Source:http://linkedlifedata.com/resource/pubmed/id/15247299
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
38
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| pubmed:dateCreated |
2004-9-13
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| 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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Avil protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Gelsolin,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Scavenger,
http://linkedlifedata.com/resource/pubmed/chemical/Scavenger Receptors, Class F
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
17
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| pubmed:volume |
279
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
40084-90
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| pubmed:dateRevised |
2005-11-17
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| pubmed:meshHeading |
pubmed-meshheading:15247299-Amino Acid Sequence,
pubmed-meshheading:15247299-Animals,
pubmed-meshheading:15247299-Cell Adhesion Molecules,
pubmed-meshheading:15247299-Cell Size,
pubmed-meshheading:15247299-Cells, Cultured,
pubmed-meshheading:15247299-Cytoplasm,
pubmed-meshheading:15247299-Ganglia, Spinal,
pubmed-meshheading:15247299-Gelsolin,
pubmed-meshheading:15247299-Mice,
pubmed-meshheading:15247299-Microfilament Proteins,
pubmed-meshheading:15247299-Molecular Sequence Data,
pubmed-meshheading:15247299-Neurites,
pubmed-meshheading:15247299-Neurons,
pubmed-meshheading:15247299-Protein Structure, Tertiary,
pubmed-meshheading:15247299-Receptors, LDL,
pubmed-meshheading:15247299-Receptors, Scavenger,
pubmed-meshheading:15247299-Scavenger Receptors, Class F,
pubmed-meshheading:15247299-Transfection
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| pubmed:year |
2004
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| pubmed:articleTitle |
Type F scavenger receptor SREC-I interacts with advillin, a member of the gelsolin/villin family, and induces neurite-like outgrowth.
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| pubmed:affiliation |
Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
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| pubmed:publicationType |
Journal Article
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