Mechanism of action of the platelet function inhibitor from Vipera russelli siamensis snake venom

Li, Yue-Sheng; Kwang-Fen, Liu; Wang, Qing-Chuang

doi:10.1016/0041-0101(86)90088-7

Cited by 12 publications

(4 citation statements)

References 17 publications

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“…In the case of PLA 2 enzymatic activity dependent induction, the induced effects may be caused by the hydrolysis of critical phospholipids or by the released lysophospholipids and/or fatty acids (Lin-Shiau et al, 1978;Andreasen et al, 1979;Rosenberg, 1986). In the case of PLA 2 enzymatic activity independent induction, the effects may be induced by the physical binding of PLA 2 s to their targets (Bevan & Hiestand, 1983;Freedman & Snyder, 1981;Li et al, 1986). For the snake-venom PLA 2 s possessing anticoagulant activity, the enzymes appear to inhibit the formation of the prothrombinase complex composed of haemostatic factors Va and X, phospholipids and calcium ions by degrading the phospholipids involved in the complex (Verheij et al, 1980;Kini & Evans, 1988).…”

Section: Introductionmentioning

confidence: 99%

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Huang

Zhu

et al. 2000

Acta Crystallogr D Biol Cryst

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Acutohaemolysin, a phospholipase A(2) (PLA(2)) from the venom of the snake Agkistrodon acutus, has been isolated and purified to homogeneity by anion-exchange chromatography on a DEAE-Sepharose column followed by cation-exchange chromatography on a CM-Sepharose column. It is an alkaline protein with an isoelectric point of 10.5 and is comprised of a single polypeptide chain of 13 938 Da. Its N-terminal amino-acid sequence shows very high similarity to Lys49-type PLA(2) proteins from other snake venoms. Although its PLA(2) enzymatic activity is very low, acutohaemolysin has a strong indirect haemolytic activity and anticoagulant activity. Acutohaemolysin crystals with a diffraction limit of 1.60 A were obtained by the hanging-drop vapour-diffusion method. The crystals belong to the space group C2, with unit-cell parameters a = 45.30, b = 59.55, c = 46.13 A, beta = 117.69 degrees. The asymmetric unit contains one molecule.

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Section: Introductionmentioning

confidence: 99%

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Huang

Zhu

et al. 2000

Acta Crystallogr D Biol Cryst

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“…Ouyang and Huang (38) have proposed that Trimeresurus gramineus PLA2 probably acts on a common final step of intercellular adhesion between activated platelets. Li et al (18) studied the PLA2 of Vipera russelli siamensis and suggested that increasing platelet cyclic AMP and disruption of the cytoskeleton of platelets are the mechanisms of inhibition. However, the mode of PLA2 action still remains unclear.…”

Section: Enzymatic Activity and Inhibition Of Platelet Aggregationmentioning

confidence: 99%

“…4) enzymes attack various vital organs and organ systems, inducing several pharmacological effects (1). They interfere with hemostasis in both coagulation (2)(3)(4)(5) and platelet functions (6)(7)(8). The mechanisms of inhibition of coagulation (9)(10)(11)(12)(13)(14)(15)(16) and platelet aggregation (17,18) by PLAz enzymes are not well understood.…”

Section: Introductionmentioning

confidence: 99%

“…They interfere with hemostasis in both coagulation (2)(3)(4)(5) and platelet functions (6)(7)(8). The mechanisms of inhibition of coagulation (9)(10)(11)(12)(13)(14)(15)(16) and platelet aggregation (17,18) by PLAz enzymes are not well understood. The essentiality of enzymatic activity in inducing these pharmacological effects is controversial and still unproven (10)(11)(12)(13)(14)(15)(16)19).…”

Section: Introductionmentioning

confidence: 99%

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Correlation Between the Enzymatic Activity, Anticoagulant and Antiplatelet Effects of Phospholipase A2 Isoenzymes from Naja nigricollis Venom

Kini

Evans

1988

Thromb Haemost

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SummaryThe three phospholipase A2 isoenzymes from Naja nigricollis crawshawii snake venom inhibit both blood coagulation and platelet aggregation. To investigate the correlation between phospholipid splitting ability of these enzymes and their inhibitory activities, the effects of various preincubation times and the inclusion of EDTA were examined. Preincubation of plasma and thromboplastin with the phospholipase isoenzymes resulted in an increase in Ca2+-initiated clotting time with time of preincubation. Incubation of the isoenzymes with EDTA before their addition to the plasma-thromboplastin mixture reduced the anticoagulant effect. These results indicate that the catalytic activity contributes at least partially to the anticoagulant effect. However, inhibition of platelet aggregation appears to be independent of enzymatic activity since there is no increase in inhibition with time of preincubation of platelets and phospholipases, and inclusion of EDTA has no significant effect on inhibition of aggregation. All three enzymes appear to belong to class B of the platelet affector PLA2 enzymes as determined by platelet effects, since they do not initiate platelet aggregation.

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Phospholipase A2 with Platelet Aggregation Inhibitor Activity from Austrelaps superbus Venom: Protein Purification and cDNA Cloning

Singh

Armugam

Kini

et al. 2000

Archives of Biochemistry and Biophysics

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Mechanism of action of the platelet function inhibitor from Vipera russelli siamensis snake venom

Cited by 12 publications

References 17 publications

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Characterization, crystallization and preliminary X-ray diffraction analysis of acutohaemolysin, a haemolytic toxin fromAgkistrodon acutusvenom

Correlation Between the Enzymatic Activity, Anticoagulant and Antiplatelet Effects of Phospholipase A2 Isoenzymes from Naja nigricollis Venom

Phospholipase A2 with Platelet Aggregation Inhibitor Activity from Austrelaps superbus Venom: Protein Purification and cDNA Cloning

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