본문 바로가기
KERD
논문KCI 등재

Honey Bee Venom (Apis mellifera) Contains Anticoagulation Factors and Increases the Blood-clotting Time

2

조회

0

다운로드

3

인용

0

참고문헌

키워드

주제분류한의학

초록

Objectives: Bee venom (BV) is a complex mixture ofproteins and contains proteins such as phospholipaseand melittin, which have an effect on blood clottingand blood clots. The mechanism of action of honey beevenom (HBV, Apis mellifera) on human plasma proteinsand its anti-thrombotic effect were studied. The purposeof this study was to investigate the anti-coagulationeffect of BV and its effects on blood coagulation andpurification. Methods: Crude venom obtained from Apis melliferawas selected. The anti-coagulation factor of the crudevenom from this species was purified by using gel filtrationchromatography (sephadex G-50), and the molecularweights of the anti-coagulants in this venom estimatedby using sodium dodecyl sulfate-polyacrylamide gelelectrophoresis (SDS-PAGE). Blood samples were obtainedfrom 10 rabbits, and the prothrombin time (PT)and the partial thromboplastin time (PTT) tests wereconducted. The approximate lethal dose (LD) values ofBV were determined. Results: Crude BV increased the blood clotting time. For BV concentrations from 1 to 4 mg/mL, clotting wasnot observed even at more than 300 seconds, standard deviations (SDs) = ± 0.71; however, clotting was observedin the control group 13.8 s, SDs = ± 0.52. Thus,BV can be considered as containing anti-coagulationfactors. Crude BV is composed 4 protein bands withmolecular weights of 3, 15, 20 and 41 kilodalton (kDa),respectively. The LD50 of the crude BV was found to be177.8 μg/mouse. Conclusion: BV contains anti-coagulation factors. Thefraction extracted from the Iranian bees contains proteinsthat are similar to anti-coagulation proteins, suchas phospholipase A2 (PLA2) and melittin, and that canincrease the blood clotting times in vitro.

Abstract

Objectives: Bee venom (BV) is a complex mixture ofproteins and contains proteins such as phospholipaseand melittin, which have an effect on blood clottingand blood clots. The mechanism of action of honey beevenom (HBV, Apis mellifera) on human plasma proteinsand its anti-thrombotic effect were studied. The purposeof this study was to investigate the anti-coagulationeffect of BV and its effects on blood coagulation andpurification. Methods: Crude venom obtained from Apis melliferawas selected. The anti-coagulation factor of the crudevenom from this species was purified by using gel filtrationchromatography (sephadex G-50), and the molecularweights of the anti-coagulants in this venom estimatedby using sodium dodecyl sulfate-polyacrylamide gelelectrophoresis (SDS-PAGE). Blood samples were obtainedfrom 10 rabbits, and the prothrombin time (PT)and the partial thromboplastin time (PTT) tests wereconducted. The approximate lethal dose (LD) values ofBV were determined. Results: Crude BV increased the blood clotting time. For BV concentrations from 1 to 4 mg/mL, clotting wasnot observed even at more than 300 seconds, standard deviations (SDs) = ± 0.71; however, clotting was observedin the control group 13.8 s, SDs = ± 0.52. Thus,BV can be considered as containing anti-coagulationfactors. Crude BV is composed 4 protein bands withmolecular weights of 3, 15, 20 and 41 kilodalton (kDa),respectively. The LD50 of the crude BV was found to be177.8 μg/mouse. Conclusion: BV contains anti-coagulation factors. Thefraction extracted from the Iranian bees contains proteinsthat are similar to anti-coagulation proteins, suchas phospholipase A2 (PLA2) and melittin, and that canincrease the blood clotting times in vitro.

