Isolation, characterization and crystallization of a phospholipase A2 myotoxin from the venom of the prairie rattlesnake (Crotalus viridis viridis)

Toxicon ◽  
1997 ◽  
Vol 35 (1) ◽  
pp. 111-124 ◽  
Author(s):  
Charlotte L Ownby ◽  
Terry R Colberg ◽  
Steven P White
Keyword(s):  
Phospholipase A2 ◽  
Crotalus Viridis

scholarly journals A Novel Phospholipase A2(D49) from the Venom of theCrotalus oreganus abyssus(North American Grand Canyon Rattlesnake)

2014 ◽  
Vol 2014 ◽  
pp. 1-15 ◽  
Author(s):  
W. Martins ◽  
P. A. Baldasso ◽  
K. M. Honório ◽  
V. G. Maltarollo ◽  
R. I. M. A. Ribeiro ◽  
...  
Keyword(s):  
Amino Acids ◽  
Phospholipase A2 ◽  
North American ◽  
Grand Canyon ◽  
Phospholipase A ◽  
Primary Sequence ◽  
Crotalus Viridis ◽  
Current Classification ◽  
Crotalus Oreganus ◽  
Independent Species

Currently,Crotalus viridiswas divided into two species:Crotalus viridisandCrotalus oreganus. The current classification divides “the old”Crotalus viridisinto two new and independent species:Crotalus viridis(subspecies:viridis and nuntius) andCrotalus oreganus(subspecies:abyssus, lutosus, concolor, oreganus, helleri, cerberus, and caliginis). The analysis of a product from cDNA (E6d), derived from the gland of a specieCrotalus viridis viridis, was found to produce an acid phospholipase A2. In this study we isolated and characterized a PLA2(D49) fromCrotalus oreganus abyssusvenom. Our studies show that the PLA2produced from the cDNA ofCrotalus viridis viridis(named E6d) is exactly the same PLA2primary sequence of amino acids isolated from the venom ofCrotalus oreganus abyssus. Thus, the PLA2from E6d cDNA is actually the same PLA2presented in the venom ofCrotalus oreganus abyssusand does not correspond to the venom fromCrotalus viridis viridis. These facts highlight the importance of performing more studies on subspecies ofCrotalus oreganusandCrotalus viridis, since the old classification may have led to mixed results or mistaken data.

44. Leishmanicidal Effects of a Phospholipase A2 Isolated from Crotalus viridis viridis Snake Venom

Toxicon ◽  
2012 ◽  
Vol 60 (2) ◽  
pp. 117
Author(s):  
Camila M. Adade ◽  
S. Fernandes Anne Cristine ◽  
O. Carvalho Ana Lúcia ◽  
Russolina B. Zingali ◽  
Thais Souto-Padrón
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Crotalus Viridis

Deficiency of Group VIA phospholipase A2 Primes the Cytokine Releases by Kupffer cells and Lymphocytes

2015 ◽  
Vol 53 (12) ◽  
Author(s):  
J Inhoffen ◽  
S Tuma-Kellner ◽  
W Stremmel ◽  
W Chamulitrat
Keyword(s):  
Phospholipase A2 ◽  
Kupffer Cells

Mechanism of Inhibitory Action on Platelet Activation of a Phospholipase A2 Isolated from Lachesis muta (Bushmaster) Snake Venom

1997 ◽  
Vol 78 (05) ◽  
pp. 1372-1380 ◽  
Author(s):  
André L Fuly ◽  
Olga L T Machado ◽  
Elias W Alves ◽  
Célia R Carlinis
Keyword(s):  
Platelet Aggregation ◽  
Enzymatic Activity ◽  
Phospholipase A2 ◽  
Inhibitory Activity ◽  
Thermal Inactivation ◽  
Anticoagulant Activity ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Crude Venom ◽  
Lachesis Muta

SummaryCrude venom from Lachesis muta exhibited procoagulant, proteolytic and phospholipase A2 activities. A phospholipase A2, denoted LM-PLA2 was purified from L. muta venom to homogeneity, through a combination of chromatographic steps involving gel-filtration on Sephacryl S-200 HR and reverse phase chromatography on a C2/C18 column. LM-PLA2 presented a single polypeptide chain with an isoelectric point at pH 4.7 and apparent molecular weight of 17 kDa. Partial aminoacid sequence indicated a high degree of homology for LM-PLA2 with other PLA2 from different sources.LM-PLA2 displayed a potent enzymatic activity as measured by indirect hemolysis of red blood cells but it was neither lethal when injected i.p. into mice nor did it present anticoagulant activity. Furthermore, LM-PLA2 displayed a moderate inhibitory activity on the aggregation of rabbit platelets induced by low levels of ADP, thrombin and arachidonate. In contrast, platelet aggregation induced by high doses of collagen was strongly inhibited by LM-PLA2 as well as ATP-release. Treatment of the protein with p-bromophenacyl bromide or 2-mercapto-ethanol, as well as thermal inactivation studies, suggested that the platelet inhibitory effect of LM-PLA2 is dependent on its enzymatic activity. Thus, the platelet inhibitory activity of LM-PLA2 was shown to be dependent on the hydrolysis of plasma phospholipids and/or lipoproteins, most probably those rich in phosphatidylcholine. Surprisingly, lyso-phosphatidylcholine released by LM-PLA2 from plasma was shown to preferentially inhibited collagen-induced platelet aggregation, in contrast to other PLA2s, whose plasma hydrolytic products indistinctly affect platelet’s response to several agonists.

Stimulation of Ca(2+)-dependent exocytosis of the sperm acrosome by cAMP acting downstream of phospholipase A2

Reproduction ◽  
2000 ◽  
pp. 57-68 ◽  
Author(s):  
J Garde ◽  
ER Roldan
Keyword(s):  
Arachidonic Acid ◽  
Phospholipase A2 ◽  
Phospholipase C ◽  
Phosphodiesterase Inhibitors ◽  
Dibutyryl Camp ◽  
Camp Phosphodiesterase ◽  
Ram Sperm ◽  
Camp Formation ◽  
Stimulation Of

Spermatozoa undergo exocytosis in response to agonists that induce Ca2+ influx and, in turn, activation of phosphoinositidase C, phospholipase C, phospholipase A2, and cAMP formation. Since the role of cAMP downstream of Ca2+ influx is unknown, this study investigated whether cAMP modulates phospholipase C or phospholipase A2 using a ram sperm model stimulated with A23187 and Ca2+. Exposure to dibutyryl-cAMP, phosphodiesterase inhibitors or forskolin resulted in enhancement of exocytosis. However, the effect was not due to stimulation of phospholipase C or phospholipase A2: in spermatozoa prelabelled with [3H]palmitic acid or [14C]arachidonic acid, these reagents did not enhance [3H]diacylglycerol formation or [14C]arachidonic acid release. Spermatozoa were treated with the phospholipase A2 inhibitor aristolochic acid, and dibutyryl-cAMP to test whether cAMP acts downstream of phospholipase A2. Under these conditions, exocytosis did not occur in response to A23187 and Ca2+. However, inclusion of dibutyryl-cAMP and the phospholipase A2 metabolite lysophosphatidylcholine did result in exocytosis (at an extent similar to that seen when cells were treated with A23187/Ca2+ and without the inhibitor). Inclusion of lysophosphatidylcholine alone, without dibutyryl-cAMP, enhanced exocytosis to a lesser extent, demonstrating that cAMP requires a phospholipase A2 metabolite to stimulate the final stages of exocytosis. These results indicate that cAMP may act downstream of phospholipase A2, exerting a regulatory role in the exocytosis triggered by physiological agonists.

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