• Title/Summary/Keyword: 1-2 toxin

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Application of botulinum toxin in maxillofacial field: Part II. Wrinkle, intraoral ulcer, and cranio-maxillofacial pain

  • Kwon, Kyung-Hwan;Shin, Kyung Su;Yeon, Sung Hee;Kwon, Dae Gun
    • Maxillofacial Plastic and Reconstructive Surgery
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    • v.41
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    • pp.42.1-42.15
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    • 2019
  • Botulinum toxin (BTX) is used in various ways such as temporarily resolving muscular problems in musculoskeletal temporomandibular disorders, inducing a decrease in bruxism through a change in muscular patterns in a patient's bruxism, and solving problems in patients with tension headache. And also, BTX is widely used in cosmetic applications for the treatment of facial wrinkles after local injection, but conditions such as temporomandibular joint disorders, headache, and neuropathic facial pain could be treated with this drug. In this report, we will discuss the clinical use of BTX for facial wrinkle, intraoral ulcer, and cranio-maxillofacial pain with previous studies and share our case.

Effect of Api-Toxin Therapy on Depression of Immune Response in Mice (봉독침자극(蜂毒鍼刺戟)이 생쥐의 면역기능(免疫機能)에 미치는 영향(影響))

  • Kang, Seung-Bum;Koh, Hyung-Kyun;Kim, Chang-Hwan
    • The Journal of Korean Medicine
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    • v.17 no.1 s.31
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    • pp.234-246
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    • 1996
  • In order to investigate the effects of api-toxin therapy on depression of immune response, mice were exposed to cold stress $(-20^{\circ}C)$) in 30 minutes twice a day and api-toxin(Bee Venom from Korea and U.S.A) therapy was treated to the Kihae $(CV_6)$ locus of human body every two days with 4 sessions of treatment for 8 days. The mice were sensitized i.v. with $5{\times}10^8$ sheep red blood cells (SRBC) on the 4th day and challenged i.d. with $2{\times}10^9$ SRBC 4 days later. Immune Response for delayed type hypersensitivity (DTH), lympocyte transformation(LTT), hemolysin titer(HL), plaque forming cells (PFC) were measured.

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Characterization of a Toxin isolated from Bacillus thuringiensis var. alesti and Its Toxicity to the Silkworm, Bombyx mori (Bacillus thuringiensis var. alesti로부터 분리된 독소의 성상과 누에에 대한 독성)

  • 이영근;조용섭;임종성
    • Journal of Sericultural and Entomological Science
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    • v.17 no.1
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    • pp.55-62
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    • 1975
  • In the studies of characterization of crystal prototoxin isolated from Bacillus thuringinensis var. alesti and its bioassay to the silkworm larvae, Bombyx mori L., the following results were obtained. 1. The complete lysis of bacteria grown on the nutrient agar at 30$^{\circ}C$ in an incubator took 30 days, but the period could be reduced by a half in a devised broth media in a fermentation jar. 2. The protein toxin extracted directly from a mixture of crystals and spores without separation of crystals and spores was pure as same as the protein toxin extracted from only crysals separated. 3. By SLS polyacrylamide gel electrophoresis of prototoxin released from crystals in alkali (pH 9.5) three different proteins in molecular weights of 120,000, 87,000, 74,000 were separated. 4. In the bioassay of the toxin to the silkworm larvae, LD$\sub$50/ per gram of the larvae in the 4th instar was 0.080 $\mu\textrm{g}$.

