Skip to main content
Have a personal or library account? Click to login
Snake Venom Metalloproteinases Cover

Snake Venom Metalloproteinases

Acta Marisiensis - Seria Medica
Volume 62 (2016): Issue 1 (March 2016)
By: ,  ,   and    
Open Access
|Feb 2016
References

References

  1. 1. http://www.outsideonline.com/1912971/venom-not-just-poison
    Search in Google Scholar
  2. 2. http://www.wondersandmarvels.com/2011/11/the-uses-of-snakevenom-in-antiquity.html
    Search in Google Scholar
  3. 3. Kang TS, Georgieva D, Kini RM et al. Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis. FEBS J. 2011;278(23):4544-4476.
    Open DOISearch in Google Scholar
  4. 4. Mitchell SW, Reichert ET. Researches upon the venoms of poisonous serpents.Smithsonian Contribution to Knowledge Smithsonian Institute, Washington D.C. 1886;pp.89-95.
    Search in Google Scholar
  5. 5. Markland Jr. FS, Swenson S. Snake venom metalloproteinases. Toxicon. 2013;62:3-18.
    Open DOISearch in Google Scholar
  6. 6. Ohsaka A. Fractionation of Habu snake venom by chromatography on cm-cellulose with special reference to biological activities. Jpn J Med Sci Biol. 1960;13:199-205.
    Open DOISearch in Google Scholar
  7. 7. Ohsaka A, Ikezawa H, Kondo H, Kondo S. Two hemorrhagic principles derived from Habu snake venom and their difference in zone electrophoretical mobility. Jpn J Med Sci Biol. 1960;13:73-76.
    Open DOISearch in Google Scholar
  8. 8. Okonogi T, Hoshi S, Honma M, et al. Studies on the habu snake venom. 3-2. A comparative study of histopathological changes caused by crude venom, purified habu-proteinase and other proteinases. Jpn J Microbiol. 1960;4:189-192.
    Open DOISearch in Google Scholar
  9. 9. Maeno H, Mitsuhashi S, Sato R. Studies on Habu snake venom. 2c. Studies on Hβ-proteinase of Habu venom.Jpn J Microbiol. 1960;4:173-180.
    Open DOISearch in Google Scholar
  10. 10. Bjarnason JB, Tu AT. Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e. Biochemistry. 1978;17(16):3395-3404.
    Open DOISearch in Google Scholar
  11. 11. Takahashi T, Ohsaka A. Purification and some properties of two hemorrhagic principles (HR2a and HR2b) in the venom of Trimeresurus flavoviridis; complete separation of the principles from proteolytic activity. Biochim Biophys Acta. 1970;207(1):65-75.
    Open DOISearch in Google Scholar
  12. 12. Takeda S, Takeya H, Iwanaga S. Snake venom metalloproteinase: structure, function and relevance to the mammalian ADAM/ADAMTS family proteins. Biochim Biophys Acta. 2012;1824(1):164-176.
    Open DOISearch in Google Scholar
  13. 13. Fox JW, Serrano SMT. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J. 2008;275:3016-3030.
    Open DOISearch in Google Scholar
  14. 14. Shannon JD, Baramovat EN, Bjarnason JB, Fox JW. Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin. J Biol Chem. 1989;264(20):11575-11583.
    Open DOISearch in Google Scholar
  15. 15. Bjarnason JB, Fox JW. Snake venom metalloendopeptidases: Reprolysins. Methods Enzymol. 1995;248:345-368.
    Open DOISearch in Google Scholar
  16. 16. Bjarnason JB, Fox JW. Hemorrhagic metalloproteinases from snake venoms. Pharmacol Ther. 1994;62(3):325-372.
    Open DOISearch in Google Scholar
  17. 17. Hite LA, Shannon JD, Bjarnason JB, Fox JW. Sequence of cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: Evidence for signal, zymogen, and disintegrin-like structures. Biochemistry. 1992;31:6203-6211.
    Open DOISearch in Google Scholar
  18. 18. Shimokawa K, Jia LG, Wang XM, Fox JW. Expression, activation, and processing of the recombinant snake venom metalloproteinase, proatrolysin E. Arch BiochemBiophys. 1996;335(2):283-294.
    Open DOISearch in Google Scholar
  19. 19. Fox JW, Serano SMT. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases.Toxicon. 2005; 45: 969-985;
    Open DOISearch in Google Scholar
