• Title/Summary/Keyword: venoms

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Studies on the Venom Inhibtor (Part Ⅵ) Reaction of the sample in vivo

  • 서정훈
    • Proceedings of the Korean Society for Applied Microbiology Conference
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    • 1978.10a
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    • pp.209.4-209
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    • 1978
  • Previously, we reported the inhibitory substane which reacts on venoms proteinases and haemorrha-ghagic factors. The active substsnce was originated from soil fungi. This report describes the results of molecular weight determination, the activity by the derivatives, and also the reaction in vivo by the administration of sample L175-68-B.

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Histopathological and Fine Structural Changes in Mouse Skin after Injection of Honeybee Venom (꿀벌의 독에 의한 생쥐 피부의 조직병리학적 및 미세구조적 변화)

  • Shin, Sang-Hee;Jeong, Moon-Jin;Moon, Myung-Jin
    • Applied Microscopy
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    • v.27 no.2
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    • pp.145-153
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    • 1997
  • Histopathological and fine structural changes in mouse skin after injection of venoms extracted from the venom glands of the honeybee, Apis mellifera, were studied with light and electron microscopes. At this experiment the venoms were directly injected at the hairless abdominal skin of the mouse through the sting of the bee's venomous organ. Main changes appeared within one hour after injection at both epithelial and connective tissues as considerable hyperemia and angioedema, and slight edema and fibrosis. High magnified electron micrographs reveal not only increase of diameter but also deposition of electron dense grains (which seems to be an auto immunoglobulin) at the collagenous fibers characteristically. This kinds of histological and fine structural responses were diminished from 12 hour after injection, and the pathological symptoms disappeared within 3 days at most cases. So, the skin responses induced by honeybee venom seem to be not severe compare to other cases reported by other venomous arthropods.

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The venom of jellyfish, Chrysaora pacifica, induces neurotoxicity via activating Ca2+-mediated ROS signaling in HT-22 cells

  • Yang, Yoon-Sil;Kang, Young-Joon;Kim, Hye-Ji;Kim, Min-Soo;Jung, Sung-Cherl
    • Journal of Applied Biological Chemistry
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    • v.62 no.4
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    • pp.347-353
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    • 2019
  • Stings of jellyfish, which frequently occur in a warm season, cause severe pain, inflammation and sometimes irreversible results such as the death. Harmful venoms from jellyfish, therefore, have been studied for finding the therapeutic agents to relieve pain or to neutralize toxic components. However, it is still unclear if and how jellyfish venom reveal neuronal toxicity even though pain induction seems to result from the activation of nociceptors such as nerve endings. In this study, using HT-22 cell line, we investigated neurotoxic effects of the venom of Chrysaora pacifica (CpV) which appears in South-East ocean of Korea. In 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide assay, CpV significantly reduced the viability of HT-22 cells in a dose-dependent manner. Additionally, in 2',7'-Dichlorofluorescin diacetate fluorescence test under the culture condition lacking dominant inflammatory factors, CpV remarkably increased the production of intracellular reactive oxygen species (ROS). Reduced responsive fluorescence to Rhodamine123 and increased expression of intracellular cytochrome c were also observed in HT-22 cells treated with CpV. These indicate that CpV-reduced viability of HT-22 cells may be due to the activation of apoptotic signalings mediated with oxidative stress and mitochondrial dysfunction. Furthermore, removing Ca2+ ion or adding N-acetyl-Lcystein remarkably blocked the CpV effect to reduce the viability of HT-22 cells. The findings in this study clearly demonstrate that CpV may activate Ca2+-mediated ROS signalings and mitochondrial dysfunction resulting in neuronal damage or death, and suggest that blocking Ca2+ pathway is a therapeutic approach to possibly block toxic effects of jellyfish venoms.

Inhibitory Substance on the Snake Venoms Produced by Penicillium sp. (사독의 조해물질에 관한 연구)

  • Seu, Jung-Hwn;Yi, Dong-Heui
    • Microbiology and Biotechnology Letters
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    • v.7 no.2
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    • pp.75-89
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    • 1979
  • One strain of Penicillium sp. (175-66-B), isolated from soil, was able to produce a substance that has a strong inibition activity against the Agkistrodon and Trimeresurus venoms. In this experiment, the chemical and biological properties of the sample were investigated. As an inhibitory substance, it was effective to the proteinase, hemorrhagic and lethal factors of Agkistrodon and Trimeresurus venoms, and also effective to several fractions of the proteinases and hemorrhagic factors of Agkistrodon halys blomhoffi venom. Moreover, in the addition of prednisotone, it was more effective for the cure of the mouse envenomated with the venom amount of two fold of MLD$_{100}$. This substance was very stable to the acid, alkali and heat. Its melting point was high enough to sublime at 222$^{\circ}C$ without any decomposition. This sample was easily dissolved only in hot water, but not in several organic solvents except for a little dissolution in elate. It did not have the chelating activity. It had very strong specificity to the snake venoms. but its activity was depressed by the addition of zinc or cupric salts. This sample had no acute toxicity to the mouse. Its chemical formula was $C_{16}$ $H_{12}$$N_2$ $O_{10}$ with the molecular weight of about 392. It has two epoxy groups and four carboxyl radicals, but amino, nitrite and nitrate radicals, unsaturated bonds and aromatic ring were not detected. Theuchemical configuration of this sample was suggested to be;

