| pubmed-article:9699674 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9699674 | lifeskim:mentions | umls-concept:C1704826 | lld:lifeskim |
| pubmed-article:9699674 | lifeskim:mentions | umls-concept:C0080125 | lld:lifeskim |
| pubmed-article:9699674 | lifeskim:mentions | umls-concept:C1156237 | lld:lifeskim |
| pubmed-article:9699674 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:9699674 | pubmed:dateCreated | 1998-8-27 | lld:pubmed |
| pubmed-article:9699674 | pubmed:abstractText | The epidermal growth factor-like receptor tyrosine kinase (ErbB) family is frequently overexpressed in a variety of human carcinomas, including breast cancer. To assist in characterizing the role of ErbB-4 in breast cancer, we generated three specific hammerhead ribozymes targeted to the ErbB-4 mRNA. These ribozymes, Rz6, Rz21, and Rz29, efficiently catalyzed the specific cleavage of ErbB-4 message in a cell-free system. We demonstrated that the neuregulin-induced mitogenic effect was abolished in ribozyme Rz29- and Rz6-transfected 32D/ErbB-4 cells. Inhibition of mitogenesis was characterized by ribozyme-mediated down-regulation of ErbB-4 expression. In addition, we provide the first evidence that different threshold levels of ErbB-4 expression and activation correlate with different responses to neuregulin stimulation. High levels of ErbB-4 expression, phosphorylation, and homodimerization are necessary for neuregulin-stimulated, interleukin 3-independent cell proliferation in the 32D/E4 cells. In the case of Rz29-transfected 32D/E4 cells, low levels of ErbB-4 expression allowed neuregulin-induced phosphorylation but were insufficient to couple the activated receptor to cellular signaling. Furthermore, expression of the functional ErbB-4 ribozyme in T47D human breast carcinoma cells led to a down-regulation of endogenous ErbB-4 expression and a reduction of anchorage-independent colony formation. These studies support the use of ErbB-4 ribozymes to define the role of ErbB-4 receptors in human cancers. | lld:pubmed |
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| pubmed-article:9699674 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9699674 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699674 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9699674 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699674 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9699674 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699674 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9699674 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9699674 | pubmed:issn | 0008-5472 | lld:pubmed |
| pubmed-article:9699674 | pubmed:author | pubmed-author:LippmanM EME | lld:pubmed |
| pubmed-article:9699674 | pubmed:author | pubmed-author:GoldsteinD... | lld:pubmed |
| pubmed-article:9699674 | pubmed:author | pubmed-author:PayneJJ | lld:pubmed |
| pubmed-article:9699674 | pubmed:author | pubmed-author:TangC KCK | lld:pubmed |
| pubmed-article:9699674 | pubmed:author | pubmed-author:WangL MLM | lld:pubmed |
| pubmed-article:9699674 | pubmed:author | pubmed-author:PierceJ HJH | lld:pubmed |
| pubmed-article:9699674 | pubmed:author | pubmed-author:CzubaykoFF | lld:pubmed |
| pubmed-article:9699674 | pubmed:author | pubmed-author:AlimandiMM | lld:pubmed |
| pubmed-article:9699674 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9699674 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9699674 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:9699674 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9699674 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9699674 | pubmed:pagination | 3415-22 | lld:pubmed |
| pubmed-article:9699674 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:9699674 | pubmed:meshHeading | pubmed-meshheading:9699674-... | lld:pubmed |
| pubmed-article:9699674 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9699674 | pubmed:articleTitle | ErbB-4 ribozymes abolish neuregulin-induced mitogenesis. | lld:pubmed |
| pubmed-article:9699674 | pubmed:affiliation | Department of Biochemistry, Georgetown University Medical Center, Washington, DC 20007-2197, USA. Tangc@gunet.georgetown.edu | lld:pubmed |
| pubmed-article:9699674 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9699674 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9699674 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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