  20. 20. White JM. ADAMs: modulators of cell-cell and cell-matrix interactions. CurrOpin Cell Biol. 2003;15(5):598-606.
    Search in Google Scholar
  21. 21. Mackessy S. Handbook of Venom and Toxins of Reptiles. CRC Press, Taylor & Francis Group, Boca Raton, Florida, USA; 2010;P.12-16,P. 95-132.
    Search in Google Scholar
  22. 22. Pinto A FM, Terra MS, Guimares JA, Fox JW. Mapping von Willebrand factor A domain binding sites on a snake venom metalloproteinase cysteine-rich domain. Arch Biochem Biophys. 2007;457(1):41-46.
    Open DOISearch in Google Scholar
  23. 23. Moura-da-Silva AM, Della-Casa MS, David AS, Assakura MT, Butera D, Lebrun I, Shannon JD, Serrano SM, Fox JW. Evidence for heterogeneous forms of the snake venom metalloproteinase jararhagin: A factor contributing to snake venom variability. Arch BiochemBiophys. 2003;409(2):395-401.
    Open DOISearch in Google Scholar
  24. 24. Calvete JJ, Juarez P, Sanz L. Snake venomics. Strategy and applications.J Mass Spectrom. 2007;42:1405-1414.
    Open DOISearch in Google Scholar
  25. 25. Ompraba C, Chapeaurouge A, Kini RM et al. Identification of a novel family of snake venom proteins veficolins from Cerberus rynchops using a venom gland transcriptomics and proteomics approach. J Proteome Res. 2010;9(4):1882-1893.
    Open DOISearch in Google Scholar
  26. 26. Weldon CL, Mackessy SP. Biological and proteomic analysis of venom from the Puerto Rican Racer (Alsophis Portoricensis: Dipsadidae). Toxicon. 2010;55:558-569.
    Open DOISearch in Google Scholar
  27. 27. Georgieva D, Seifert J, Betzel C et al. Pseudechis australis venomics: adaptation for a defense against microbial pathogens and recruitment of body transferrin. 2011;10(5):2440-2464.
    Search in Google Scholar
  28. 28. Petras D, Sanz L, Calvette JJ et al. Snake venomics of African spitting cobras: toxin composition and assessment of congeneric cross-reactivity of the pan-African EchiTAb-Plus-ICP antivenom by antivenomics and neutralization approaches. J. ProteomeRes. 2011;10:1266-1280.
    Search in Google Scholar
  29. 29. Shimokawa K, Shannon JD, Jia LG, Fox JW. Sequence and biological activity of Catrocollastatin-C: a disintegrin-like/cysteine-rich twodomain protein from Crotalus atrox venom. Arch BiochemBiophys. 1997;343(1):35-43.
    Open DOISearch in Google Scholar
  30. 30. Kress LF, Paroski EA. Enzymatic inactivation of human serum proteinase inhibitors by snake venom proteinase. BiochemBiophys Res Commun. 1978;83:649-656.
    Open DOISearch in Google Scholar
  31. 31. Zhang D, Fox JW, Meyer EF et al. Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase atrolysin C (form d). ProcNatlAcadSci USA 1994;91(18):8447-8451.
    Open DOISearch in Google Scholar
  32. 32. Gutierrez JM, Romero M, Diaz C, Borkow G, Ovadia M. Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo). Toxicon. 1995;33:19-29.
    Open DOISearch in Google Scholar
  33. 33. Rucavado A, Lomonte B, Ovadia M, Gutierrez JM. Local tissue damage induced by BaP1, a metalloproteinase isolated from Bothrops asper (terciopelo) snake venom. ExpMolPathol. 1995;63:186-199.
    Open DOISearch in Google Scholar
  34. 34. Takeya H, Arakawa M, Miyata T, Iwanaga S, Omori-Satoh T. Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, Trimeresurus flavoviridis. J Biochem. 1989;106:151-157.
    Open DOISearch in Google Scholar
  35. 35. Wu WB, Chang SC, Liau MY, Huang TF. Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells. Biochem J. 2001;357:719-728.
    Open DOISearch in Google Scholar
  36. 36. Bernardes CP, Soares AM, de Oliveira F et al. Isolation and structural characterization of a new fibrin(ogen)olytic metalloproteinase from Bothrops moojeni snake venom. Toxicon. 2008;51:574-584.
    Open DOISearch in Google Scholar
  37. 37. Cintra AC, De Toni LG, Sampaio SV et al. Batroxase, a new metalloproteinase from B. atrox snake venom with strong fibrinolytic activity. Toxicon. 2012;60(1):70-82.
