| pubmed-article:17032310 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17032310 | lifeskim:mentions | umls-concept:C1515657 | lld:lifeskim |
| pubmed-article:17032310 | lifeskim:mentions | umls-concept:C0035541 | lld:lifeskim |
| pubmed-article:17032310 | lifeskim:mentions | umls-concept:C0380603 | lld:lifeskim |
| pubmed-article:17032310 | lifeskim:mentions | umls-concept:C0596087 | lld:lifeskim |
| pubmed-article:17032310 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:17032310 | lifeskim:mentions | umls-concept:C0162768 | lld:lifeskim |
| pubmed-article:17032310 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:17032310 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:17032310 | pubmed:dateCreated | 2006-11-2 | lld:pubmed |
| pubmed-article:17032310 | pubmed:abstractText | It is thought that the export of angiogenic fibroblast growth factors (FGF) from tumors may be involved in the onset of tumor angiogenesis. To create a new active targeting drug that inhibits the tumor angiogenic process without toxicities to normal cells, human basic FGF (h-bFGF) was inserted genetically into the Gly89 position of cross-linked RNase1 (the ribonuclease inhibitor protein [RI] binding site of cross-linked human pancreatic RNase) to prevent stereospecific binding to RI. The resultant insertional-fusion protein (CL-RFN89) was active both as h-bFGF and as RNase1. Furthermore, it acquired an additional ability of evading RI through steric blockade of RI binding caused by the fused h-bFGF domain. In the present study, the effect of the resultant protein, CL-RFN89, on the antitumor response though its antiangiogenic properties was investigated in an in vivo model. Continuous systemic treatment with CL-RFN89 significantly inhibited the growth of human A431 squamous cell carcinomas in vivo. Seven days of treatment with CL-RFN89 resulted in a 58.2% inhibition of tumor growth compared with control mice (P < 0.0001). Furthermore, immunohistochemistry using a rat antimouse CD31 antibody showed that treatment with CL-RFN89 reduced tumor vascularization. These findings identify CL-RFN89 as a potent systemic inhibitor of tumor growth as a result of its antiangiogenic properties. This protein appears to be a new systemic antitumor agent. | lld:pubmed |
| pubmed-article:17032310 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17032310 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17032310 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17032310 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17032310 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17032310 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17032310 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17032310 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17032310 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17032310 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17032310 | pubmed:issn | 1347-9032 | lld:pubmed |
| pubmed-article:17032310 | pubmed:author | pubmed-author:AiuraKoichiK | lld:pubmed |
| pubmed-article:17032310 | pubmed:author | pubmed-author:KitajimaMasak... | lld:pubmed |
| pubmed-article:17032310 | pubmed:author | pubmed-author:TadaHirokoH | lld:pubmed |
| pubmed-article:17032310 | pubmed:author | pubmed-author:UedaMasakazuM | lld:pubmed |
| pubmed-article:17032310 | pubmed:author | pubmed-author:YamadaHidenor... | lld:pubmed |
| pubmed-article:17032310 | pubmed:author | pubmed-author:SenoMasaharuM | lld:pubmed |
| pubmed-article:17032310 | pubmed:author | pubmed-author:JinnoHiromits... | lld:pubmed |
| pubmed-article:17032310 | pubmed:author | pubmed-author:YagiHiroshiH | lld:pubmed |
| pubmed-article:17032310 | pubmed:author | pubmed-author:MikamiShujiS | lld:pubmed |
| pubmed-article:17032310 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17032310 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:17032310 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17032310 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17032310 | pubmed:pagination | 1315-20 | lld:pubmed |
| pubmed-article:17032310 | pubmed:meshHeading | pubmed-meshheading:17032310... | lld:pubmed |
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| pubmed-article:17032310 | pubmed:meshHeading | pubmed-meshheading:17032310... | lld:pubmed |
| pubmed-article:17032310 | pubmed:meshHeading | pubmed-meshheading:17032310... | lld:pubmed |
| pubmed-article:17032310 | pubmed:meshHeading | pubmed-meshheading:17032310... | lld:pubmed |
| pubmed-article:17032310 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17032310 | pubmed:articleTitle | Anti-tumor effect in an in vivo model by human-derived pancreatic RNase with basic fibroblast growth factor insertional fusion protein through antiangiogenic properties. | lld:pubmed |
| pubmed-article:17032310 | pubmed:affiliation | Department of Surgery, Keio University School of Medicine, Tokyo, Japan. | lld:pubmed |
| pubmed-article:17032310 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17032310 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17032310 | lld:pubmed |
