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dc.contributor.author Fuentes, Jose M.
dc.contributor.author Hesse, Matthias
dc.contributor.author Fitzpatrick, Jennifer M.
dc.contributor.author Hoffmann, Karl F.
dc.contributor.author Wynn, Thomas A.
dc.contributor.author Chalmers, Iain W.
dc.contributor.author Modolell, Manuel
dc.date.accessioned 2010-03-12T15:22:31Z
dc.date.available 2010-03-12T15:22:31Z
dc.date.issued 2010-03-12
dc.identifier.citation Fuentes , J M , Hesse , M , Fitzpatrick , J M , Hoffmann , K F , Wynn , T A , Chalmers , I W & Modolell , M 2010 , ' Schistosoma mansoni arginase shares functional similarities with human orthologs but depends upon disulphide bridges for enzymatic activity ' International Journal for Parsitology , pp. 267-279 . en
dc.identifier.other PURE: 153739
dc.identifier.other dspace: 2160/4422
dc.identifier.uri http://hdl.handle.net/2160/4422
dc.description Fitzpatrick, J. M., Fuentes, J. M., Chalmers, I. W., Wynn, T. A., Modolell, M., Hoffmann, K. F., Hesse, M. (2009). Schistosoma mansoni arginase shares functional similarities with human orthologs but depends upon disulphide bridges for enzymatic activity. International Journal for Parsitology, 39, (3), 267-279. en
dc.description.abstract Schistosome helminths constitute a major health risk for the human population in many tropical areas. We demonstrate for the first time that several developmental stages of the human parasite Schistosoma mansoni express arginase, which is responsible for the hydrolysis of l-arginine to l-ornithine and urea. Arginase activity by alternatively activated macrophages is an essential component of the mammalian host response in schistosomiasis. However, it has not been previously shown that the parasite also expresses arginase when it is in contact with the mammalian host. After cloning and sequencing the cDNA encoding the parasite enzyme, we found that many structural features of human arginase are well conserved in the parasite ortholog. Subsequently, we discovered that S. mansoni arginase shares many similar molecular, biochemical and functional properties with both human arginase isoforms. Nevertheless, our data also reveal striking differences between human and schistosome arginase. Particularly, we found evidence that schistosome arginase activity depends upon disulphide bonds by cysteines, in contrast to human arginase. In conclusion, we report that S. mansoni arginase is well adapted to the physiological conditions that exist in the human host. en
dc.format.extent 13 en
dc.language.iso eng
dc.relation.ispartof International Journal for Parsitology en
dc.title Schistosoma mansoni arginase shares functional similarities with human orthologs but depends upon disulphide bridges for enzymatic activity en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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