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Development of Fibrinolytic Agents from Snake Venoms

  • 김영식;한범수;장일무
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1994.04a
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    • pp.279-279
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    • 1994
  • Fibrinolytic proteases, piscivorase I (PI) and piscivorase II (PII), were isolated from Agkistrodon piscivorus piscivorus (eastern cotonmouth moccasin) venom using gel filtration on Bio-Gel P100 and ion-exchange chromatography on CM-Sepharose. The molecular welghts of two proteases were approximately 23400 and 29000. Their isoelectric points 6.6 and 8.5, respectively. The partial amino acid sequences of PI were characterized by tryptic digestion. PI readily cleaves the A${\alpha}$-and B${\beta}$-chaln of fibronogen, but PII rapidly cleaves A${\alpha}$-chain and more slowly the B${\beta}$-chain, They were activated by Ca$\^$2+/, Mg$\^$2+/ and Ba$\^$2+/, but inhibited by Zn$\^$2+/, Cu$\^$2+/ and Mn$\^$2+/. Two enzymes were also inhibited by cysten, ${\beta}$-mercapto -ethanol, and by metal chelators such as EDTA and EGTA, but not by benzamidine, PMSF, soybean trypsin inhibitor and aprotinin. They did not act like thrombin, plasmin and kallikrein, using specific chromogenllc substrates. Two protease did not induce platelet aggregation. PI showed low hemorrhagic activity at dosage of 50 $\mu\textrm{g}$.

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Epidemiology of anaphylaxis in Korean children (소아청소년에서 아나필락시스의 역학)

  • Lim, Dae Hyun
    • Clinical and Experimental Pediatrics
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    • v.51 no.4
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    • pp.351-354
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    • 2008
  • Anaphylaxis is an acute systemic reaction caused by IgE-mediated immunological release of mediators from mast cells and basophils to allergenic triggers, such as food, insect venoms, and medications. An alternative definition was recently proposed as follows: anaphylaxis is a "condition caused by an IgE mediated reaction" that is "often life threatening and almost always unanticipated." The reaction can be severe enough to lead to the rapid onset of symptoms, including dizziness, upper airway occlusion, bronchial constriction, hypotension, urticaria, cardiovascular arrhythmias and possible cardiac arrest. The incidence or prevalence of anaphylaxis in Korean pediatrics has not known. Thus, Epidemiology of Anaphylaxis in Pediatrics based on the data from Korean Health Insurance Review and Assessment Service (KHIRA) from 2001 to 2007 and questionnaire to the member of Korean Academy of Pediatric Allergy and Respiratory Disease (KAPARD) who are working at the training hospitals was studied. The incidence of anaphylaxis under age 19 is 0.7-1.0 per 100,000 year-person. The causes of anaphylaxis based on data from KHIRA were unknown (61.7%), food (24.9%), medications (12.4%), and serum (1.0%).

Purification and characterization of the low molecular weight collagenase from pyloric caeca of tuna, Katsuwonus pelamis

  • Lee, Sang-Hoon;Park, Pyo-Jam;Kim, Se-Kwon
    • Proceedings of the Korean Society of Fisheries Technology Conference
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    • 2001.10a
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    • pp.239-240
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    • 2001
  • Collagenases are generally defined as enzymes capable of degrading the polypeptide backbone of native collagen under conditions which do not denature the protein. Two types of proteases with collagenolytic activity have been reported and thought to play different physiological functions. Metallo-collagenases, firstly discovered in tadpole tissue explants are zinc-containing enzymes requiring calcium for optimum activity and stability, and These enzymes have been widely studied from various mammalian tissues as well as from bacteria, such as Bacillus cereus, Clostridium histolyticum, Achromobacter, Vibrio alginolyticus and Clostridium perfringens and snake venoms. (omitted)

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Inhibitory Activity of Bumblebee Worker (Bombus terrestris L.) Venoms on Nitric Oxide, TNF-${\alpha}$ and IL-6 Production in Lipopolysaccharide-Activated Macrophages

  • Han Sang-Mi;Lee Kwang-Gill;Yeo Joo-Hong;Kweon Hae-Yong;Woo Soon-Ok;Yoon Hyung-Joo;Baek Ha-Ju;Park Kwan-Kyu
    • International Journal of Industrial Entomology and Biomaterials
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    • v.12 no.2
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    • pp.69-73
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    • 2006
  • To elucidate the composition of bumblebee (Bomb us terrestris) venom (BBV) and the anti-inflammatory effect of BBV. The major components of BBV by LC chromatography and SDS-PAGE were identified. The production of nitric oxide (NO) and proinflammatory cytokines was examined by lipopolysaccharide (LPS) in a macrophage cell line, RAW 264.7 cells, with BBV. BBV inhibits LPS-induced NO in a dose dependent manner. We also found that BBV inhibits proinflammatory cytokine, tumor necrosis factor (TNF)-${\alpha}$ and interleukin (IL)-6 production. These findings mean that BBV can be used in controlling macrophages mediated inflammation related disease. Additional studies on the pharmacological aspects of the individual components of BBV are recommended for future trials.