Anti-microtubule activity of tubeimoside I and its colchicines binding site of tubulin

作     者：Rundi Ma~1 Gang Song~1 Wenbing You~1 Lijian Yu~(1*) Weiming Su~1 Mingneng Liao~1 Yongping Zhang~1 Laizhen Huang~1 Xiaoyu Zhang~(1,3) Tingxi Yu~(1,2) ~1Key Laboratory of Marine Materia Medica,Guangdong Ocean University,Jiefang East Avenue 40,Xiashan,Zhanjiang 524025,China ~2Department of Biochemistry and Molecular Biology,Public Health,Johns Hopkins University, Baltimore,MD 21205,USA ~3Department of Otorhinolaryngology-Head and Neck Surgery,University of Maryland School of Medicine,Baltimore,MD 21228,USA.The authors contributed equally to this work. 

会议名称：《第九届全国中药和天然药物学术研讨会》

会议日期：2007年

学科分类：1008[医学-中药学(可授医学、理学学位)] 1006[医学-中西医结合] 100602[医学-中西医结合临床] 10[医学] 

关 键 词：Bolbostemma paniculatum(Maxim.)Franquet Tubeimoside I Uptake kinetics Anti-microtubule activity Colchicine binding site of tubulin 

摘      要：Background:Tubeimoside I(TBMS1)was isolated from the tubers of Bolbostemma paniculatum(Maxim.)***1 shows potent antitumor *** present study was conducted to investigate the antimicrotubule role of TBMS1 and its binding site of ***:Cell growth inhibition was measured by MTT after treatment with *** kinetics of TBMS1 by human nasopharyngeal carcinoma CNE-2Z cell line(CNE-2Z)was assayed by *** protein(MTP)was prepared from porcine brain through two cycles of polymerization-depolymerization in a high molarity *** of MTP polymerization induced by TBMSI was determined by a turbidity measurement and a sedimentation assay:the interactions of TBMS1 with tuhulin within CNE-2Z cells were investigated by immunofluorescence microscopy and ***1 was tested for its ability to inhibit binding of known tubulin ligands through competitive binding ***:TBMS1 displayed growth inhibitory activity against CNE-2Z cells with ICvalue of 16.7μM for 72 *** analysis of TBMS1 uptake by CNE-2Z cells displayed the initial slow TBMS1 uptake and then gradually reaching an maximum uptake near 18 ***-2Z cells treated with TBMSI(25μM,3 h)were sufficient to cause the microtubular network disruption,lmmunohlot analysis showed that the proportion of cytosolic tubulin of cells treated with TBMS1 increased in a time-and concentration-dependent ***1 did not inhibit the binding of vinblastine to *** binding to tubulin was inhibited in the presence of ***:TBMS1 is an anti-microtubule agent,and its binding site of tubulin is the colchicine binding site of tubulin.