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  • Title: Presynaptically acting snake venom phospholipase A2 enzymes attack unique substrates.
    Author: Fletcher JE, Jiang MS.
    Journal: Toxicon; 1995 Dec; 33(12):1565-76. PubMed ID: 8866614.
    Abstract:
    Synaptosomes were incubated with bovine serum albumin (BSA) to examine whether the presynaptic action of snake venom phospholipase A2 (PLA2) toxins is due either to the release of fatty acids resistant to extraction by BSA or to the liberation of a specific fatty acid type. In the presence of BSA (0.5% or 1.0%) two PLA2 enzymes from Naja naja atra and Naja naja kaouthia snake venoms that do not have a predominant presynaptic action at the neuromuscular junction (PS-) did not stimulate acetylcholine (ACh) release from synaptosomes. In contrast, two PLA2 enzymes (beta-bungarotoxin, scutoxin) that do have a predominant presynaptic action at the neuromuscular junction (PS+) did stimulate ACh release. BSA did not antagonize PS- enzymes by more efficiently extracting the fatty acids produced by these enzymes relative to PS+ enzymes. While absolute amounts of total and unsaturated fatty acid produced overlapped for the PS- and PS+ enzymes, the two PS+ enzymes produced a significantly greater absolute amount and relative percentage of palmitic acid (16:0) than did either of the PS- enzymes. However, the levels of free palmitic acid remaining in the synaptosomes where they would exert effects on ACh release were similar for the N. n. kaouthia PLA2 (PS-) and beta-bungarotoxin (PS+). Therefore, the total (supernatant plus synaptosomal) amount of palmitic acid produced per se did not account for stimulation of ACh release, since the greater amounts produced by the PS+ enzymes were removed from the synaptosomes by BSA. The production of higher levels of palmitic acid suggests either that PS+ enzymes gain access to sites containing phospholipid substrates unavailable to the PS- enzymes, or that they have a different substrate preference. These findings suggest new possibilities for the mechanism of PS+PLA2 action, including site-directed enzymatic activity and protein acylation.
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