Generic placeholder image

Current Enzyme Inhibition

Editor-in-Chief

ISSN (Print): 1573-4080
ISSN (Online): 1875-6662

Review Article

Evaluation of the Pharmacological Properties of Piscine Venoms from both Lionfish (Pterois) and Stonefish (Synanceja)

Author(s): Karthikeyan Ramalingam*

Volume 17 , Issue 1 , 2021

Published on: 31 December, 2020

Page: [9 - 15] Pages: 7

DOI: 10.2174/1573408016999201231204746

Price: $65

Abstract

Background: For the past 70 years, the focus of research is on the search for poisons and toxins found in venomous and poisonous organisms, purely directed towards the pharmacological properties of the toxins. In the research of finding novel compounds in pharmaceutical research, the identified source was the piscine venom.

Objective: The Scorpaenidae family was considered the most venomous of all. The toxins isolated from stonefish and lionfish are responsible for the effects caused in cardiovascular and neuromuscular systems and also for causing cytolytic activities. The main objective of the review is to study the mechanism of the stonefish venom and portray its benefits in the field of drug discovery.

Methods: A study on the mechanism of stonefish venom was carried out by inducing cardiovascular endothelium. The release of neurotransmitter signals thus leads to the depolarisation of cell membrane by the formation of pores in the cell membrane in the neuromuscular system of rabbits, porcine artery, mice and rats. Lionfish venom in cross-reactivity with the results evolved from a stonefish venom activity. The presence of enzymatic hyaluronidases in the primary structures of lionfish has evolved from stonefish and their anticancer potential has also been demonstrated for the benefits of drug discovery as they possess biological and chemical activity.

Conclusion: This review depicts an overview of the pharmacological activities of lionfish venom in comparison with the stonefish venom and their purpose of applications for future research in drug discovery.

Keywords: Lionfish venom, stonefish venom, scorpaenidae, neurotoxins, pharmacological activities, drug discovery.

