pubmed-article:15247299 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15247299 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
pubmed-article:15247299 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
pubmed-article:15247299 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:15247299 | lifeskim:mentions | umls-concept:C0074129 | lld:lifeskim |
pubmed-article:15247299 | lifeskim:mentions | umls-concept:C0061187 | lld:lifeskim |
pubmed-article:15247299 | lifeskim:mentions | umls-concept:C0078238 | lld:lifeskim |
pubmed-article:15247299 | lifeskim:mentions | umls-concept:C1422473 | lld:lifeskim |
pubmed-article:15247299 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:15247299 | pubmed:issue | 38 | lld:pubmed |
pubmed-article:15247299 | pubmed:dateCreated | 2004-9-13 | lld:pubmed |
pubmed-article:15247299 | pubmed:abstractText | The scavenger receptor expressed by endothelial cells (SREC) was isolated from a human endothelial cell line and consists of two isoforms named SREC-I and -II. Both isoforms have no significant homology to other types of scavenger receptors. They contain 10 repeats of epidermal growth factor-like cysteine-rich motifs in the extracellular domains and have unusually long C-terminal cytoplasmic domains with Ser/Pro-rich regions. The extracellular domain of SREC-I binds modified low density lipoprotein and mediates a homophilic SREC-I/SREC-I or heterophilic SREC-I/SREC-II trans-interaction. However, the significance of large Ser/Pro-rich cytoplasmic domains of SRECs is not clear. Here, we found that when SREC-I was overexpressed in murine fibroblastic L cells, neurite-like outgrowth was induced, indicating that the receptor can lead to changes in cell morphology. The SREC-I-mediated morphological change required the cytoplasmic domain of the protein, and we identified advillin, a member of the gelsolin/villin family of actin regulatory proteins, as a protein binding to this domain. Reduction of advillin expression in L cells by RNAi led to the absence of the described SREC-I-induced morphological changes, indicating that advillin is a prerequisite for the change. Finally, we demonstrated that SREC-I and advillin were co-expressed and interacted with each other in dorsal root ganglion neurons during embryonic development and that overexpression of both SREC-I and advillin in cultured Neuro-2a cells induced long process formation. These results suggest that the interaction of SREC-I and advillin are involved in the development of dorsal root ganglion neurons by inducing the described morphological changes. | lld:pubmed |
pubmed-article:15247299 | pubmed:language | eng | lld:pubmed |
pubmed-article:15247299 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15247299 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15247299 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15247299 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15247299 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15247299 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15247299 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15247299 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15247299 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15247299 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15247299 | pubmed:month | Sep | lld:pubmed |
pubmed-article:15247299 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:15247299 | pubmed:author | pubmed-author:AraiHiroyukiH | lld:pubmed |
pubmed-article:15247299 | pubmed:author | pubmed-author:TsujimotoMasa... | lld:pubmed |
pubmed-article:15247299 | pubmed:author | pubmed-author:TakioKojiK | lld:pubmed |
pubmed-article:15247299 | pubmed:author | pubmed-author:DohmaeNaoshiN | lld:pubmed |
pubmed-article:15247299 | pubmed:author | pubmed-author:AdachiHidekiH | lld:pubmed |
pubmed-article:15247299 | pubmed:author | pubmed-author:KoizumiHiroyu... | lld:pubmed |
pubmed-article:15247299 | pubmed:author | pubmed-author:IshiiJunkoJ | lld:pubmed |
pubmed-article:15247299 | pubmed:author | pubmed-author:ShibataMamiM | lld:pubmed |
pubmed-article:15247299 | pubmed:author | pubmed-author:ShibataNorihi... | lld:pubmed |
pubmed-article:15247299 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15247299 | pubmed:day | 17 | lld:pubmed |
pubmed-article:15247299 | pubmed:volume | 279 | lld:pubmed |
pubmed-article:15247299 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15247299 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15247299 | pubmed:pagination | 40084-90 | lld:pubmed |
pubmed-article:15247299 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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pubmed-article:15247299 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15247299 | pubmed:articleTitle | Type F scavenger receptor SREC-I interacts with advillin, a member of the gelsolin/villin family, and induces neurite-like outgrowth. | lld:pubmed |
pubmed-article:15247299 | pubmed:affiliation | Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. | lld:pubmed |
pubmed-article:15247299 | pubmed:publicationType | Journal Article | lld:pubmed |
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