• Molecules and Cells
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• v.23 no.1
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• pp.1-10
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• 2007

Invading pathogens are recognized by diverse germline-encoded pattern-recognition receptors (PRRs) which are distributed in three different cellular compartments: extracellular, membrane, and cytoplasmic. In mammals, the major extracellular PRRs such as complements may first encounter the invading pathogens and opsonize them for clearance by phagocytosis which is mediated by membrane-associated phagocytic receptors including complement receptors. The major membrane-associated PRRs, Toll-like receptors, recognize diverse pathogens and generate inflammatory signals to coordinate innate immune responses and shape adaptive immune responses. Furthemore, certain membrane-associated PRRs such as Dectin-1 can mediate phagocytosis and also induce inflammatory response. When these more forefront detection systems are avoided by the pathogens, cytoplasmic PRRs may play major roles. Cytoplasmic caspase-recruiting domain (CARD) helicases such as retinoic acid-inducible protein I (RIG-I)/melanoma differentiation-associated gene 5 (MDA5), mediate antiviral immunity by inducing the production of type I interferons. Certain members of nucleotide-binding oligomerization domain (NOD)-like receptors such as NALP3 present in the cytosol form inflammasomes to induce inflammatory responses upon ligand recognition. Thus, diverse families of PRRs coordinately mediate immune responses against diverse types of pathogens.

• Journal of Embryo Transfer
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• v.8 no.2
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• pp.83-90
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• 1993

To investigate the effect of extracellular matrix proteins on the in vitro development of ethanol-induced parthenogenetic eggs of ICR strain mice, those were cultured in vitro in fibronectin, gelatin, or collagen precoated culture dishes containing 1.5 ml of NaH-C03$_3$-BMOC-3 medium at 37$^{\circ}C$ for 96 hrs. under the atmosphere of 5% $CO_2$ and 95% air. Fibronectin, gelatin, or collagen significantly(P$\pm$1.4, 45.4i1.4, and 44.8$\pm$O.9, respectively. And the diameter of those eggs ranged 104.6$\pm$1.9, 102.8$\pm$2.3, and 103.4$\pm$O.8 $\mu$m, respectively.

• Journal of Microbiology and Biotechnology
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• v.6 no.6
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• pp.439-444
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• 1996

A bacterial strain, designated as WY22, producing extracellular chitinase was isolated from the soil around the Youngduck area, after enrichment culture in a medium containing $1{\%}$ (w/v) wet colloidal chitin as a sole carbon source. The isolate was identified as a strain of Bacillus sp. based on its morphological and physiological characteristics. It was observed that Bacillus sp. WY22 could inhibit the growth of Fusarium oxysporum with hyphal extention-inhibition assay on potato dextrose agar plate supplemented with $1{\%}$ collidal chitin. Optimum culture conditions of Bacillus sp. WY22 were examined for chitinase production in a chitin medium. High level production of chitinase was observed not only in the chitin medium but in a medium supplemented with $1{\%}$ N-glucosamine or lactose instead of chitin. The optimum concentrations of colloidal chitin and yeast extract were 3.0 and $0.5{\%}$, and the optimum culture conditions for initial pH of medium and temperature were 7.0 and $30^{\circ}C$, respectively, for the production of chitinase.

• Microbiology and Biotechnology Letters
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• v.24 no.4
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• pp.408-414
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• 1996

The SecY is a central component of the protein export machinery that mediate the translocation of secretory proteins across the plasma membrane, and has been known to be rate-limiting factor of secretion in Escherichia coli. In order to study the extracellular protein secretion in Gram-positive microorganism, we have, constructed strains harboring more than one copy of the gene for SecY. Firstly, the gene, for B. subtilis SecY and its promoter region was subcloned into pDH32 and the chimeric vector was inserted into amyE locus by homologous recombination. Secondly, low copy number vector, pCED6, was also used for subcloning the secY gene and for constructing a strain which harbors several copies of secY. The KH1 cell which harbor two copies of secY on the chromosome excreted more extracellular proteins than the wild type PB2. Moreover, the KH2 cells which harbor several copies of secY in pCED6 vector excreted more extracellular proteins than the KH1 cells. Here, we found that the capacity of protein secretion is partly controlled by the number of secY and it is suggested that SecY has also an important role in protein secretion in B. subtilis, a gram positive microorganism, as like in E. coli. This will promote the use of B. subtilis as a host for the expression of useful foreign gene and excretion of precious proteins.

• Journal of Physiology & Pathology in Korean Medicine
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• v.27 no.5
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• pp.563-569
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• 2013

This study was undertaken to apply the yin-yang theory in action potential. In order to apply the yin-yang theory in action potential, nature of yin and yang, interrelation of yin and yang and action potential in cell were reviewed. According to the yin-yang theory, inner cellular space corresponds to yin, but outer cellular space corresponds to yang. If we classify ions in intracellular fluid or extracellular fluid by nature of yin and yang, potassium(K+) corresponds to yang within yin(陰中之陽), protein(Pr-) corresponds to yin within yin(陰中之陰) in intracellular fluid, and sodium(Na+) corresponds to yang within yang(陽中之陽), chloride(Cl-) corresponds to yin within yang(陽中之陰) in extracellular fluid. Double donnan equilibrium and equilibrium potential were caused by intracellular anion(Pr-) and extracellular cation(Na+) are related with mutual rooting of yin and yang(陰陽互根) and opposition of yin and yang(陰陽對立). The influx and efflux of ion through cell membrane means waxing and waning of yin and yang(陰陽消長), the change of membrane potential means yin-yang conversion(陰陽轉化) during action potential.

