Source:http://linkedlifedata.com/resource/pubmed/id/17845804
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2007-12-24
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pubmed:databankReference | |
pubmed:abstractText |
Members of the transforming growth factor-beta/bone morphogenetic protein (TGF-beta/BMP) family of cytokines play crucial roles in animal development and are candidate molecules for host-parasite cross-communication in helminth diseases. TGF-beta/BMP-signalling involves binding of the cytokines to receptor kinases which subsequently activate intracellular transcription factors of the Smad family. We have previously characterized two members of the receptor-regulated Smad (R-Smad) family, EmSmadA and EmSmadB, from the human parasitic cestode Echinococcus multilocularis and now present evidence for two additional Smads that are expressed by the larval stages of the parasite. The full-length cDNAs coding for a third R-Smad, EmSmadC, and a common mediator Smad (Co-Smad), EmSmadD, were characterized. While EmSmadD displayed a typical Co-Smad structure, EmSmadC lacked the N-terminal MH1 domain which is typically found in Smads. In yeast two-hybrid analyses, EmSmadC and EmSmadD were capable of homo- and heterodimer formation with other Echinococcus Smads. Furthermore, EmSmadC displayed autonomous transcription activation activity and interacted with EmSkip, a member of the SNW/SKIP family of transcriptional regulators. In a heterologous expression system, EmSmadC was specifically phosphorylated by mammalian TGF-beta receptors, indicating that it is a member of the AR-Smad sub-family. Finally, in activity assays, the parasite's Erk-like kinase EmMPK1 phosphorylated EmSmadD, indicating cross-regulation between mitogen-activated protein kinase cascade- and TGF-beta/BMP-signalling in Echinococcus. The data presented herein significantly broaden our knowledge of Smad-signalling factors in E. multilocularis and will facilitate studies on TGF-beta/BMP-regulated genes in the parasite as well as TGF-beta/BMP mediated host-parasite cross-interaction during alveolar echinococcosis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0020-7519
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
161-76
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pubmed:meshHeading |
pubmed-meshheading:17845804-Amino Acid Sequence,
pubmed-meshheading:17845804-Animals,
pubmed-meshheading:17845804-Base Sequence,
pubmed-meshheading:17845804-Bone Morphogenetic Proteins,
pubmed-meshheading:17845804-Cloning, Molecular,
pubmed-meshheading:17845804-Echinococcosis,
pubmed-meshheading:17845804-Echinococcus multilocularis,
pubmed-meshheading:17845804-Genes, Helminth,
pubmed-meshheading:17845804-Host-Parasite Interactions,
pubmed-meshheading:17845804-Humans,
pubmed-meshheading:17845804-Larva,
pubmed-meshheading:17845804-Molecular Sequence Data,
pubmed-meshheading:17845804-Protein Structure, Tertiary,
pubmed-meshheading:17845804-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:17845804-Sequence Alignment,
pubmed-meshheading:17845804-Smad Proteins,
pubmed-meshheading:17845804-Smad4 Protein,
pubmed-meshheading:17845804-Transforming Growth Factor beta,
pubmed-meshheading:17845804-Two-Hybrid System Techniques
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pubmed:year |
2008
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pubmed:articleTitle |
Molecular characterisation of a second structurally unusual AR-Smad without an MH1 domain and a Smad4 orthologue from Echinococcus multilocularis.
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pubmed:affiliation |
University of Würzburg, Institute of Hygiene and Microbiology, Josef-Schneider-Strasse 2, D-97080 Würzburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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