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Co-expression of CdtA and CdtC subunits of cytolethal distending toxin from Aggregatibacter actinomycetemcomitans

  • Lee, Seung-Jae;Lee, Kyung-Yeol;Kim, Hyung-Seop
    • Journal of Periodontal and Implant Science
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    • v.39 no.sup2
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    • pp.231-237
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    • 2009
  • Purpose: Cytolethal distending toxin (CDT) is a family of heat-labile cytotoxins produced by several gram-negative mucosa-associated pathogens, including Aggregatibacter actinomycetemcomitans. CDT is well known to be capable of inducing growth arrest, morphological alterations, and eventually death in various cells. CDT belongs to a tripartite $AB_2$ toxin (CdtB: the enzymatic A subunit; CdtA and CdtC: the heterodimeric B subunit). Previous studies proposed that CdtA and CdtC together bind to a cell surface receptor and glycolipids act as a receptor for A. actinomycetemcomitans CDT (AaCDT). In this study, recombinant CdtA and CdtC proteins of AaCDT were co-expressed in a bacterial expression system and tested for their affinity for $GM_1$ ganglioside. Methods: The genes for CdtA and CdtC from A. actinomycetemcomitans Y4 were utilized to construct the expression vectors, pRSET-cdtA and pET28a-cdtC. Both CdtA and CdtC proteins were expressed in Escherichia coli BL21(DE3) and then purified using hexahistidine (His6) tag. The identity of purified protein was confirmed by anti-His6 antibody and monoclonal anti-CdtA antibody. Furthermore, the affinity of recombinant protein to $GM_1$ ganglioside was checked through ELISA. Results: Recombinant CdtA and CdtC proteins were expressed as soluble proteins and reacted to anti-His6 and monoclonal anti-CdtA antibodies. ELISA revealed that purified soluble CdtA-CdtC protein bound to $GM_1$ ganglioside, while CdtA alone did not. Conclusions: Co-expression of CdtA and CdtC proteins enhanced the solubility of the proteins in E. coli, leading to convenient preparation of active CdtA-CdtC, a critical material for the study of AaCDT pathogenesis.

Analysis of Total Aflatoxin, Ochratoxin A, Zearalenone, Deoxynivalenol and T-2 Toxin Contamination in Nuts (시중유통 견과류의 총아플라톡신, 오크라톡신 A, 제랄레논, 데옥시니발레놀, T-2 독소의 오염도 조사)

  • Hong, JoonBae;Park, Kun Taek
    • Journal of Food Hygiene and Safety
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    • v.34 no.1
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    • pp.58-64
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    • 2019
  • In the current study, 109 commercial nut samples were collected from different Korean markets and analyzed for the contamination of 5 different mycotoxins (aflatoxin, ochratoxin A, deoxynivalenol, zearalenone, and T-2 toxin) using ELISA kits. The results revealed that the most frequently detected mycotoxin was zearalenone (n=36, 33%), followed by aflatoxin (n=31, 28.4%) and ochratoxin A (n=30, 27.5%). Deoxynivalenol and T-2 toxin were also detected in 22 (20.3%) samples, respectively. Among 109 nut samples, 33 samples (30.3%) were contaminated only with one kind of mycotoxin, whereas 43 samples had at least 2 kinds of mycotoxins. Two samples were contaminated with as many as 4 different mycotoxins, and they were both walnuts. Although the monitoring results revealed the amount of aflatoxin contamination was under the safety criteria, there is no current safety guideline for other kinds of mycotoxins or multiple contaminations in Korea. Therefore, further studies should be performed to reveal the distribution of mycotoxin in different foods and propose appropriate safety guidelines for Korean markets.

Regulation of Insulin-Sensitive Cyclic Nucleotide Phosphodiesterase in Adipocytes of Streptozotocin-Induced Diabetic Rats (Streptozotocin으로 당뇨병을 유발시킨 흰쥐의 지방세포에서 일어나는 Insulin-Sensitive Phosphodiesterase의 조절에 관한 연구)

