Journal of Physiology & Pathology in Korean Medicine (동의생리병리학회지)

The Physiological Society of Korean Medicine and The Society of Pathology in Korean Medicine (대한동의생리학회·한의병리학회)
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The Extracts of Kalopanax pictus Nakai. for Inhibitory Effects on HIV-1 and Its Essential Enzymes

Human Immunodeficiency Virus Type Ⅰ에 대한 음나무 추출물의 억제활성

  • Yu Young Beob (Department of Medical Research, Korea Institute of Oriental Medicine) ;
  • Shim Bum Sang (Department of Oriental Pathology, College of Oriental Medicine, Kyunghee University) ;
  • Ahn Kyoo Seok (Department of Oriental Pathology, College of Oriental Medicine, Kyunghee University) ;
  • Choi Seung Hoon (WHO Western Pacific Regional Office) ;
  • Park Jong Cheol (Department of Oriental Medicine Resources, Sunchon National University) ;
  • Miyashiro H. (Research Institute for Wakan Yaku, Toyama Medical and Pharmaceutical University) ;
  • Hattori M. (Research Institute for Wakan Yaku, Toyama Medical and Pharmaceutical University)
  • 유영법 (한국한의학연구원 의료연구부) ;
  • 심범상 (경희대학교 한의과대학 병리학교실) ;
  • 안규석 (경희대학교 한의과대학 병리학교실) ;
  • 최승훈 (WHO 서태평양지역사무국 전통의약담당) ;
  • 박종철 (순천대학교 한약자원학과) ;
  • ;
  • Published : 2004.08.01
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Abstract

For the purpose of developing new anti-HIV agents from natural sources, the extracts of Kalopanax pictus were tested for their inhibitory effects on HIV-1 replication and its essential enzymes as the reverse transcriptase (RT). protease and α-glucosidase. In the assay of HIV-1-infected human T-cell line, water extracts of stem and leafstalk inhibited the HIV-1-induced cytopathic effects with Ie (inhibitory concentration) of 25 and 50㎍/㎖, respectively. Moreover water extracts (100㎍/㎖) of stem and leafstalk showed strong activity of 80% and 90% on anti-HIV-1 RT using Enzyme Linked Oligonucleotide Sorbent Assay (ELOSA) method. In the HIV-1 protease inhibition assay, aqueous stem extract inhibited the activity of the enzyme to cleave an oligopeptide, resembling one of the cleavage sites in the viral polyprotein which can only be processed by HIV-1 protease with 58%, but no glucosidase inhibitory activities. We found out this result, for these samples it is possible that the inhibition of the viral replication in vitro is due to the inhibition at least one of RT and protease. It would be of great interest to identify the compounds which are responsible for this inhibition, since all therapeutically useful agent up to date are RT, PR and α-glucosidase inhibitors.

