Pancreatic and snake venom presynaptically active phospholipases A2 inhibit nicotinic acetylcholine receptors

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Pancreatic and snake venom presynaptically active phospholipases A2 inhibit nicotinic acetylcholine receptors

Phospholipases A2 (PLA2s) are enzymes found throughout the animal kingdom. They hydrolyze phospholipids in the sn-2 position producing lysophospholipids and unsaturated fatty acids, agents that can damage membranes. PLA2s from snake venoms have numerous toxic effects, not all of which can be explained by phospholipid hydrolysis, and each enzyme has a specific effect. We have earlier demonstrate...

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Inhibition of Nicotinic Acetylcholine Receptors, a Novel Facet in the Pleiotropic Activities of Snake Venom Phospholipases A2

Phospholipases A2 represent the most abundant family of snake venom proteins. They manifest an array of biological activities, which is constantly expanding. We have recently shown that a protein bitanarin, isolated from the venom of the puff adder Bitis arietans and possessing high phospholipolytic activity, interacts with different types of nicotinic acetylcholine receptors and with the acety...

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Structural and Functional Characterization of Anticoagulant, FXa-binding Viperidae Snake Venom Phospholipases A2.

Certain snake venom phospholipases A2 (PLA2) have been identified as specific, non-competitive blood coagulation inhibitors that bind with high affinity to human activated blood coagulation factor X (hFXa). Recent determination of the three-dimensional structures of PLA2 isoforms which differ in anticoagulant activity contributes to a better understanding of their mode of binding to human FXa. ...

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Activation of J77A.1 Macrophages by Three Phospholipases A2 Isolated from Bothrops atrox Snake Venom

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ژورنال

عنوان ژورنال: PLOS ONE

سال: 2017

ISSN: 1932-6203

DOI: 10.1371/journal.pone.0186206