Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-10-21
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.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-230489, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-2960385, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-3011821, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-3015587, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-3031062, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-3031063, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-3032981, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-306388, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-313931, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-315944, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-3316935, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-356052, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-4636326, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6090128, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6092175, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6094567, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6095297, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6128346, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6149699, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6149810, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6153980, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6190668, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6196602, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6202705, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6220739, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6246084, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6253485, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6259181, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6260020, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6268987, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6269748, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6272837, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6273899, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6276390, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6279628, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6282315, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6286649, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6288686, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6298257, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6298788, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6325444, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6326261, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6328312, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6498281, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-6946494, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-7040412, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-786865, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-911982, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-944704, http://linkedlifedata.com/resource/pubmed/commentcorrection/3262110-977646
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:volume
107
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
801-10
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
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.
pubmed:affiliation
Department of Pathology, University of Utah, Salt Lake City 84132.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.