Chemical stabilization and pharmacological characterization of the venom of the lionfish, Pterois volitans Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/p5547v39p

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  • There are well over 200 species of fishes which are known to be venomous, and which are capable of inflicting serious and potentially fatal wounds. Within this group, less than 5% have been studied even in the most preliminary manner and, to date, the basic chemical structure of even a single fish venom has not been elucidated. It is evident that the major reason for this apparent lack of knowledge is the inherent and extreme instability of fish venoms. Lionfish (Pterois volitans) venom stabilization was achieved with the addition of protease inhibitors during venom apparatus homogenization, and was confirmed by assay on an isolated fish heart preparation. Administration of stabilized lionfish venom to the isolated heart of the buffalo sculpin (Enophrys bison) resulted in a positive chronotropic effect from low doses (40 ug protein/ml), but produced a negative chronotropic effect from higher doses (100-200 ug protein/ml). Cardiac output changes coincided with those of the heart rate, and no ionotropic changes were detected at any dose. This same chronotropic effect difference produced by the higher doses of venom was also observed in the in vivo sculpin preparations. Venom administration to the live buffalo sculpin also produced a distinct increase in blood pressure not seen in the isolated heart preparations. This apparent increase in peripheral resistance produced by lionfish venom administration was also confirmed by use of an isolated tail/intact vasculature preparation, and is assumed to be due to vasoconstriction. Bioassay of the lionfish venom on juvenile buffalo sculpin resulted in a LD50 determination of 200 ug protein/kg. Stabilized lionfish venom was also analyzed with gel electrophoretic and high performance liquid chromatographic (HPLC) techniques. Gel electrophoretic separation of the venom revealed high molecular weight components in the range of 29,000 to 116,000. HPLC analysis with a Waters SW-300 protein column revealed three peaks when measured at 219 nm. Reverse phase HPLC analysis offered a greater resolution of the venom components and resulted in approximately 20 peaks. Fractions eluted from this separation which were administered to buffalo sculpin failed to produce any observable adverse effects. The varied effects produced by lionfish venom cannot be explained by a single mechanism. Although this venom may have direct effects on the cardiovascular system, indirect effects caused by the release of natural pharmacological substances and neurogenic reflex mechanisms must also be considered.
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