• Korean Journal of Microbiology
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• v.28 no.1
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• pp.83-89
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• 1990

Two strains of actinomycetes producing extracellular adenosine deaminase, strain J-845S and strain J-326TK, were isolated from soil. Strain J-845S was gram-positive and non-acid-fast. This strain formed whitish, rod-shaped, smooth and non-motile spores on the aerial mycelium, and the spore chain was spiral. The hyphae of the mycelium branched abundantly. Cell wall chemotypes of the strain were of type I containing LL-diaminopimelic acids, and of phospholipid type II, and then strain J-845S was designated as Streptomyces sp.. Strain J-326TK was gram-positive and non-acid-fast. The hyphae of primary and aerial mycelium fragmented into irregular rod of coccus-like elements. The aerial mycelium either did not branch or sparsely branched. Cell wall composition was of type I and phospholipid type I. Thus, strain J-326TK was identified as Nocardioides sp.

• Biotechnology and Bioprocess Engineering:BBE
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• v.6 no.4
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• pp.264-268
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• 2001

Aggregates of specific cells are often regarded as better from in artificial organs and mammalian cell bioreactors in terms of cell-specific functionality. In this study, the morphology and liver specific functions of freshly harvested primary rat hepatocytes, which were cultivated as spheroids and entrapped in a synthetic thermo-reversible extracellular matrix, were examined and compared to a control (hepatocytes in single cell form). A copolymer of N-isopropylacrylamide(98 mole % in feed) and acrylic acid (poly (NiPAAm-co-AAC)), a thermo- reversible copolymer gel ma- trix, was used to entrap hepatocytes either in spheroids or single cells. During a 7-day culture pe-riod, the spheroids maintained higher viability and produced albumin and urea at a relatively con-stant rate, while, the single cell culture showed a slight increase in cell numbers and a reduction in albumin secretion Hepatocytes cultrured as spheroids present a potentially useful three-dimensional cell culture system for application in bioartificial liver device.

• Korean Journal of Microbiology
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• v.30 no.3
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• pp.149-153
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• 1992

Cloning of the gene encoding extracellular .betha.-lactamase from Streptomyces sp. SMF13 in a plasmid pIJ702 and expression of the gene in Streptomyces invidans were carried out. Optimal conditions for the formation of protoplasts of S.lividans and the regeneration of the protoplasts were evaluated. Streptomyces sp. SMF-13 was selected as a donor strain of .betha.-lactamase gene and totla DNA of the strain was partially digested with Sau3A I. DNA fragments ranged from 4kb to 10 kb were ligated to pIJ702 AT Bgl II site and then the ligated DNAs were transformed to the protoplasts of S, livivans. The transformation efficiency was $2 *10^{3}$ .$\mu$g DNA for the ligated DNA mixture. One colony among a thousand colonies regenerated showed extracellular .betha.-lactamase and the size of the inserted DNA fragment was estimated to be 3.94 kb. The .betha.-lactamase activity in the culture broth of the recombinant strain was maximum at 3 days culture to be 1.0 unit/ml.

• BMB Reports
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• v.34 no.1
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• pp.85-89
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• 2001

Both topoisomerase $II{\alpha}$ and $II{\beta}$ east as phosphoproteins in the cells. Recently it was reported that DNA topoisomerase $II{\alpha}$ associates with and is phosphorylated by the extracellular signal-regulated kinase 2 (ERK2). Also, ERK2 stimulates the activity of topoisomerase II by a phosphorylation-independent manner [Shapiro et al., (1999) Mol. Cell. Biol. 19, 3551-3560]. In this study, a yeast two-hybrid system was used to investigate the binding site between topoisomerase $II{\alpha}$ or $II{\beta}$ and ERK2. The two-hybrid test clearly showed that topoisomerase $II{\beta}$ residues 1099-1263, and topoisomerase $II{\alpha}$ residues 1078-1182, mediate the interaction with ERK2, and that the leucine zipper motifs of topoisomerase $II{\alpha}$ and $II{\beta}$ are not required for its physical binding to ERK2. Our results suggest that topoisomerase $II{\beta}$ residues 1099-1263, and topoisomerase $II{\alpha}$ residues 1078-1182, may be common binding sites for activator proteins.

• Journal of Microbiology and Biotechnology
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• v.8 no.6
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• pp.581-587
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• 1998

Essential amino acids involved in the catalytic role of the extracellular cytosine deaminase from Chromobacterium violaceum YK 391 were determined by chemical modification studies. The enzyme activity required the reduced form of Fe (II) ion, since the enzyme was inhibited by ο-phenanthroline. The enzyme activity was completely inhibited by the chemical modifiers, such as p-chloromercuribenzoate (p-CMB), p-hydroxymercuribenzoate, and chloramine-T at 1 mM each. The enzyme activity was also markedly inhibited by pyridoxal-5'-phosphate, diethyl pyrocarbonate, and phenylmethylsulfonyl fluroride at 1 mM each. The inactivation of the enzyme activity with p-CMB was reversed by a high concentration of cytosine. Furthermore, the inactivation of the enzyme activity with p-CMB was also reactivated by 1 mM dithiothreitol, 1 mM 2-mercaptoethanol, 1 mM cysteine-HCI, 10% ethyl alcohol, and 10% methyl alcohol. These results suggested that cysteine and methionine residues might be located in or near the active site of the enzyme, while lysine, histidine, and serine residues might be indirectly involved in the enzyme activity.