    Open DOISearch in Google Scholar
  38. 38. de Toni LGB, Menaldo DL, Sampaio SV. Inflammatory mediators involved in the paw edema and hyperalgesia induced by Batroxase, a metalloproteinase isolated from Bothrops atrox snake venom. Int Immunopharmacol. 2015;28(1):199-207.
    Open DOISearch in Google Scholar
  39. 39. Achê DC, Gomes MS, Rodrigues VdeM et al. Biochemical properties of a new PI SVMP from Bothrops pauloensis: inhibition of cell adhesion and angiogenesis. Int J Biol Macromol. 2015;72:445-453.
    Open DOISearch in Google Scholar
  40. 40. Chen RQ, Jin Y, Xiong YL et al. A new protein structure of P-II class snake venom metalloproteinase: it comprise metalloproteinase and disintegrin domains. Biochem Biophys Res Commun. 2003;310:182-187.
    Open DOISearch in Google Scholar
  41. 41. Nikai T, Fox JW, Sugihara H et al. Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom. Arch Biochem Biophys. 2000;378:6-15.
    Open DOISearch in Google Scholar
  42. 42. Jeon OH, Kim DS. Molecular cloning and functional characterization of a snake venom metalloproteinase.Eur J Biochem. 1999;263:526-533.
    Open DOISearch in Google Scholar
  43. 43. Camacho E, Gutierrez JM, Rucavado A et al. Understanding structural and functional aspects of PII snake venom metalloproteinase: Characterization of BlatH1, a hemorrhagic dimeric enzyme from the venom of Bothriechis lateralis. Biochimie. 2014;101:145-155.
    Open DOISearch in Google Scholar
  44. 44. Oyama E, Takahashi H. Purification and characterization of two high molecular mass snake venom metalloproteinase (P-III SVMPs), named SV-PAD-2 and HR-Ele-1, from the venom of Protobothrops elegansi (Sakishima-habu). Toxicon. 2015;103:30-38.
    Open DOISearch in Google Scholar
  45. 45. Leonardi A, Sajevic T, Križaj I et al. Structural and biochemical characterization of VaF1, a P-IIIafibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom. Biochimie. 2015;109:78-87.
    Open DOISearch in Google Scholar
  46. 46. Shioi N, Nishijima A, Terada S. Flavorase, a novel non-hemorrhagic metalloproteinase in Protobothrops flavoviridis venom, is a target molecule of small serum protein-3. J Biochem. 2015;158(1):37-48.
    Open DOISearch in Google Scholar
  47. 47. Paine MJ, Desmond HP, Theakston RD, Crampton JM. Purification, cloning and molecular characterization of high molecular weight hemorrhagic metalloproteinase, jarahagin from Bothrops jararaca venom. Insights into the disintegrin gene family. J Biol Chem. 1992;267:22869-22876.
    Open DOISearch in Google Scholar
  48. 48. Sartim MA, Costa TR, Sampaio SV et al. Moojenactivase, a novel procoagulant PIIIdmetalloprotease isolated from Bothrops moojeni snake venom, activates coagulation factors II and X and induces tissue factor up-regulation in leukocytes. Arch Toxicol. 2015;DOI10.1007/s00204-015-1533-6. (terciopelo) snake venom. ExpMolPathol. 1995;63:186-199.
    Search in Google Scholar
DOI: https://doi.org/10.1515/amma-2015-0114 | Journal eISSN: 2668-7763 (formerly 2247-6113) | Journal ISSN: 2668-7755
Journal RSS Feed
Language: English
Page range: 106 - 111
Submitted on: Aug 18, 2015
Accepted on: Sep 21, 2015
Published on: Feb 9, 2016
Published by: University of Medicine, Pharmacy, Science and Technology of Targu Mures
In partnership with: Paradigm Publishing Services
Publication frequency: 4 issues per year
Keywords:
snake venom metalloproteinases,
hemorrhagic activity,
hemostatic distruption,
ADAM and ADAMTS,
SVMPs
Related subjects:
Medicine,
Clinical medicine,
Clinical medicine, other

© 2016 Şerban Andrei Gâz Florea, Adriana Gâz Florea, Hajnal Kelemen, Daniela-Lucia Muntean, published by University of Medicine, Pharmacy, Science and Technology of Targu Mures
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Volume 62 (2016): Issue 1 (March 2016)
Previous article
Next article