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dc.contributor.author Yoshino, Timothy P.
dc.contributor.author Humphries, Judith E.
dc.date.accessioned 2008-12-12T11:13:04Z
dc.date.available 2008-12-12T11:13:04Z
dc.date.issued 2005-08-01
dc.identifier.citation Yoshino , T P & Humphries , J E 2005 , ' Schistosoma mansoni excretory-secretory products stimulate a p38 signalling pathway in Biomphalaria glabrata embryonic cells ' International Journal for Parasitology , pp. 37-46 . , 10.1016/j.ijpara.2005.08.009 en
dc.identifier.other PURE: 92680
dc.identifier.other dspace: 2160/1569
dc.identifier.uri http://hdl.handle.net/2160/1569
dc.identifier.uri http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T7F-4H3Y8PM-2&_user=10&_coverDate=01%2F31%2F2006&_rdoc=5&_fmt=summary&_orig=browse&_srch=doc-info(%23toc%235057%232006%23999639998%23614642%23FLA%23display%23Volume)&_cdi=5057&_sort=d&_docanchor=& en
dc.description Judith E. Humphries, and Timothy P. Yoshino (2006). Schistosoma mansoni excretory-secretory products stimulate a p38 signalling pathway in Biomphalaria glabrata embryonic cells. International Journal for Parasitology, 36(1), 37-46. Sponsorship: NIH grant AI015503 RAE2008 en
dc.description.abstract Following infection with Schistosoma mansoni larvae, haemocytes of resistant Biomphalaria glabrata snails execute a rapid defence during which they migrate towards and encapsulate the parasites. Such immediate and precise responses are thought to depend on signal transduction cascades though the signalling components involved remain largely unknown. It is proposed that mitogen-activated protein kinases may play a role in B. glabrata immune signalling, in particular p38 mitogen-activated protein kinases, which are known to be associated with stress and inflammatory signalling. Using degenerate PCR followed by Rapid Amplification of cDNA Ends a full-length p38 mitogen-activated protein kinase-like cDNA was cloned from both the B. glabrata embryonic (Bge) cell line (Bge-p38) and haemocytes (Bgh-p38). In addition, B. glabrata p38 mitogen-activated protein kinase activation was examined at the protein level in Western blot analyses using an antibody that specifically recognises activated/diphosphorylated p38 mitogen-activated protein kinase. Results showed that Bge cell p38 mitogen-activated protein kinase was activated/phosphorylated following 30 min incubation with anisomycin, an established p38 mitogen-activated protein kinase activator. Furthermore, p38 mitogen-activated protein kinase was also activated after only 5 min exposure to either the β-glucan polymer laminarin or S. mansoni larval excretory–secretory products. In a comparative study, activated haemocyte p38 mitogen-activated protein kinase could also be detected using the anti-phosphorylated p38 antibody following cell treatment with anisomycin. However, in contrast with Bge cells, haemocyte p38 was not activated by either excretory–secretory products or laminarin treatments, suggesting fundamental differences in the role of p38 mitogen-activated protein kinase in signal transduction pathways between haemocytes and Bge cells. en
dc.format.extent 10 en
dc.language.iso eng
dc.relation.ispartof International Journal for Parasitology en
dc.title Schistosoma mansoni excretory-secretory products stimulate a p38 signalling pathway in Biomphalaria glabrata embryonic cells en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1016/j.ijpara.2005.08.009
dc.contributor.institution Aberystwyth University en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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