of oocytes and follicular cell fore exploring the regulatory mechanism of oocyte maturation as well as for finding the finest culture conditions for in vitro maturation.

Production of Xylooligo-Saccharides and Purification of Extracellular Xylanase from Streptomyces chibaensis J-59 (방선균 Streptomyces chibaensis J-59 Xylanase의 정제 및 자일로 올리고당(Xylooligo-Saccharides)의 생산)

  • Joo, Gil-Jae;Rhee, In-Koo
    • Current Research on Agriculture and Life Sciences
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    • v.14
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    • pp.111-122
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    • 1996
  • S. chibaensis J-59 produced an extracellular xylanase in a CSL medium composed of 1.5% com steep liquor, 0.1% $MgSO_4{\cdot}7H_2O$, 0.012% $CoCl_2{\cdot}6H_2O$, and 0.15% glucose containing xylan. but it did not produce in the culture medium containing xylose. The production of enzyme reached to a maximum level (0.83 uints/ml) when bacteria were cultured in 2.5 l jar fermentor for 48hrs at $30^{\circ}C$ and pH 7.0. Furthermore, S. chibaensis J-59 produced an intracellular glucose isomerase in a medium containing xylan and/or xylose. Xylanase was purified 29-fold over the culture supernatants of S. chibaensis J-59 by ammonium sulfate fractionation, chromatography on DEAE-Sephadex A-50, and gel filtration on Sephadex G-200. The purified enzyme is a monomeric enzyme with a native molecular mass of 25 kDa and a subunit molecular mass of 25 kDa. The purified enzyme requires $Mg^{2+}$ for activity, $Ca^{2+}$, $Co^{2+}$ is not an inhibitor but inhibit by $Fe^{3+}$, $Hg^{2+}$, and $Cu^{2+}$, sodium dodecyl sulfate, N-bromosuccinide. Pattern of hydrolysis demonstrated that the xylanase was an endo-splitting enzyme able to break down birchwood xylan at random giving xylobiose, xylotriose and xylotetrose as the main end products.

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CD4+CD25+ Regulatory T Cells Selectively Diminish Systemic Autoreactivity in Arthritic K/BxN Mice

  • Kang, Sang Mee;Jang, Eunkyeong;Paik, Doo-Jin;Jang, Young-Ju;Youn, Jeehee
    • Molecules and Cells
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    • v.25 no.1
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    • pp.64-69
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    • 2008
  • Although the arthritis symptoms observed in the K/BxN model have been shown to be dependent on the functions of T and B cells specific to the self antigen glucose-6-phosphate isomerase, less is known about the in vivo roles of $CD4^{+}CD25^{+}$ regulatory T($T_{reg}$) cells in the pathology of K/BxN mice. We determined the quantitative and functional characteristics of the $T_{reg}$ cells in K/BxN mice. These mice contained a higher percentage of $Foxp3^+\;T_{reg}$ cells among the $CD4^+$ T cells than their BxN littermates. These $T_{reg}$ cells were anergic and efficiently suppressed the proliferation of $na\ddot{i}ve$ $CD4^+$ T cells and cytokine production by effector $CD4^+$ T cells in vitro. Antibody-mediated depletion of $CD25^+$ cells caused K/BxN mice to develop multi-organ inflammation and autoantibody production, while the symptoms of arthritis were not affected. These results demonstrate that despite the inability of the $T_{reg}$ cells to suppress arthritis development, they play a critical role protecting the arthritic mice from systemic expansion of autoimmunity.

Analysis of Functional Genes in Carbohydrate Metabolic Pathway of Anaerobic Rumen Fungus Neocallimastix frontalis PMA02

  • Kwon, Mi;Song, Jaeyong;Ha, Jong K.;Park, Hong-Seog;Chang, Jongsoo
    • Asian-Australasian Journal of Animal Sciences
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    • v.22 no.11
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    • pp.1555-1565
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    • 2009
  • Anaerobic rumen fungi have been regarded as good genetic resources for enzyme production which might be useful for feed supplements, bio-energy production, bio-remediation and other industrial purposes. In this study, an expressed sequence tag (EST) library of the rumen anaerobic fungus Neocallimastix frontalis was constructed and functional genes from the EST library were analyzed to elucidate carbohydrate metabolism of anaerobic fungi. From 10,080 acquired clones, 9,569 clones with average size of 628 bp were selected for analysis. After the assembling process, 1,410 contigs were assembled and 1,369 sequences remained as singletons. 1,192 sequences were matched with proteins in the public data base with known function and 693 of them were matched with proteins isolated from fungi. One hundred and fifty four sequences were classified as genes related with biological process and 328 sequences were classified as genes related with cellular components. Most of the enzymes in the pathway of glucose metabolism were successfully isolated via construction of 10,080 ESTs. Four kinds of hemi-cellulase were isolated such as mannanase, xylose isomerase, xylan esterase, and xylanase. Five $\beta$-glucosidases with at least three different conserved domain structures were isolated. Ten cellulases with at least five different conserved domain structures were isolated. This is the first solid data supporting the expression of a multiple enzyme system in the fungus N. frontalis for polysaccharide hydrolysis.