Acceso abierto

Detrimental effects of geldanamycin on adults and larvae of Trichinella spiralis


Cite

Alford, K., Obendorf, D.L., Fredeking, E., Haehling, E., Stewart, G.L. (1998): Comparison of the inflammatory responses of mice with American and Australian Trichinella pseudospiralis or Trichinella spiralis. Int. J. Parasitol., 28: 343 – 348. DOI: 10.1016/ S0020-7519(97)00184-7AlfordKObendorfDLFredekingEHaehlingEStewartGL1998Comparison of the inflammatory responses of mice with American and Australian Trichinella pseudospiralis or Trichinella spiralis. IntJ. Parasitol2834334810.1016/ S0020-7519(97)00184-7Open DOISearch in Google Scholar

Aligue, R., Akhavan-Niak, H., Russell, P. (1994): A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90. EMBO J., 13: 6099 – 6106AligueRAkhavan-NiakHRussellP1994A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90EMBO J136099610610.1002/j.1460-2075.1994.tb06956.xSearch in Google Scholar

Birnby, D.A., Link, E.M., Vowels, J.J., Tian, H., Colacurcio, P.L., Thomas, J.H. (2000): A trans-membrane guanylylcyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in Caenorhabditis elegans. Genetics, 155: 85-104BirnbyDALinkEMVowelsJJTianHColacurcioPLThomasJH2000A trans-membrane guanylylcyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in Caenorhabditis elegansGenetics1558510410.1093/genetics/155.1.85146107410790386Search in Google Scholar

Bowman, D.D., Oaks, J.A., Grieve, R.B. (1993): Ultrastructure of the infective-stage larva of Toxocara canis (Nematoda: Ascaridoidea). J. Helminthol. Soc. Wash., 60:183-204BowmanDDOaksJAGrieveRB1993Ultrastructure of the infective-stage larva of Toxocara canis (Nematoda: Ascaridoidea)J. Helminthol. Soc. Wash60183204Search in Google Scholar

Bruschi, F., Dupouy-Camet, J. (2014): Trichinellosis. In Bruschi, F. (Ed) Helminth infections and their impact on global public health. Springer-Verlag Wien. pp. 229 – 273. DOI 10.1007/978-3-7091-1782-8 8BruschiFDupouy-CametJ2014TrichinellosisBruschiFHelminth infections and their impact on global public healthSpringer-VerlagWien229273DOI 10.1007/978-3-7091-1782-88Open DOISearch in Google Scholar

Buchmeier, N.A., Heffron, F. (1990): Induction of Salmonella stress proteins upon infection of macrophages. Science, 248:730 – 732. DOI: 10.1126/science. 1970672BuchmeierNAHeffronF1990Induction of Salmonella stress proteins upon infection of macrophagesScience24873073210.1126/science. 1970672Open DOISearch in Google Scholar

Campbell, W.C., Blair, L.S. (1975): Failure to confirm reported lethal effect of cytotoxic drugs on encapsulated Trichinella spiralis larvae in mice. J. Parasitol., 61:1116 – 1117CampbellWCBlairLS1975Failure to confirm reported lethal effect of cytotoxic drugs on encapsulated Trichinella spiralis larvae in miceJ. Parasitol611116111710.2307/3279393Search in Google Scholar

de Cárcer, G., do Carmoavides, M., Lallena, M.J., Glover, D.M., GonzÁlez, C. (2001): Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability. EMBO J., 20: 2878-2884de CárcerGdo CarmoavidesMLallenaMJGloverDMGonzÁlezC2001Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stabilityEMBO J202878288410.1093/emboj/20.11.287812547411387220Search in Google Scholar

Despommier, D.D., Campbell, W.C., Blair, L.S. (1977): The in vivo and in vitro analysis of immunity to Trichinella spiralis in mice and rats. Parasitology, 74(1):109 – 119DespommierDDCampbellWCBlairLS1977The in vivo and in vitro analysis of immunity to Trichinella spiralis in mice and ratsParasitology74110911910.1017/S0031182000047570Search in Google Scholar