  • Park, Kyung-Sun;Lee, Myung-Soon;Kim, Kyung-Hwan
    • The Korean Journal of Pharmacology
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    • v.29 no.2
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    • pp.253-261
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    • 1993
  • Possible changes in the role of insulin-sensitive cyclic nucleotide phosphodiesterase(PDE) in mediating the antilipolytic action of insulin were investigated in adipocytes from streptozotocin-induced diabetic rats. Isolated adipocytes prepared from epididymal adipose tissue were incubated, with or without insulin, at $37^{\circ}C$ for 15 min following pretreatment with various drugs or toxins, and three (plasma membranes, microsomal membranes, and cytosol) fractions prepared by differential centrifugation were then assayed for cAMP phosphodiesterase activity. The PDE activities only in the crude microsomal (P2) fractions were activated by insulin both in diabetic and control rats. The basal PDE activities in P2 fractions of adipocytes from diabetic rats were higher than those from control rats, although the maximal effects observed at 2 nM of insulin, $100\;{\mu}M$ of isoproterenol or the combination of both were not significantly different from each other. The insulin-stimulated PDE activities in P2 fractions of adipocytes from diabetic rats were not changed by PIA, a $A_{1}$ adenosine receptor agonist, whereas they were decreased to the basal PDE activities in those from control rats. In addition, the adipocytes from diabetic rats showed an increased sensitivity to pertussis toxin compared to those from controls. There were no differences between diabetic and control rats in the sensitivity of adipocytes to cholera toxin. These data indicate that the impaired signalling through inhibitory receptors such as adenosine receptors in adipocytes from streptozotocin-induced diabetes relates to the loss or the decreased function of $G_i$ proteins, and leads to the increased activity of the insulin-dependent PDE at the basal states.

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Expression and Characterization of Helicobacter pylori Adhesin Protein Linked to Cholera Toxin A2/B Subunits in Escherichia coli

  • Kim, Byung-Oh;Shin, Sung-Seup;Yoo, Young-Hyo;Pyo, Shuk-Neung
    • Journal of Microbiology and Biotechnology
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    • v.10 no.1
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    • pp.56-62
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    • 2000
  • The hpa gene genetically linked to the ctxa2b gene was cloned into the pTED expression vector, and the constructed pTEDhpa/ctxa2b was transformed into Excherichia coli. The fusion protein, the adhesin fused to the cholera toxin subunit A2B (CTXA2B) subunit, was expressed to high levels as inclusion bodies in E. coli. The expressed protein was partially purified by washing the inclusion bodies with working solution containing 8M Urea and 0.1M DTT. Refolding of denatured fusion protein was carried out in the presence of glutathione redox buffer. The refolded fusion protein was purified by size exclusion chromatography. The expressed fusion protein was verified by SDS-PAGE, western blotting with antibodies to both antigenic components of adhesin and cholera toxin subunit B (CTXB), and its N-terminal amino acid sequence was analyzed. The orderly assembled fusion protein was confirmed by modified Gm1-ganglioside ELISA with Abs to adhesin. The results indicate that the purified fusion protein is an Adhesin/CTXA2B protein containing the H. pylori adhesin and $G_{m1}4-ganglioside binding activity of CTXB and the expressed fusion protein in E. coli could be easily purified by the refolding process, Its molecular weight was 168kDa as estimated by size exclusion chromatography. The Adhesin/CTXA2B protein may be used as a candidate antigen for oral immunization against H. pylori.

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Isolation and Purification of Lipopolysaccharide Derived from Escherichia coli O157:H7 for the Specific Antibody Production (병원성 Escherichia coli O157:H7의 특이 항체 생산을 위한 Lipopolysaccharide분리 및 정제)

  • 최학선;신영민;정숙현;박영민;안원근
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.33 no.3
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    • pp.571-575
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    • 2004
  • Escherichia coli O157:H7 cause hemorrhagic colitis and the extraintestinal complication of hemolytic-uremic syndrome, with their higher incidence occurring in children. Lipopolysaccharide (LPS) of E. coli O157:H7 is very important to make IgG anti-LPS with bactericidal activity. To identify the characteristic of E. coli OI57:H7, we isolated 60 MDa plasmid and amplified stx genes of shiga-like toxin (Stx) 1, 2 of E. coli O157:H7 by polymerase chain reaction (PCR) method. Using the simple purification method which contained phenol extract, ethanol precipitation and gel filtration steps, the LPS of E. coli O157:H7 was isolated and purified. Finally, we confirmed the purity of LPS through SDS-PAGE and silver nitrate staining.

