A Functional Review of Acidic Phospholipase A2 beta from Crotalus Adamanteus

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Venoms are comprised of a plethora of proteins that each serve a purpose. Some proteins serve as neurotoxins and interfere with muscle control by acting as competitive inhibitors for acetylcholine or by causing damage to the presynaptic membrane and subcellular organelles on nerve cells. In addition, there are hemotoxins which affect blood coagulation and platelet activity and myotoxins that damage skeletal muscle tissue through depolarization. All of these proteins, however, originate from different compounds already present in snakes. Scientists have grouped these proteins into different families based on their endophysiological base, the compound they were modified from. Of these families, the snake venom Group I phospholipase A2 (SV-GI-PLA2) and snake venom Group II phospholipase A2 (SV-GII-PLA2) are among the larger superfamilies. This project focuses on analyzing the functional activity of acidic phospholipase A2 beta, a SV-GII-PLA2, found in Crotalus adamanteus venom. We expected to see significant cytotoxic activity and expect to see significant production of arachidonic acid from the enzymatic activity of the phospholipase. A measure of cytotoxic activity using the MCF-7 cell line as a model has been completed, and a functional assay of the toxin's activity is currently in progress.

First Advisor

Victor Huber

Research Area

Basic Biomedical Science

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