pubmed-article:9733802 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9733802 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:9733802 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
pubmed-article:9733802 | lifeskim:mentions | umls-concept:C0086194 | lld:lifeskim |
pubmed-article:9733802 | lifeskim:mentions | umls-concept:C0065054 | lld:lifeskim |
pubmed-article:9733802 | lifeskim:mentions | umls-concept:C0072010 | lld:lifeskim |
pubmed-article:9733802 | lifeskim:mentions | umls-concept:C1707310 | lld:lifeskim |
pubmed-article:9733802 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:9733802 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:9733802 | lifeskim:mentions | umls-concept:C0524676 | lld:lifeskim |
pubmed-article:9733802 | pubmed:issue | 38 | lld:pubmed |
pubmed-article:9733802 | pubmed:dateCreated | 1998-10-15 | lld:pubmed |
pubmed-article:9733802 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9733802 | pubmed:abstractText | Coelomic fluid of Eisenia foetida earthworms contains a 42-kDa protein named coelomic cytolytic factor 1 (CCF-1) that was described previously to be involved in cytolytic, opsonizing, and hemolytic properties of the coelomic fluid. Cloning and sequencing of CCF-1 reveal significant homology with the putative catalytic region of beta-1,3- and beta-1,3-1,4-glucanases. CCF-1 also displays homology with coagulation factor G from Limulus polyphemus and with Gram-negative bacteria-binding protein of Bombyx mori silkworm, two proteins involved in invertebrate defense mechanisms. We show that CCF-1 efficiently binds both beta-1,3-glucan and lipopolysaccharide. Moreover, CCF-1 participates in the activation of prophenoloxidase cascade via recognition of yeast and Gram-negative bacteria cell wall components. These results suggest that the 42-kDa CCF-1 protein of E. foetida coelomic fluid likely plays a role in the protection of earthworms against microbes. | lld:pubmed |
pubmed-article:9733802 | pubmed:language | eng | lld:pubmed |
pubmed-article:9733802 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9733802 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9733802 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9733802 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9733802 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9733802 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9733802 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9733802 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9733802 | pubmed:month | Sep | lld:pubmed |
pubmed-article:9733802 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:GomezJJ | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:De... | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:Van DyckEE | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:BrykDD | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:TimmermansMM | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:TheilGG | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:BiletSS | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:BeschinAA | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:RevettKK | lld:pubmed |
pubmed-article:9733802 | pubmed:author | pubmed-author:RaymakersJJ | lld:pubmed |
pubmed-article:9733802 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9733802 | pubmed:day | 18 | lld:pubmed |
pubmed-article:9733802 | pubmed:volume | 273 | lld:pubmed |
pubmed-article:9733802 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9733802 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9733802 | pubmed:pagination | 24948-54 | lld:pubmed |
pubmed-article:9733802 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:9733802 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9733802 | pubmed:articleTitle | Identification and cloning of a glucan- and lipopolysaccharide-binding protein from Eisenia foetida earthworm involved in the activation of prophenoloxidase cascade. | lld:pubmed |
pubmed-article:9733802 | pubmed:affiliation | Unit of Cellular Immunology, Flemish Interuniversity Institute for Biotechnology, VIB-VUB, Paardenstraat 65, B-1640 St-Genesius-Rode, Belgium. abeschin@vub.ac.be | lld:pubmed |
pubmed-article:9733802 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9733802 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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