Reestablishment of Approval Toxin Amount in Paralytic Shellfish Poison-Infested Shellfish 3. Thermal Resistance of Paralytic Shellfish Poison (마비성 패류독 허용기준치 재설정을 위한 연구 3. 마비성 패류독의 내열성)

  • 신일식;김영만
    • Journal of Food Hygiene and Safety
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    • v.13 no.2
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    • pp.143-148
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    • 1998
  • The purpose of this study was to determine the kinetics of paralytic shellfish poison (PSP) destruction at various temperature. The toxic digestive gland homogenate of blue mussel (Mytilus edulis), PSP crude toxin, gonyautoxin group and saxitoxin group were heated at temperature ranging from 90 to $120^{\circ}C$, and then the toxicities were measured in samples heated for various time intervals. The rate constant (k) of the toxic digestive gland homogenate, PSP crude toxin, gonyautoxin group and saxitoxin group were $3.28{\times}10^{-2},\;1.20{\times}10^{-2},\;5.88{\times}10^{-2}\;and\;2.58{\times}10^{-2}\;at\;120^{\circ}C$, respectively. The decimal reduction time (D-value) of the toxic digestive gland homogenate, PSP crude toxin, gonyautoxin group and saxitoxin group were 70, 192, 39 and 89 at $120^{\circ}C$, respectively. These results indicate that PSP crude toxin is most heat-stable of 4 types of PSP toxins and PSP toxin are more heat-stable than food poisoning bacteria and spores. The retorting condition to reduce PSP toxicity below quarantine limit ($80\;\mu\textrm{g}/100\;g$ in Korea and America, 4 MU/g in Japan) could be calculated by rate constant. For example, the digestive gland homogenate having a initial toxicity of $200\;\mu\textrm{g}/100\;g$ could have toxicity below quarantine limit when heated at $90^{\circ}C$ for 129 min., $100^{\circ}C$ for 82 min., $110^{\circ}C$ for 48 min. and $120^{\circ}C$ for 28 min. These results suggest that commercial retorting condition ($115^{\circ}C$ for 70 min) in Korea is enough to reduce toxicity below quarantine limit from initial toxicity of $200\;\mu\textrm{g}/100\;g$. From these results, the quarantine limit of PSP-infested shellfish for canning can be level up to raw score of $200\;\mu\textrm{g}/100\;g$.

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Paralytic Shellfish Poisoning of Mediterranean mussels from Jinhae Bay in Korea (진해만 해역에서 지중해담치 (Mytilus galloprovincialis)의 마비성패독 독화 양상)

  • Shon, Myung-Baek;Kim, Young-Soo;Kim, Chang-Roon
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.42 no.4
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    • pp.366-372
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    • 2009
  • This study looked at toxicity of Mediterranean mussels, Mytilus galloprovincialis, which had accumulated paralytic shellfish toxins (PST) from early March to late May 2005 at Jinhae Bay, Korea. Alexandrium sp. was observed in low densities (< 1,000 cells/L) at the beginning of the study in March, increased rapidly in April, declined rapidly and disappeared in May. Although low densities of Alexandrium sp. were observed in March, mussel toxicity exceeded regulation level ($80{\mu}g$ STXeq. /100 g). Peak PSP (Paralytic Shellfish Poisoning) toxicity in the mussels occurred during high Alexandrium sp. cell densities in April. Mussels toxicity decreased with decline of Alexandrium sp. cell density. Major toxin components identified were $GTX_1$, $GTX_4$, followed by $C_1$, $C_2$, $GTX_2$, $GTX_3$ and neoSTX. Trace or sporadic toxin components were STX, $GTX_5$, $dcGTX_2$, $dcGTX_3$ and dcSTX. Toxin component analysis from the middle to end of the study showed that $11{\beta}$-epimers ($GTX_{3,4}$, $C_2$) were converted into $11{\alpha}$-epimers ($GTX_{1,2}$, $C_1$) and started to determine STX.