Graphical Abstract
[1]
Church JE, Hodgson WC. Adrenergic and cholinergic activity contributes to the cardiovascular effects of lionfish (Pterois volitans) venom. Toxicon 2002; 40(6): 787-96.
[http://dx.doi.org/10.1016/S0041-0101(01)00285-9] [PMID: 12175616]
[2]
Ziegman R, Alewood P. Bioactive components in fish venoms. Toxins (Basel) 2015; 7(5): 1497-531.
[http://dx.doi.org/10.3390/toxins7051497] [PMID: 25941767]
[3]
Williamson JA. Clinical toxicology of venomous Scorpaenidae and other selected fish stingsClinical Toxicology of Animal Venoms and Poisons. Florida: CRC Press 1995; pp. 142-58.
[4]
Wilkinson C, Souter D, Goldberg J. Status of Coral Reefs in Tsunami Affected Countries: 2005 Townsville: Australian Institute of Marine Science and Global Coral Reef Monitoring Network. 2006; p. 154.
[5]
Halstead BW. Poisonous and venomous marine animals of the world. Vancouver, WA, U. S. A 1967; p. 2.
[6]
Moyle PB, Cech JJ Jr. Fishes: An Introduction to Ichthyology. 3rd ed. USA: Prentice- Hall 1996; pp. 308-9.
[7]
Russell FE. Marine toxins and venomous and poisonous marine animals Advances in Marine Biology. London: Academic Press 1965; Vol. 3: pp. 255-384.
[8]
Garnier P, Goudey-Perrière F, Breton P, Dewulf C, Petek F, Perrière C. Enzymatic properties of the stonefish (Synanceia verrucosa Bloch and Schneider, 1801) venom and purification of a lethal, hypotensive and cytolytic factor. Toxicon 1995; 33(2): 143-55.
[http://dx.doi.org/10.1016/0041-0101(94)00151-W] [PMID: 7597718]
[9]
Saunders PR, Taylor PB. Venom of the lionfish Pterois volitans. Am J Physiol 1959; 197: 437-40.
[http://dx.doi.org/10.1152/ajplegacy.1959.197.2.437] [PMID: 14441961]
[10]
Choromanski JM. Chemical stabilization and pharmacological characterization of the venom of the lionfish, Pterois volitans. 1985.http://hdl.handle.net/1957/9347
[11]
Tay TK, Chan HZ, Ahmad TS, Teh KK, Low TH, Wahab NA. Stonefish envenomation of hand with impending compartment syndrome. J Occup Med Toxicol 2016; 11: 23.
[http://dx.doi.org/10.1186/s12995-016-0112-y] [PMID: 27168760]
[12]
Haddad V Jr, Martins IA, Makyama HM. Injuries caused by scorpionfishes (Scorpaena plumieri Bloch, 1789 and Scorpaena brasiliensis Cuvier, 1829) in the Southwestern Atlantic Ocean (Brazilian coast): epidemiologic, clinic and therapeutic aspects of 23 stings in humans. Toxicon 2003; 42(1): 79-83.
[http://dx.doi.org/10.1016/S0041-0101(03)00103-X] [PMID: 12893064]
[13]
Resiere D, Cerland L, De Haro L, et al. Envenomation by the invasive Pterois volitans species (lionfish) in the French West Indies--a two-year prospective study in Martinique. Clin Toxicol (Phila) 2016; 54(4): 313-8.
[http://dx.doi.org/10.3109/15563650.2016.1143100] [PMID: 26857556]
[14]
Thomas L, Tharakaram S. Lionfish envenomation: Relapses controlled by intralesional triamcinolone. Indian J Dermatol Venereol Leprol 2016; 82(4): 438-9.
[http://dx.doi.org/10.4103/0378-6323.181472] [PMID: 27279312]
[15]
Diaz JH. Invasive Lionfish (Pterosis volitans) Pose Public Health Threats. J La State Med Soc 2015; 167(4): 166-71.
[PMID: 27159509]
[16]
Haddad V Jr, Stolf HO, Risk JY, França FO, Cardoso JL. Report of 15 injuries caused by lionfish (pterois volitans) in aquarists in Brazil: a critical assessment of the severity of envenomations. J Venom Anim Toxins Incl Trop Dis 2015; 2021: 8.
[17]
Auerbach PS, McKinney HE, Rees RS, Heggers JP. Analysis of vesicle fluid following the sting of the lionfish Pterois volitans. Toxicon 1987; 25(12): 1350-3.
[http://dx.doi.org/10.1016/0041-0101(87)90014-6] [PMID: 3438924]
[18]
Khoo HE. Bioactive proteins from stonefish venom. Clin Exp Pharmacol Physiol 2002; 29(9): 802-6.
[http://dx.doi.org/10.1046/j.1440-1681.2002.03727.x] [PMID: 12165046]
[19]
Shiomi K, Josaka M, Fujita S, Yumanaka H, Kikuchi T. Venoms from six species of marine fish: lethal and haemolytic activities and their neutralization b commercial stone fish anti venom. Mar Biol 1989; 103: 285-9.
[http://dx.doi.org/10.1007/BF00397261]
[20]
Rodrigues RJ. Pharmacology of South American freshwater stingray venom (Potamotrygon motoro). In: Trans N V Acad Sd. 1972; pp. 677-86.
[21]
Church JE, Hodgson WC. Dose-dependent cardiovascular and neuromuscular effects of stonefish (Synanceja trachynis) venom. Toxicon 2000; 38(3): 391-407.
[http://dx.doi.org/10.1016/S0041-0101(99)00169-5] [PMID: 10669028]
[22]
Fenner PJ. Marine envenomation: An update-a presentation on the current status of marine envenomation first aid and medical treatments. Emerg Med 2000; 12: 295-302.
[http://dx.doi.org/10.1046/j.1442-2026.2000.00151.x]
[23]
Sri Balasubashini M, Karthigayan S, Somasundaram ST, et al. Fish venom (Pterios volitans) peptide reduces tumor burden and ameliorates oxidative stress in Ehrlich’s ascites carcinoma xenografted mice. Bioorg Med Chem Lett 2006; 16(24): 6219-25.
[http://dx.doi.org/10.1016/j.bmcl.2006.09.025] [PMID: 17000104]
[24]
Gomes HL, Menezes TN, Malacarne PF, et al. Cardiovascular effects of Sp-CTx, a cytolysin from the scorpionfish (Scorpaena plumieri) venom. Toxicon 2016; 118(118): 141-8.
[http://dx.doi.org/10.1016/j.toxicon.2016.05.002] [PMID: 27155562]
[25]