참고문헌 (28)

  1. Son DJ, "Therapeutic application of anti-arthritis, pain-releasing and anti-cancer effects of bee venom and its constituent compounds", Pharmacol Ther, 115(2), pp.246~270 (2007)
  2. Habermann E, "Über die struktur des toxischen bienengiftpeptids melittin und deren beziehung zur pharmakologischen wirkung", Naunyn Schmiedebergs Arch Pharmacol, 253(1), pp.40~41 (1966)
  3. Habermann E, "Comparative studies of native and synthetic melittins", Naunyn Schmiedebergs Arch Pharmakol, 270(1), pp.1~9 (1971)
  4. Shkenderov S, "Pcelni produkti, the bee products", pp.1~238 (1983), Zemizdat
  5. Kim JI, "Bee venom reduces neuroinflammation in the MPTP-induced model of Parkinson’s disease", Int J Neurosci, 121(4), pp.209~217 (2011)
  6. Münstedt K, "Bee products and their potential use in modern medicine", JAAS, 1(3), pp.57~63 (2009)
  7. Lee SM, "Effects of bee venom on glutamate-induced toxicity in neuronal and glial cells", Evid Based Complement Alternat Med (2012)
  8. Orslic N, "Bee venom in cancer therapy", Cancer Metastasis Rev, 31(1-2), pp.173~194 (2012)
  9. Mcdonald JA, "Cancer mortality among beekeepers", J Occup Med, 21(12), pp.811~813 (1979)
  10. 김정민, "Bee Venom Pharmacopuncture: An Effective Treatment for Complex Regional Pain Syndrome", Journal of Pharmacopuncture, 17(4), pp.66~69 (2014), 대한약침학회[DOI]
  11. Park JW, "Effects of sweet bee venom pharmacopuncture treatment for chemotherapy-induced peripheral neuropathy: a case series", Integr Cancer Ther, 11(2), pp.166~171 (2012)
  12. Abdu Al-Samie MA, "Studies on bee venom and its med-ical uses", IJOART, 1(2), pp.1~15 (2012)
  13. Rizzo F, "Measurement of prothrombin time(PT)and activated partial thromboplastin time(APTT)on canine citrated plasma samples following different storage conditions", Res Vet Sci, 85(1), pp.166~170 (2008)
  14. Lowry OH, "Protein measurement with the Folin phenol reagent", J Biol Chem, 193(1), pp.265~275 (1951)
  15. Meier J, "Approximate LD50 determination of snake venoms using eight to ten experimental animals", Toxicon, 24(4), pp.395~401 (1986)
  16. Maulet Y, "Purification from bee venom of melittin devoid of phospholipase A2 contamination", Anal Biochem, 127(1), pp.61~67 (1982)
  17. Babaie M, "Isolation and partial purification of anti-coagulant fractions from the venom of the Iranian snake Echis carinatus", Acta Biochim Pol, 60(1), pp.17~20 (2013)
  18. Laemmli UK, "Cleavage of structural proteins during the assembly of the head of bacteriophage T4", Nature, 227(5259), pp.680~685 (1970)
  19. Moreno M, "Three valuable peptides from bee and wasp venoms for therapeutic and biotechnological use: melittin, apamin and mastoparan", Toxins, 7(4), pp.1126~1150 (2015)
  20. Schmidt JO, "Comparative enzymology of venoms from stinging hymenoptera", Toxicon, 24(9), pp.907~921 (1986)
  21. Shipolini RA, "The amino-acid sequence and carbohydrate content of phospholipase A2 from bee venom", Eur J Biochem, 48(2), pp.465~476 (1974)
  22. Hoffman DR, "Allergens in hymenoptera venom XI: isolation of protein allergens from Vespula maculifrons (yellow jacket) venom", J Allergy Clin Immunol, 74(1), pp.93~103 (1984)
  23. Hoffman DR, "Allergens in hymenoptera venom XIII: Isolation and purification of protein components from three species of vespid venoms", J Allergy Clin Immunol, 75(5), pp.599~605 (1985)
  24. Hoffman DR, "Allergens in hymenoptera venom XX: isolation of four allergens from imported fire ant (Solenopsis invicta) venom", J Allergy Clin Immunol, 82(5), pp.818~827 (1988)
  25. Edstrom A. Venomous, "Venomous and poisonous animals", pp.210~220 (1992), Krieger Publishing Company
  26. Habermann E, "Bee and wasp venoms", Science, 177(4046), pp.314~322 (1972)
  27. Owen MD, "Melittin synthesis in the venom system of the honey bee (Apis mellifera L.)", Toxicon, 33(9), pp.1181~1188 (1995)
  28. Benton AW, "Venom toxicity and proteins of the genus Apis", J Api Res, 7(3), pp.113~118 (1968)

관련 논문AI추천

이 간행물의 다른 논문 (9건)