Characterization of Hyaluronidase Isolated from Agkistrodon contortrix contortrix (Southern Copperhead) Venom

Kudo, Kenzo; Tu, Anthony T.

doi:10.1006/abbi.2000.2204

Cited by 40 publications

(21 citation statements)

References 29 publications

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“…This variation in venom hyaluronidase activity was also evident in vipers of other continents with high expression from the Asian Russell's viper (D. russellii) and American Western diamondback rattle snake (C. atrox) but little in other American (B. asper, B. jararaca) and Asian (C. rhodostoma) pit vipers. The variant size (50-70 kDa) of hyaluronidases in the viper venoms analysed here is generally consistent with earlier reports for viperid and elapid snake venoms (Cevallos et al, 1992;Kudo and Tu, 2001;Girish et al, 2002). The observation, in the latter study, of hyaluronidase activity in C. rhodostoma venom differs from our results, illustrating the differences in expression of venom proteins extracted from animals of distinct geographical origin (Francischetti et al, 2000) and age (Theakston and Reid, 1978), and perhaps the instability of hyaluronidase in stored venom samples.…”

Section: Hyaluronidase Activity In Snake Venomssupporting

confidence: 89%

Identification of cDNAs encoding viper venom hyaluronidases: Cross-generic sequence conservation of full-length and unusually short variant transcripts

Harrison

Ibison

Wilbraham

et al. 2007

Gene

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Section: Hyaluronidase Activity In Snake Venomssupporting

confidence: 89%

Identification of cDNAs encoding viper venom hyaluronidases: Cross-generic sequence conservation of full-length and unusually short variant transcripts

Harrison

Ibison

Wilbraham

et al. 2007

Gene

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“…[7][8][9] Exhaustive incubation with HA, resulted in the formation of tetrasaccharides as the end-products by both the isoforms; however, initially the oligosaccharides produced were of varied length. In vitro, enzymes from the venoms of Agkistrodon contortrix contortrix 58 and Apis mellifera 80 also yielded tetra-and hexasaccharides. However, no data exist regarding in vivo cleavage products.…”

Section: Venom Hyaluronidase and The Pathology Of Envenomationmentioning

confidence: 94%

Snake venom hyaluronidase: a therapeutic target

Kemparaju

Girish

2005

Cell Biochem. Funct.

152

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The diffusion of toxins from the site of a bite into the circulation is essential for successful envenomation. Degradation of hyaluronic acid in the extracellular matrix (ECM) by venom hyaluronidase is a key factor in this diffusion. Hyaluronidase not only increases the potency of other toxins but also damages the local tissue. In spite of its important role, little attention has been paid to this enzyme. Hyaluronidase exists in various isoforms and generates a wide range of hyaluronic acid degradation products. This suggests that beyond its role as a spreading factor venom hyaluronidase deserves to be explored as a possible therapeutic target for inhibiting the systemic distribution of venom and also for minimizing local tissue destruction at the site of the bite.

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“…Hyaluronidase activity has been detected in the venom of snakes (Kudo and Tu, 2001;Girish et al, 2004b;Kemparaju and Girish, 2006), bees (Gmachl and Kreil, 1993;MarkovicHousley et al, 2000), stonefish (Poh et al, 1992;Ng et al, 2005), scorpions (Ramanaiah et al, 1990;Pessini et al, 2001;Morey et al, 2006), spiders (Rash and Hodgson, 2002;Nagaraju et al, 2006), lizards (Tu and Hendon, 1983), wasps (Kreil, 1995), caterpillars (da C B Gouveia et al, 2005) and hornets (Lu et al, 1995). In all animal venoms, the hyaluronidase causes local tissue damage and is generally referred to as a spreading factor.…”

Section: Venom Hyaluronidasesmentioning

confidence: 96%