Low KSY, Gwee MCE, Yuen R, Gopalakrishnakone P, Khoo HE. Stonustoxin: Effects on neuromuscular function in vitro and in vivo. Toxicon 1994; 32(5): 573-81.
[http://dx.doi.org/10.1016/0041-0101(94)90205-4] [PMID: 8079369]
[26]
Cohen AS, Olek AJ. An extract of lionfish (Pterois volitans) spine tissue contains acetylcholine and a toxin that affects neuromuscular transmission. Toxicon 1989; 27(12): 1367-76.
[http://dx.doi.org/10.1016/0041-0101(89)90068-8] [PMID: 2560846]
[27]
Sutherland SK, Tibballs J. Australian Animals Toxins: The Creatures, their Toxins and Care of the Poisoned Patient. 2nd ed. Melbourne: Oxford University Press 2001.
[28]
Church JE, Hodgson WC. The pharmacological activity of fish venoms. Toxicon 2002; 40(8): 1083-93.
[http://dx.doi.org/10.1016/S0041-0101(02)00126-5] [PMID: 12165309]
[29]
Church JE, Moldrich RX, Beart PM, Hodgson WC. Modulation of intracellular Ca2+ levels by Scorpaenidae venoms. Toxicon 2003; 41(6): 679-89.
[http://dx.doi.org/10.1016/S0041-0101(03)00038-2] [PMID: 12727272]
[30]
Meunier FA, Mattei C, Chameau P, et al. Trachynilysin mediates SNARE-dependent release of catecholamines from chromaffin cells via external and stored Ca2+. J Cell Sci 2000; 113(Pt 7): 1119-25.
[PMID: 10704363]
[31]
Sauviat MP, Meunier FA, Kreger A, Molgó J. Effects of trachynilysin, a protein isolated from stonefish (Synanceia trachynis) venom, on frog atrial heart muscle. Toxicon 2000; 38(7): 945-59.
[http://dx.doi.org/10.1016/S0041-0101(99)00207-X] [PMID: 10728832]
[32]
Kreger AS, Molgó J, Comella JX, Hansson B, Thesleff S. Effects of stonefish (Synanceia trachynis) venom on murine and frog neuromuscular junctions. Toxicon 1993; 31(3): 307-17.
[http://dx.doi.org/10.1016/0041-0101(93)90148-C] [PMID: 8470134]
[33]
Colasante C, Meunier FA, Kreger AS, Molgó J. Selective depletion of clear synaptic vesicles and enhanced quantal transmitter release at frog motor nerve endings produced by trachynilysin, a protein toxin isolated from stonefish (Synanceia trachynis) venom. Eur J Neurosci 1996; 8(10): 2149-56.
[http://dx.doi.org/10.1111/j.1460-9568.1996.tb00736.x] [PMID: 8921306]
[34]
Moldrich RX, Giardina SF, Beart PM. Group II mGlu receptor agonists fail to protect against various neurotoxic insults induced in murine cortical, striatal and cerebellar granular pure neuronal cultures. Neuropharmacology 2001; 41(1): 19-31.
[http://dx.doi.org/10.1016/S0028-3908(01)00045-4] [PMID: 11445182]
[35]
Chen D, Kini RM, Yuen R, Khoo HE. Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: Pore formation and the role of cationic amino acid residues. Biochem J 1997; 325(Pt 3): 685-91.
[http://dx.doi.org/10.1042/bj3250685] [PMID: 9271089]
[36]
Memar B, Jamili S, Shahbazzadeh D, Bagheri KP. The first report on coagulation and phospholipase A2 activities of Persian Gulf lionfish, Pterois russelli, an Iranian venomous fish. Toxicon 2016; 113: 25-31.
[http://dx.doi.org/10.1016/j.toxicon.2016.02.004] [PMID: 26853495]
[37]
Kiriake A, Madokoro M, Shiomi K. Enzymatic properties and primary structures of hyaluronidases from two species of lionfish (Pterois antennata and Pterois volitans). Fish Physiol Biochem 2014; 40(4): 1043-53.
[http://dx.doi.org/10.1007/s10695-013-9904-5] [PMID: 24395601]
[38]
EI-Safory NS. Fazary AE, Lee C. Hyaluronidases, a group of glycosidases: Current and future perspectives. Carbohydr Polym 2010; 81: 165-81.
[http://dx.doi.org/10.1016/j.carbpol.2010.02.047]
[39]
Poh CH, Yuen R, Khoo HE, Chung M, Gwee M, Gopalakrishnakone P. Purification and partial characterization of stonustoxin (lethal factor) from Synanceja horrida venom. Comp Biochem Physiol B 1991; 99(4): 793-8.
[http://dx.doi.org/10.1016/0305-0491(91)90143-2] [PMID: 1790672]
[40]
Tintore SG, Perez CM, Guerrero LC, Perera AA, Ancona DZB. Antioxidant activity of Lion Fish (Pterois volitans L.) muscle protein hydrolysates. J Food Process Technol 2014; 5: 4.
[41]
Balasubashini MS, Karthigayan S, Somasundaram ST, Balasubramanian T, Viswanathan P, Menon VP. In vivo and in vitro characterization of the biochemical and pathological changes induced by lionfish (pterios volitans) venom in mice. Toxicol Mech Methods 2006; 16(9): 525-31.
[http://dx.doi.org/10.1080/15376510600803573] [PMID: 20020995]
[42]
Sri Balasubashini M, Karthigayan S, Somasundaram STT, Balasubramanian T, Rukkumani R, Menon VP. FV peptide induces apoptosis in HEp 2 and HeLa cells: An insight into the mechanism of induction. J Carcinog 2006; 5: 27.
[http://dx.doi.org/10.1186/1477-3163-5-27] [PMID: 17137521]
[43]
Gerl R, Vaux DL. Apoptosis in the development and treatment of cancer. Carcinogenesis 2005; 26(2): 263-70.
[http://dx.doi.org/10.1093/carcin/bgh283] [PMID: 15375012]
[44]
Aissaoui N, Abidi F, Hardouin J, et al. Two novel peptides with angiotensin I converting enzyme inhibitory and antioxidative activities from Scorpaena notata muscle protein hydrolysate. Biotechnol Appl Biochem 2016.
[PMID: 26799603]
[45]
Burns JR, Morton CJ, Parker MW, Tweten RK. An intermolecular π-stacking interaction drives conformational changes necessary to β-barrel formation in a poreforming toxin. MBio 2019; 10(4): e01017-9.
[http://dx.doi.org/10.1128/mBio.01017-19] [PMID: 31266869]

Rights & Permissions Print Export Cite as
© 2022 Bentham Science Publishers | Privacy Policy