Pharmacology of Phospholipase A2 from Snake Venoms

Rosenberg, Philïp

doi:10.1007/978-3-642-66913-2_12

Cited by 45 publications

(12 citation statements)

References 252 publications

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“…Variation in species sensitivity to hemolysis as seen herein (sheep < cow/rat < horse) has also been observed with other Bothrops venoms, e.g., B. asper venom causes direct hemolysis of mouse erythrocytes but has no effect on goat, horse, rabbit, sheep and toad erythrocytes; in contrast, lysis of human erythrocytes requires bovine serum albumin and Ca 2+ (17). These variations may reflect differences in the phospholipid composition of the erythrocyte plasma membrane of these species (18)(19)(20), as well as the accessibility of the cellular membrane targets such as negative phospholipids to PLA 2 action (17,18). Incubation of the venom at different temperatures indicated that the venom component responsible for hemolysis is thermolabile.…”

Section: Discussionsupporting

confidence: 72%

In vitro hemolytic activity of Bothrops lanceolatus (fer-de-lance) venom

Martins¹,

Araújo²,

Bon³

et al. 2009

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

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Bothrops lanceolatus venom contains a variety of enzymatic and biological activities. The present work investigated the hemolytic activity of this venom and its phospholipase A 2 (PLA 2 ). Bothrops lanceolatus venom (6.7 µg/mL) caused indirect hemolysis of cow, horse, rat and sheep erythrocytes, with horse erythrocytes being the most sensitive; no direct hemolysis was observed. Hemolysis in sheep erythrocytes was concentration-dependent (5-11.7 µg/mL) and markedly attenuated by heating the venom for 30 minutes at ≥ 40°C and by the PLA 2 inhibitor p-bromophenacyl bromide. An acidic PLA 2 (5 µg/mL) purified from B. lanceolatus venom also caused hemolysis. This PLA 2 showed immunoprecipitin lines with antivenom against B. lanceolatus, which suggests that the enzymatic and hemolytic activities of this enzyme may be neutralized during antivenom therapy. These results indicate that B. lanceolatus venom and its PLA 2 can cause hemolysis in vitro.

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Section: Discussionsupporting

confidence: 72%

In vitro hemolytic activity of Bothrops lanceolatus (fer-de-lance) venom

Martins¹,

Araújo²,

Bon³

et al. 2009

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

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“…It has been shown to act as a noncompetitive inhibitor of the nicotinic acetylcholine receptor (nAChR), though this mechanism is still controversial (60). Phospholipase A 2 leads to an increase in capillary permeability and to myonecrosis by the disruption of lipid membranes (in vitro and in vivo) that end in hemolysis, as an indirect effect (38,54). It is also involved in membrane signal transduction, cellular function, and inflammatory responses (7).…”

Section: Effects Of Nhav On Rat Paw Edemamentioning

confidence: 99%

Pharmacological characterization of rat paw edema induced by Naja haje arabica venom

Alasmari¹

2005

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

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ABSTRACT:This investigation was performed in order to assess the inflammatory response induced by Naja haje arabica venom (NhaV) in rat hind paw. The Commercially available antivenom was ineffective when administered intravenously, whereas its local administration with NhaV attenuated the edema formation (P<0.001). In conclusion, NhaV-induced edema in rat paw involves PLA 2 and adenosine mechanisms. Additionally, the use of polyspecific antivenom, intravenously, was ineffective in preventing NhaV-induced edema.KEY WORDS: rat paw edema, Naja haje arabica venom, inflammatory mediators, inhibitor, antivenom.

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“…Snake venoms are complex mixtures of proteins and polypeptides that induce various biological activities [1]. Phospholipases (PLA 2 ) are amongst the most toxic venom constituents.…”

Section: Introductionmentioning

confidence: 99%

Purification and activity of two phospholipase enzymes from Naja nigricolis nigricolis reinhardt venom

Abubakar

Nok

Abdurahman

et al. 2003

J Biochem & Molecular Tox

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Two phospholipase enzymes NN1 and NN2 were purified from the venom of Naja nigricolis nigricolis Reinhardt to apparent homogeneity. NN1 was purified by a two-step anion-exchange chromatography on DEAE-cellulose column while NN2 was purified by a combination of anion-exchange chromatography and gel filtration on Sephadex G-150. The enzyme NN1 moved homogenously on acrylamide gel as a monomer with a molecular weight of 65 kDa while NN2 was a dimer of 71 kDa. Both enzymes were clearly separated. Both enzymes hydrolyzed L-alpha-phosphatidyl choline with activities of 345.5 for NN1 and 727.8 micromol min(-1) x mg(-1) for NN2. The dimeric 71-kDa enzyme has a higher haemolytic and anticoagulant activity than the monomeric 65-kDa enzyme. It is apparent that the dimeric enzyme has a more pronounced activity than the monomer has, thus toxic activity may be related to the hydrolysis of phospholipids.

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Pharmacology of Phospholipase A2 from Snake Venoms

Cited by 45 publications

References 252 publications

In vitro hemolytic activity of Bothrops lanceolatus (fer-de-lance) venom

In vitro hemolytic activity of Bothrops lanceolatus (fer-de-lance) venom

Pharmacological characterization of rat paw edema induced by Naja haje arabica venom

Purification and activity of two phospholipase enzymes from Naja nigricolis nigricolis reinhardt venom

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