Keywords

References

  1. Journal of Natural Products v.64 no.2 Natural product-based anti-HIV drug discovery and development facilitated by the NCI developmental therapeutics program Yang, S. S.;Cragg, G. M.;Newman, D. J.;Bader, J. P.
  2. 생약학회지 v.29 no.4 Human Immunodeficiency Virus Type Ⅰ에대한 수종 식물 추출물의 억제활성 검색 유영법;박종철;이종호;김경업;조성기;변명우;Hirotsu Miyashiro;Masao Hattori.
  3. Journal of Medicinal Chemistry v.35 no.15 HIV-1 neutralization and tumor cell proliferation inhibition in vitro by simplified analogues of pyrido[4,3,2-mn]thiazolo[5,4-b]acridine marine alkaloids Taraporewala, I.B.;Cessac, J.W.;Chanh, T.C.;Delgado, A.V.;Schinazi, R.F.
  4. Antiviral Research v.18 Inhibition of human immunodeficiency viral replication by tannins and related compounds Nakashima, H.;Murakami, T.;Yamamoto, N.;Sakagami, H.;Tanuma, S.;Hatano, T.;Yoshida, T.;Okuda, T.
  5. Phytotherpy Research v.9 Screening of various plant extracts used in ayurvedic medicine for inhibitory effects on human immunodeficiency virus type 1 (HIV-1) protease Kusumoto, I.T.;Nakabayashi, T.;Kida, H.;Miyashiro, H.;Hattori, M.;Namba T.;Shimotohno, K.
  6. 대한식물도감 이창복
  7. 완역중약대사전 이경순;김창민;신민교;안덕균
  8. 생약학회지 v.33 no.4 해동피로부터 Kalopanax - saponin B의 분리 및 함량분석 홍성수;황지상;허재두;노재섭;이경순
  9. Korean Journal of Pharmacognosy v.33 no.4 Flavonol glycosides from the leaves of Kalopanax pictum Jung, K.Y.;Son, K.H.;Do, J.C.
  10. 생약학회지 v.32 no.4 음나무 수피의 화학적성분 홍성수;한두일;황방연;최우희;강호상;이명구;이동구;이경순;노재섭
  11. 생약학회지 v.26 no.2 해동피의 화학성분 및 생리활성 이은;최무영;박희준;차배천;조순현
  12. 한국식품영양과학회지 v.18 no.3 해동피추출물이 실험적으로 유발된 가토의 간장기능장애에 미치는 영향 전성주;서화중
  13. Science v.243 Structural origins of high-affinity biotin binding to streptavidin Weber, P.C.;Ohlendorf, D.H.;Wendoloski, J.J.;Salemme, F.R.
  14. J. Traditional medicines v.11 Anti-human immunodeficiency virus activity of som tropical medicinal plants Otake, T.;Mori, H.;Morimoto, M.;Ueba, N.;Kusumoto, I.T.
  15. Aids Research and Human Retroviruses v.10 Cellular distribution of HIV type Ⅰ nef protein: Identification of domains in nef required for association with membrane and detergent-insoluble cellular matrix Kaminchik, J.;Margalit R.;Yaish S.;Drummer H.;Amit B.;Saver N.;Gorecki M.;Panet A.
  16. Science v.258 Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reversetranscriptase Peliska, J.A.;Benkovic, S. J.
  17. Proc. Natl. Acad. Sci. USA. v.86 Linker insertion mutagenesis of human immunodeficiency virus reversetranscriptase expressed in bacteria: definition of the minimal polymerase domain Prasad, V.R.;Goff, S.P.
  18. Annu. Rev. Biochem. v.63 The retroviral enzymes Katz, R.A.;Skalka, A.M.
  19. Antimicrobacterial Agents & Chemotherapy v.38 no.8 Inhibition of alpha-glucosidase I of the glycoprotein-processing enzymes by 6-O-butanoyl castanospermine (MDL 28,574) and its consequences in human immunodeficiency virus-infected T cells Taylor, D.L.;Kang, M.S.;Brennan, T.M.;Bridges, C.G.;Sunkara, P.S.;Tyms, A.S.
  20. Pharmaceutical Research v.9 no.6 Anti-AIDS drug development: challenges and strategies Mohan, P.
  21. Journal of Natural Products v.48 no.4 Inhibitory effect of tannins on reverse transcriptase from RNA tumor virus Kakiuchi, N.;Hattori, M.;Namba T.
  22. Journal of Biological Chemistry v.267 The V3 region of the envelope glycoprotein of human immunodeficiency virus type 1 binds sulfated polysaccharides and CD4-derived synthetic peptides Batinic, D.;Robey, R.A.
  23. Antiviral Res. v.18 Balzar·n-specific plant lectin from Urtica dioica are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replication in vitro
  24. Proc. Natl. Acad. Sci. USA. v.91 Triterpene derivatives that block entry of human immunodeficiency virus type 1 into cells Mayaux, J.F.;Bousseau, A.;Pauwels, R.;Huet, T.;Henin, Y.;Dereu, N.; Evers, M.;Soler, F.;Poujade, C.;De Clercq, E.;Le Pecq J.B.
  25. Proc. Natl. Acad. Sci. USA. v.85 Antiviral agents targeted to interact with viral capsid proteins and a possible application to human immunodeficiency virus Rossmann, M.G.