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dc.contributor.authorMayuri Tarasuken_US
dc.contributor.authorSuksiri Vichasri Gramsen_US
dc.contributor.authorVithoon Viyananten_US
dc.contributor.authorRudi Gramsen_US
dc.contributor.otherThammasat Universityen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-09-13T06:22:09Z-
dc.date.available2018-09-13T06:22:09Z-
dc.date.issued2009-09-01en_US
dc.identifier.citationMolecular and Biochemical Parasitology. Vol.167, No.1 (2009), 60-71en_US
dc.identifier.issn01666851en_US
dc.identifier.other2-s2.0-67650364778en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=67650364778&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/27146-
dc.description.abstractIn the present study we describe type 1 cystatin, a cysteine protease inhibitor, as a major released antigen of the tropical liver fluke Fasciola gigantica (FgStefin-1). Immunohistochemical analysis showed that FgStefin-1 is abundant in (a) tissue of tegumental type, including oral and ventral sucker, pharynx, genital atrium, metraterm, cirrus and (b) the intestinal epithelium. Faint staining was observed in the epithelia of ovary and proximal uterus. Immunoblots showed the presence of FgStefin-1 in the parasite's excretion/secretion (ES) product and immunodepletion demonstrated that FgStefin-1 herein is partially complexed with cathepsin L. Furthermore, quantitation of FgStefin-1 in comparison to cathepsin L in ES product and crude worm extract of adults supports a major external function of FgStefin-1 with an estimated 50% being released in at least equimolar amounts to cathepsin L. Sera of an experimentally infected rabbit reacted with recombinant FgStefin-1 starting 8 weeks postinfection. Activity analyses of recombinant FgStefin-1 showed nanomolar inhibition constants for mammalian cathepsin B, L, and S cysteine proteases and released cysteine proteases of the parasite. The protein is active over a wide pH range and is heat stable. Our results suggest protective functions of FgStefin-1, regulating intracellular cysteine protease activity, and possibly protection against extracellular proteolytic damage to the parasite's intestinal and tegumental surface proteins. Considering inhibition kinetics and previously demonstrated immunomodulatory properties of cystatin in parasitic nematodes a comparable function of FgStefin-1 is suggested and is at present under investigation. © 2009 Elsevier B.V. All rights reserved.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=67650364778&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleType I cystatin (stefin) is a major component of Fasciola gigantica excretion/secretion producten_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.molbiopara.2009.04.010en_US
Appears in Collections:Scopus 2006-2010

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