Role of catalytic function in the antiplatelet activity of phospholipase A2 cobra (Naja naja naja) venom

Three acidic phospholipases A2 from Indian cobra (Naja naja naja) venom inhibited platelet aggregation in platelet rich plasma induced separately by ADP, collagen and epinephrine with different potencies. The order of inhibition was epinephrine > collagen > ADP. They did not inhibit platelet a...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 2001-03, Vol.219 (1-2), p.39-44
Main Authors: Rudrammaji, L M, Machiah, K D, Kantha, T P, Gowda, T V
Format: Article
Language:English
Subjects:
Acetophenones - pharmacology
Adenosine Diphosphate - pharmacology
Adrenergic Agonists - pharmacology
Animals
Blood Platelets - drug effects
Blood Platelets - metabolism
Catalysis
Collagen - pharmacology
Dose-Response Relationship, Drug
Elapid Venoms - chemistry
Elapid Venoms - enzymology
Elapid Venoms - isolation & purification
Enzymatic activity
Enzyme Inhibitors - pharmacology
Enzymes
Epinephrine - pharmacology
Humans
In Vitro Techniques
Isoenzymes - isolation & purification
Isoenzymes - metabolism
Naja naja naja
Phospholipases A - isolation & purification
Phospholipases A - metabolism
Phospholipases A2
Platelet Aggregation Inhibitors - pharmacology
Time Factors
Citations: Items that cite this one
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Summary:Three acidic phospholipases A2 from Indian cobra (Naja naja naja) venom inhibited platelet aggregation in platelet rich plasma induced separately by ADP, collagen and epinephrine with different potencies. The order of inhibition was epinephrine > collagen > ADP. They did not inhibit platelet aggregation induced by arachidonic acid (10 microM). The inhibition was dependent on concentration of the protein and the time of incubation of the phospholipases A2 with platelet rich plasma. Parabromophenacyl bromide modified PLA2 enzymes lost their enzymatic activity as well as platelet aggregation inhibition activity suggesting the involvement of catalytic function in platelet aggregation inhibitory activity.
ISSN:0300-8177
1573-4919
DOI:10.1023/A:1011002606505