pubmed-article:7929459 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7929459 | lifeskim:mentions | umls-concept:C0034802 | lld:lifeskim |
pubmed-article:7929459 | lifeskim:mentions | umls-concept:C0019143 | lld:lifeskim |
pubmed-article:7929459 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:7929459 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:7929459 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:7929459 | pubmed:issue | 43 | lld:pubmed |
pubmed-article:7929459 | pubmed:dateCreated | 1994-11-23 | lld:pubmed |
pubmed-article:7929459 | pubmed:abstractText | Human amphiregulin (AR) is a heparin-binding growth factor which functions by binding to and activating the epidermal growth factor (EGF) receptor tyrosine kinase. AR contains an EGF-like domain (residues 44-84) and a Lys/Arg-rich NH2-terminal extension (residues 1-43). Synthetic peptides corresponding to residues 8-26, 26-44, and 68-84 of AR were tested for their ability to compete for the binding of AR to immobilized heparin. AR8-26 and AR68-84 had no significant effect on the binding of AR to heparin, whereas AR26-44 bound to heparin and blocked the binding of AR to heparin. Both soluble heparin and heparan sulfate inhibited AR-induced mitogenesis in MCF-10A human mammary epithelial cells with an IC50 of 5 and 2 micrograms/ml, respectively, whereas soluble chondroitin sulfate had only a slight inhibitory effect. When MCF-10A cells were grown in the presence of chlorate, an inhibitor of sulfation, or exposed to the glycosaminoglycan-degrading enzymes heparitinase or heparinase, the ability of AR to evoke mitogenesis in these cells was lost. Chlorate, heparitinase, or heparinase treatment inhibited AR-induced autophosphorylation of tyrosine residues in the EGF receptor. None of these treatments had any significant effect on EGF-triggered mitogenic signaling by the EGF receptor. These results indicate that extracellular heparan sulfate glycosaminoglycan is essential to AR-induced mitogenic signaling by the EGF receptor tyrosine kinase. | lld:pubmed |
pubmed-article:7929459 | pubmed:language | eng | lld:pubmed |
pubmed-article:7929459 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7929459 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7929459 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7929459 | pubmed:month | Oct | lld:pubmed |
pubmed-article:7929459 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7929459 | pubmed:author | pubmed-author:JohnsonG RGR | lld:pubmed |
pubmed-article:7929459 | pubmed:author | pubmed-author:WongLL | lld:pubmed |
pubmed-article:7929459 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7929459 | pubmed:day | 28 | lld:pubmed |
pubmed-article:7929459 | pubmed:volume | 269 | lld:pubmed |
pubmed-article:7929459 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7929459 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7929459 | pubmed:pagination | 27149-54 | lld:pubmed |
pubmed-article:7929459 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:7929459 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7929459 | pubmed:articleTitle | Heparan sulfate is essential to amphiregulin-induced mitogenic signaling by the epidermal growth factor receptor. | lld:pubmed |
pubmed-article:7929459 | pubmed:affiliation | Division of Cytokine Biology, Food and Drug Administration, Bethesda, Maryland 20892. | lld:pubmed |
pubmed-article:7929459 | pubmed:publicationType | Journal Article | lld:pubmed |
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