pubmed-article:3262110 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3262110 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:3262110 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
pubmed-article:3262110 | lifeskim:mentions | umls-concept:C0678226 | lld:lifeskim |
pubmed-article:3262110 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:3262110 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:3262110 | lifeskim:mentions | umls-concept:C0599283 | lld:lifeskim |
pubmed-article:3262110 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:3262110 | pubmed:dateCreated | 1988-10-21 | lld:pubmed |
pubmed-article:3262110 | pubmed:abstractText | This study was conducted to determine how extraordinarily high numbers of epidermal growth factor receptors (EGF-R) affected the binding and internalization of EGF in the transformed cell line A431. I found that at low EGF concentrations, the kinetics of binding behaved as a nonsaturable, first-order process showing no evidence of multiple-affinity classes of receptors. However, EGF dissociation rates were strongly dependent on the degree of receptor occupancy in both intact cells and isolated membranes. This occupancy-dependent dissociation appears to be due to diffusion-limited binding. EGF-induced receptor internalization was rapid and first order when the absolute number of occupied receptors was below 4 x 10(3) min-1. However, at higher occupancies the specific internalization rate progressively declined to a final limiting value of 20% normal. The saturation of EGF-R endocytosis was specific since internalization of transferrin receptors was not affected by high concentrations of either transferrin or EGF. Saturation of EGF-R endocytosis probably involves a specific component of the endocytic pathway since fluid phase endocytosis increased coordinately with EGF-R occupancy. I conclude that there are several aspects of EGF-R dynamics on A431 cells are neither similar to the behavior of EGF-R in other cell types nor similar to the reported behavior of other hormone receptors. Although A431 cells have an extraordinary number of EGF-R, they do not seem to have corresponding levels of at least two other crucial cell surface components: one that mediates EGF-induced rapid receptor internalization and one that attenuates EGF-induced membrane responses. These factors, in addition to the presence of diffusion-limited binding at low EGF concentrations, are probably responsible for the appearance of multiple-affinity classes of receptors in this cell type. | lld:pubmed |
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pubmed-article:3262110 | pubmed:language | eng | lld:pubmed |
pubmed-article:3262110 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3262110 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3262110 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3262110 | pubmed:month | Aug | lld:pubmed |
pubmed-article:3262110 | pubmed:issn | 0021-9525 | lld:pubmed |
pubmed-article:3262110 | pubmed:author | pubmed-author:WileyH SHS | lld:pubmed |
pubmed-article:3262110 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3262110 | pubmed:volume | 107 | lld:pubmed |
pubmed-article:3262110 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3262110 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3262110 | pubmed:pagination | 801-10 | lld:pubmed |
pubmed-article:3262110 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:3262110 | pubmed:meshHeading | pubmed-meshheading:3262110-... | lld:pubmed |
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pubmed-article:3262110 | pubmed:meshHeading | pubmed-meshheading:3262110-... | lld:pubmed |
pubmed-article:3262110 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:3262110 | pubmed:articleTitle | Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system. | lld:pubmed |
pubmed-article:3262110 | pubmed:affiliation | Department of Pathology, University of Utah, Salt Lake City 84132. | lld:pubmed |
pubmed-article:3262110 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3262110 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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