Devaney, E. (2006): Thermoregulation in the life cycle of nematodes. Int. J. Parasitol., 36: 641 – 649. DOI: 10.1016/j.ijpa-ra.2006.02.006DevaneyE2006Thermoregulation in the life cycle of nematodesInt. J. Parasitol3664164910.1016/j.ijpa-ra.2006.02.006Open DOISearch in Google Scholar

Devaney, E., O’neill, K., Harnett, W., Whitesell, L., Kinnaird, J.H. (2005): Hsp90 is essential in the filarial nematode Brugia pahangi. Int. J. Parasitol., 35: 627-636. DOI: 10.1016/j.ijpara.2005.01.007DevaneyEO’neillKHarnettWWhitesellLKinnairdJH2005Hsp90 is essential in the filarial nematode Brugia pahangiInt. J. Parasitol3562763610.1016/j.ijpara.2005.01.00715862576Open DOISearch in Google Scholar

Dunn, I.J., Wright, K.A. (1985): Cell injury caused by Trichinella spiralis in the mucosal epithelium of B10 A mice. J. Parasitol., 71: 757 – 766DunnIJWrightKA1985Cell injury caused by Trichinella spiralis in the mucosal epithelium of B10 A miceJ. Parasitol7175776610.2307/3281709Search in Google Scholar

Gottstein, B., Pozio, E., Nöckler, K. (2009): Epidemiology, diagnosis, treatment, and control of trichinellosis. Clin. Microbiol. Rev., 22: 127-145. DOI: 10.1128/CMR.00026-08GottsteinBPozioENöcklerK2009Epidemiology, diagnosis, treatment, and control of trichinellosisClin. Microbiol. Rev2212714510.1128/CMR.00026-08262063519136437Open DOISearch in Google Scholar

Grenert, J.P., Sullivan, W.P., Fadden, P., Haystead, T.A., Clark, J., Mimnaugh E., Krutzsch, H., Ochel, H.J., Schulte, T.W., Sausville, E., Neckers, L.M., Toft, D.O. (1997): The ami no-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. The J. Biol. Chem., 272: 23843-23850. DOI: 10.1074/jbc.272.38.23843GrenertJPSullivanWPFaddenPHaysteadTAClarkJMimnaughEKrutzschHOchelHJSchulteTWSausvilleENeckersLMToftDO1997The ami no-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformationThe J. Biol. Chem272238432385010.1074/jbc.272.38.238439295332Open DOISearch in Google Scholar

Lechler, P., Wu, X., Bernhardt, W., Campean, V., Gastiger, S., Hackenbeck, T., Klanke, B., Weidemann, A., Warnecke, C., Amann, K., Engehausen, D., Willam, C., Eckardt, K.U., Rödel, F., Wiesen-er, M.S. (2007): The tumor gene survivin is highly expressed in adult renal tubular cells: implications for a pathophysiological role in the kidney. Am. J. Pathol., 171: 1483 – 1498. DOI: 10.2353/ ajpath.2007.070132LechlerPWuXBernhardtWCampeanVGastigerSHackenbeckTKlankeBWeidemannAWarneckeCAmannKEngehausenDWillamCEckardtKURödelFWiesenerMS2007The tumor gene survivin is highly expressed in adult renal tubular cells: implications for a pathophysiological role in the kidneyAm. J. Pathol1711483149810.2353/ ajpath.2007.070132Open DOISearch in Google Scholar

Martinez, J., Perez-Serrano, J., Bernadina, W.E., Rodriguez-Caabei-ro, F. (2002): Expression of Hsp90, Hsp70 and Hsp60 in Trichinella species exposed to oxidative shock. J. Helminthol., 76: 217 – 223. DOI: 10.1079/JOH2002127MartinezJPerez-SerranoJBernadinaWERodriguez-CaabeiroF2002Expression of Hsp90, Hsp70 and Hsp60 in Trichinella species exposed to oxidative shockJ. Helminthol7621722310.1079/JOH200212712363374Open DOISearch in Google Scholar

