pubmed-article:21402050 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21402050 | lifeskim:mentions | umls-concept:C0147139 | lld:lifeskim |
pubmed-article:21402050 | lifeskim:mentions | umls-concept:C0678222 | lld:lifeskim |
pubmed-article:21402050 | lifeskim:mentions | umls-concept:C1518174 | lld:lifeskim |
pubmed-article:21402050 | lifeskim:mentions | umls-concept:C0007577 | lld:lifeskim |
pubmed-article:21402050 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:21402050 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:21402050 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
pubmed-article:21402050 | lifeskim:mentions | umls-concept:C0600210 | lld:lifeskim |
pubmed-article:21402050 | lifeskim:mentions | umls-concept:C1533157 | lld:lifeskim |
pubmed-article:21402050 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:21402050 | pubmed:dateCreated | 2011-4-22 | lld:pubmed |
pubmed-article:21402050 | pubmed:abstractText | Secreted frizzled-related protein (sFRP)-1 is a Wnt antagonist that inhibits breast carcinoma cell motility, whereas the secreted glycoprotein thrombospondin-1 stimulates adhesion and motility of the same cells. We examined whether thrombospondin-1 and sFRP-1 interact directly or indirectly to modulate cell behavior. Thrombospondin-1 bound sFRP-1 with an apparent K(d)=48nM and the related sFRP-2 with a K(d)=95nM. Thrombospondin-1 did not bind to the more distantly related sFRP-3. The association of thrombospondin-1 and sFRP-1 is primarily mediated by the amino-terminal N-module of thrombospondin-1 and the netrin domain of sFRP-1. sFRP-1 inhibited ?3?1 integrin-mediated adhesion of MDA-MB-231 breast carcinoma cells to a surface coated with thrombospondin-1 or recombinant N-module, but not adhesion of the cells on immobilized fibronectin or type I collagen. sFRP-1 also inhibited thrombospondin-1-mediated migration of MDA-MB-231 and MDA-MB-468 breast carcinoma cells. Although sFRP-2 binds similarly to thrombospondin-1, it did not inhibit thrombospondin-1-stimulated adhesion. Thus, sFRP-1 binds to thrombospondin-1 and antagonizes stimulatory effects of thrombospondin-1 on breast carcinoma cell adhesion and motility. These results demonstrate that sFRP-1 can modulate breast cancer cell responses by interacting with thrombospondin-1 in addition to its known effects on Wnt signaling. | lld:pubmed |
pubmed-article:21402050 | pubmed:language | eng | lld:pubmed |
pubmed-article:21402050 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21402050 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:21402050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21402050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21402050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21402050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21402050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21402050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21402050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21402050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21402050 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21402050 | pubmed:month | May | lld:pubmed |
pubmed-article:21402050 | pubmed:issn | 1096-0384 | lld:pubmed |
pubmed-article:21402050 | pubmed:author | pubmed-author:RubinJeffrey... | lld:pubmed |
pubmed-article:21402050 | pubmed:author | pubmed-author:RobertsDavid... | lld:pubmed |
pubmed-article:21402050 | pubmed:author | pubmed-author:CalzadaMaria... | lld:pubmed |
pubmed-article:21402050 | pubmed:author | pubmed-author:SipesJohn MJM | lld:pubmed |
pubmed-article:21402050 | pubmed:author | pubmed-author:ChumanYoshiro... | lld:pubmed |
pubmed-article:21402050 | pubmed:author | pubmed-author:WolfVladimirV | lld:pubmed |
pubmed-article:21402050 | pubmed:author | pubmed-author:KuznetsovaSve... | lld:pubmed |
pubmed-article:21402050 | pubmed:author | pubmed-author:Martin-MansoG... | lld:pubmed |
pubmed-article:21402050 | pubmed:author | pubmed-author:XavierCharles... | lld:pubmed |
pubmed-article:21402050 | pubmed:copyrightInfo | Published by Elsevier Inc. | lld:pubmed |
pubmed-article:21402050 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21402050 | pubmed:day | 15 | lld:pubmed |
pubmed-article:21402050 | pubmed:volume | 509 | lld:pubmed |
pubmed-article:21402050 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21402050 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21402050 | pubmed:pagination | 147-56 | lld:pubmed |
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pubmed-article:21402050 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:21402050 | pubmed:articleTitle | sFRP-1 binds via its netrin-related motif to the N-module of thrombospondin-1 and blocks thrombospondin-1 stimulation of MDA-MB-231 breast carcinoma cell adhesion and migration. | lld:pubmed |
pubmed-article:21402050 | pubmed:affiliation | Laboratory of Pathology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. mansog@mail.nih.gov | lld:pubmed |
pubmed-article:21402050 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:21402050 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:21402050 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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