Hemorrhagic, Necrotizing and Edema-Forming Effects of Snake Venoms

Ohsaka, Akira

doi:10.1007/978-3-642-66913-2_14

Cited by 84 publications

(44 citation statements)

References 127 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This suggests that O. hannah venom presents higher enzymatic activity. This is confirmed by reports from Ohsaka (27), who described that none of the Elapidae venoms (B. fasciatus and Naja spp.) exhibit hemorrhagic activity, apart from O. hannah venom that displays an hemorrhagic activity similar to that of Viperidae venoms.…”

Section: Discussionsupporting

confidence: 82%

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

Vejayan¹,

Yee²,

Ponnudurai³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

View full text Add to dashboard Cite

Snake venoms comprise a highly complex mixture of proteins, which requires for their characterization the use of versatile two-dimensional electrophoresis techniques. In the present study, venoms obtained from eight snakes (Ophiophagus hannah, Naja kaouthia, Naja sumatrana, Bungarus fasciatus, Trimeresurus sumatranus, Tropidolaemus wagleri, Enhydrina schistosa and Calloselasma rhodostoma) commonly found in Malaysia were separated based on two independent properties, isoelectric point (pI) and molecular weight (MW). Many differences in snake venoms at the inter-family, inter-subfamily, inter-genus and inter-species levels were revealed. Notably, proteins from individuals of the Viperidae family -Trimeresurus sumatranus, Tropidolaemus wagleri and Calloselasma rhodostoma -were found to be numerous and scattered by the two-dimensional gel electrophoresis (2DE) specifically in regions between 37 and 100 kDa compared to the Elapidae venom proteins. The latter were clustered at the basic and lower molecular mass region (less than 20 kDa). Trains of spots were commonly observed, indicating that these proteins may be derived from post-translational modifications. Ophiophagus hannah (Elapidae) revealed a great amount of protein spots in the higher molecular mass range when compared to Enhydrina schistosa, Naja kaouthia, Naja sumatrana and Bungarus fasciatus. Overall 2DE showed large differences in the venom profile of each species, which might be employed as an ancillary tool to the identification of venomous snake species.

show abstract

Section: Discussionsupporting

confidence: 82%

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

Vejayan¹,

Yee²,

Ponnudurai³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

View full text Add to dashboard Cite

show abstract

“…As proeminentes atividades edematogênica e hiperalgésica, características nestes acidentes, e seus rápidos desenvolvimentos são típicos sinais do processo inflamatório agudo, decorrente da ação de substâncias endógenas que são liberadas após o estímulo lesivo (OHSAKA 1979, CHACUR et al 2001, PRADO-FRANCESCHI & HYSLOP 2002 Figuras 7-9. (7) Atividade nociceptiva dos venenos de P. olfersii e P. patagoniensis na dose de 1 µg; (8) comparação das Doses Mínimas Necrosantes dos venenos de P. olfersii e P. patagoniensis; (9) comparação dos níveis plasmáticos de Cretino-quinase (CK) após a inoculação i.m.…”

Section: Discussionunclassified

Análise das atividades biológicas dos venenos de Philodryas olfersii (Lichtenstein) e P. patagoniensis (Girard) (Serpentes, Colubridae)

Rocha

Furtado

2007

Rev. Bras. Zool.

View full text Add to dashboard Cite

Philodryas olfersii (Lichtenstein, 1823) e P.patagonienis (Girard, 1857) são serpentes colubrídeas da série opistóglifa, restritas à América do Sul. Vários acidentes ocasionados por estas serpentes têm sido relatados, caracterizando-se por ação local importante: dor, edema e hemorragia. É um acidente muito semelhante àquele causado por serpentes do gênero Bothrops Wagler, 1824 e muitas vezes os pacientes são tratados com soro antibotrópico. Poucos estudos tratam da caracterização destes venenos, assim tivemos como objetivo de trabalho o estudo dos venenos de P.olfersii e P.patagonienis. Os venenos apresentaram teor de proteínas entre 75 e 90%. A atividade desfibrinante não foi detectada quando testada em camundongos. O quadro de dor causado pelo envenenamento experimental, em camundongos, mostrou que os venenos de P.olfersii e P.patagoniensis causaram intensa reatividade, sendo que o veneno de P.patagoniensis foi o mais ativo. Ambos os venenos apresentaram dose mínima edematogênica em torno de 1 µg/camundongo com ação máxima em 30 minutos.A ação hemorrágica se instalou rapidamente, com doses mínimas semelhantes. As atividades tóxicas foram semelhantes, com valores em torno de 60,0 µg/camundongo, comparáveis aos venenos botrópicos.

show abstract

“…Hemorrhage is a common mani- festation in the victim following the bite of crotalid and viperid snakes (Ohsaka, 1979). Various components, such as hemorrhagic factors and metalloproteinases (Tu, 1991), in the snake venoms would cause localized hemorrhage by direct actions on the blood vessel walls.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

et al. 2006

View full text Add to dashboard Cite

-During the characterization of hemorrhagic factor in venom of Rhabdophis tigrinus tigrinus, so-called Yamakagashi in Japan, one of the Colubridae family, a novel metalloproteinase with molecular weight of 38 kDa in the Duvernoy's gland of Yamakagashi was identified by gelatin zymography and by monitoring its proteolytic activity using a fluorescence peptide substrate, MOCAc-PLGLA 2 pr(Dnp)AR-NH 2 , which was developed for measuring the well-known matrix metalloproteinase (MMP) activity.After purification by gel filtration HPLC and/or column switch HPLC system consisting of an affinity column, which was immobilized with a synthetic BS-10 peptide (MQKPRCGVPD) originating from propeptide domain of MMP-7 and a reversed-phase column, the N-terminal amino acid sequence of the 38 kDa metalloproteinase was identified as FNTFPGDLK which shared a high homology to Xenopus MMP-9.The 38 kDa metalloproteinase required Zn 2+ and Ca 2+ ions for its proteolytic activity. In addition, the proteolytic activity was almost completely inhibited by BS-10, a MMP inhibitor, but not by the serine proteinase inhibitors, cysteine proteinase inhibitors and aspartic proteinase inhibitors.Together these results demonstrated that the 38 kDa proteinase is a novel snake verom metalloproteinase (SVMP) containing HExGHxxGxxH motif which possesses high affinity to the BS-10 peptide, into its molecule, and the enzymatic properties are closed to that of MMPs.Based on the results obtained in the present study, we concluded that the 38 kDa metalloproteinase is a novel metalloproteinase whose activity may be regulated by the cysteine switch mechanism, and could be classified as one of the matrix metalloproteinases rather than snake venom metalloproteinases.

show abstract

Hemorrhagic, Necrotizing and Edema-Forming Effects of Snake Venoms

Cited by 84 publications

References 127 publications

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

Análise das atividades biológicas dos venenos de Philodryas olfersii (Lichtenstein) e P. patagoniensis (Girard) (Serpentes, Colubridae)

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

Contact Info

Product

Resources

About