Martinez, J., Perez-Serrano, J., Bernadina, W.E., Rincon, I., Rodri-guez-Caabeiro, F. (2004): Heat shock protein synthesis over time in infective Trichinella spiralis larvae raised in suboptimal culture conditions. J. Helminthol., 78: 243-247. DOI: 10.1079/JOH2003225MartinezJPerez-SerranoJBernadinaWERinconIRodriguez-CaabeiroF2004Heat shock protein synthesis over time in infective Trichinella spiralis larvae raised in suboptimal culture conditionsJ. Helminthol7824324710.1079/JOH2003225Open DOISearch in Google Scholar

Mollenhauer, H.H. (1964): Plastic embedding mixtures for use in electron microscopy. Stain Technol., 39:111 – 114MollenhauerHH1964Plastic embedding mixtures for use in electron microscopyStain Technol39111114Search in Google Scholar

Morimoto, R.I. (1998): Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev., 12: 3788-3796. DOI: 10.1101/gad.12.24.3788MorimotoRI1998Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulatorsGenes Dev123788379610.1101/gad.12.24.37889869631Open DOISearch in Google Scholar

Neckers, L., Neckers, K. (2002): Heat-shock protein 90 inhibitors as novel cancer chemotherapeutic agents. Expert Opin. Emerg. Drugs, 7: 277-288. DOI: 10.1517/14728214.7.2.277NeckersLNeckersK2002Heat-shock protein 90 inhibitors as novel cancer chemotherapeutic agentsExpert Opin. Emerg. Drugs727728810.1517/14728214.7.2.27715989551Open DOISearch in Google Scholar

Ozeretskovskaia, N.N., Sergiev, V.P. (1994): The specific and biological actions of chemical preparations and their combination with pathogenic agents in trichinosis. Med. Parazitol., 4: 9 – 14OzeretskovskaiaNNSergievVP1994The specific and biological actions of chemical preparations and their combination with pathogenic agents in trichinosisMed. Parazitol4914Search in Google Scholar

Roberts, L.S., Janovy, J., Nadler, S. (2013): Nematodes: Trichinellida and Dioctophymatida, Enoplean Parasites. In: Schmidt G.D. & Roberts L.S.’s Foundations of Parasitology. 9th edition. McGraw-Hill, New York, USA. pp. 381 – 388RobertsLSJanovyJNadlerS2013Nematodes: Trichinel-lida and Dioctophymatida, Enoplean ParasitesSchmidtGDRobertsLSFoundations of Parasitology9th editionMcGraw-HillNew York, USA381388Search in Google Scholar

Sacchi, L., Corona, S., Gajadhar,A.A., Pozio, E. (2001): Ultrastructural characteristics of nurse cell- larva complex of four species of Trichinella in several hosts. Parasite, 8(Suppl): S54 – S58. DOI: 10.1051/parasite/200108s2054SacchiLCoronaSGajadharAAPozioE2001Ultrastruc-tural characteristics of nurse cell- larva complex of four species of Trichinella in several hostsParasite8S54S5810.1051/parasite/200108s205411484383Open DOISearch in Google Scholar

Salem, S.A., El-Kowrany, S.I., Ismail, H.I., El-Sheikh, T.F. (2001): Study on the possible role of heat shock proteins in host resistance to Trichinella spiralis infection in experimental animals. J. Egypt. Soc. Parasitol., 31:133-144SalemSAEl-KowranySIIsmailHIEl-SheikhTF2001Study on the possible role of heat shock proteins in host resistance to Trichinella spiralis infection in experimental animalsJ. Egypt. Soc. Parasitol31133144Search in Google Scholar

Selkirk, M.E., Denham, D.A., Partono, F., Maizels, R.M. (1989): Heat shock cognate 70 is a prominent immunogen in Brugian filariasis. J. Immunol., 143: 299-308SelkirkMEDenhamDAPartonoFMaizelsRM1989Heat shock cognate 70 is a prominent immunogen in Brugian filariasisJ. Immunol14329930810.4049/jimmunol.143.1.299Search in Google Scholar

