| pubmed-article:8833657 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8833657 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:8833657 | lifeskim:mentions | umls-concept:C1512505 | lld:lifeskim |
| pubmed-article:8833657 | lifeskim:mentions | umls-concept:C0596138 | lld:lifeskim |
| pubmed-article:8833657 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8833657 | lifeskim:mentions | umls-concept:C0021666 | lld:lifeskim |
| pubmed-article:8833657 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:8833657 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8833657 | pubmed:dateCreated | 1997-5-1 | lld:pubmed |
| pubmed-article:8833657 | pubmed:abstractText | We have investigated the autocrine regulation of insulin-like growth factor-II (IGF-II) signaling by the insulin-like growth factor-I receptor (IGF-IR) and the insulin-like growth factor-II/mannose 6-phosphate receptor (IGF-IIR) in MCF-7 breast cancer cells, employing retroviruses encoding both IGF-I, IGF-II, and IGF-I and II mutants with reductions in affinity for either the IGF-IR or the IGF-IIR. These studies revealed reciprocal roles for IGF-IR and IGF-IIR affinity in the regulation of autocrine IGF-II activity. IGF-IR affinity was required for serum-free proliferation but also for efficient IGF-II secretion. In contrast, cellular proliferation, receptor tyrosine kinase-dependent signaling, and extracellular IGF-II protein accumulation were all reduced in the presence of IGF-IIR affinity. Inhibition of IGF-II signaling appeared to be the sole consequence of IGF-IIR affinity, as no cellular responses attributable to selective IGF-IIR binding by a reduced IGF-IR affinity IGF-II mutant could be detected. By operating as an IGF-II antagonist, the IGF-IIR has tumor suppressor-like properties, a suggestion consistent with reports of loss of heterozygosity at the IGF-IIR locus in a variety of human malignancies. | lld:pubmed |
| pubmed-article:8833657 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8833657 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8833657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8833657 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8833657 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8833657 | pubmed:issn | 0888-8809 | lld:pubmed |
| pubmed-article:8833657 | pubmed:author | pubmed-author:LippmanM EME | lld:pubmed |
| pubmed-article:8833657 | pubmed:author | pubmed-author:PearceAA | lld:pubmed |
| pubmed-article:8833657 | pubmed:author | pubmed-author:RasmussenAA | lld:pubmed |
| pubmed-article:8833657 | pubmed:author | pubmed-author:EllisM JMJ | lld:pubmed |
| pubmed-article:8833657 | pubmed:author | pubmed-author:CullenK JKJ | lld:pubmed |
| pubmed-article:8833657 | pubmed:author | pubmed-author:YanoRR | lld:pubmed |
| pubmed-article:8833657 | pubmed:author | pubmed-author:ParrP LPL | lld:pubmed |
| pubmed-article:8833657 | pubmed:author | pubmed-author:ZweibelJ AJA | lld:pubmed |
| pubmed-article:8833657 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8833657 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:8833657 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8833657 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8833657 | pubmed:pagination | 286-97 | lld:pubmed |
| pubmed-article:8833657 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:meshHeading | pubmed-meshheading:8833657-... | lld:pubmed |
| pubmed-article:8833657 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8833657 | pubmed:articleTitle | Affinity for the insulin-like growth factor-II (IGF-II) receptor inhibits autocrine IGF-II activity in MCF-7 breast cancer cells. | lld:pubmed |
| pubmed-article:8833657 | pubmed:affiliation | Vincent T Lombardi Cancer Center, Georgetown University Medical Center, Washington, D.C, USA. | lld:pubmed |
| pubmed-article:8833657 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8833657 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8833657 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8833657 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8833657 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8833657 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8833657 | lld:pubmed |