Shalaby H.A., Abdel-Shafy S., Abdel-Rahman K.A., Derbala A.A. (2009): Comparative in vitro effect of artemether and albendazole on adult Toxocara canis. Parasitol. Res., 105, 967 – 976. DOI: 10.1007/s00436-009-1479-9.ShalabyHAAbdel-ShafySAbdel-RahmanKADerbalaAA2009Comparative in vitro effect of artemether and albendazole on adult Toxocara canisParasitol. Res10596797610.1007/s00436-009-1479-919468753Open DOISearch in Google Scholar

Shoheib, Z.S., Shamloula, M.M., Abdin, A.A., El-Segai, O. (2006): Role of α-chemotrypsin and colchicine as adjuvant therapy in experimental muscular trichinellosis: Parasitological, biochemical, and immunohistochemical study. Egypt. J. Med. Microbiol., 15: 773-789ShoheibZSShamloulaMMAbdinAAEl-SegaiO2006Role of α-chemotrypsin and colchicine as adjuvant therapy in experimental muscular trichinellosis: Parasitological, biochemical, and immunohistochemical studyEgypt. J. Med. Microbiol15773789Search in Google Scholar

Tatokoro, M., Koga, F., Yoshida, S., Kihara, K. (2015): Heat shock protein 90 targeting therapy: state of the art and future perspective. EXCLIJ., 14: 48-58. DOI: 10.17179/excli2015-586TatokoroMKogaFYoshidaSKiharaK2015Heat shock protein 90 targeting therapy: state of the art and future perspectiveEXCLIJ14485810.17179/excli2015-586465263626600741Open DOISearch in Google Scholar

Wakelin, D., Lloyed, M. (1976): Immunity to primary and challenge infection of Trichinella spiralis in mice, a re- examination of conventional parameters. Parasitology, 71: 173 – 182. DOI: http://dx.doi.org/10.1017/S0031182000048472WakelinDLloyedM1976Immunity to primary and challenge infection of Trichinella spiralis in mice, a re- examination of conventional parametersParasitology7117318210.1017/S00311820000484721264489Open DOISearch in Google Scholar

Whitesell, L., Sutphin, P.D., Pulcini, E.J., Martinez, J.D., Cook, P.H. (1998): The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol., 18: 1517 – 1524.DOI: 10.1128/MCB. 18.3.1517WhitesellLSutphinPDPulciniEJMartinezJDCookPH1998The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agentMol. Cell. Biol1815171524DOI: 10.1128/MCB.18.3.1517Open DOISearch in Google Scholar

Zügel, U., Kaufmann, S.H. (1999): Role of heat shock proteins in protection from and pathogenesis of infectious diseases. Clin. Microbiol. Rev., 12:19-39ZügelUKaufmannSH1999Role of heat shock proteins in protection from and pathogenesis of infectious diseasesClin. Microbiol. Rev12193910.1128/CMR.12.1.19889059880473Search in Google Scholar

Yang, Y., Qin, W., Zarlenga, D., Cao, L., Tian, G. (2013): TsDAF-21/ Hsp90 is expressed in all examined stages of Trichinella spiralis. Vet. Parasitol., 194:171-174. DOI: 10.1016/j.vetpar.2013.01.048.YangYQinWZarlengaDCaoLTianG2013TsDAF-21/ Hsp90 is expressed in all examined stages of Trichinella spiralisVet. Parasitol19417117410.1016/j.vetpar.2013.01.04823465439Open DOISearch in Google Scholar

Yang, Y., Qin, W., Qiu, H., Liu, Y. (2014): Characterization of Ts-DAF-21/HSP90 protein from the parasitic nematode Trichinella spiralis. Parasitol. Res., 113: 2209-2217. DOI: 10.1007/s00436-014-3874-0YangYQinWQiuHLiuY2014Characterization of Ts-DAF-21/HSP90 protein from the parasitic nematode Trichinella spiralisParasitol. Res1132209221710.1007/s00436-014-3874-024710664Open DOISearch in Google Scholar

eISSN:
1336-9083
ISSN:
0440-6605
Idioma:
Inglés
Calendario de la edición:
4 veces al año
Temas de la revista:
Life Sciences, Zoology, Ecology, other, Medicine, Clinical Medicine, Microbiology, Virology and Infection Epidemiology