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dc.contributor.authorDavis, Roger J.
dc.contributor.authorFaucher, Mark
dc.contributor.authorRacaniello, Lori Kuck
dc.contributor.authorCarruthers, Anthony
dc.contributor.authorCzech, Michael P.
dc.date2022-08-11T08:10:05.000
dc.date.accessioned2022-08-23T16:54:44Z
dc.date.available2022-08-23T16:54:44Z
dc.date.issued1987-09-25
dc.date.submitted2008-08-15
dc.identifier.citationJ Biol Chem. 1987 Sep 25;262(27):13126-34.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid3498714
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42570
dc.description.abstractThe transferrin receptor cycles rapidly between cell surface and endosomal membrane compartments. Treatment of cultured cells with epidermal growth factor (EGF) or insulin-like growth factor I (IGF-I) at 37 degrees C causes a rapid redistribution of transferrin receptors from an intracellular compartment to the cell surface. The effects of EGF and IGF-I on the kinetics of the cycling of the transferrin receptor in A431 human epidermoid carcinoma cells were compared. The primary site of EGF action was found to be an increase in the rate of transferrin receptor exocytosis. The exocytotic rate constant was measured to be 0.11 min-1 in control cells and 0.33 min-1 in EGF-treated cells. In contrast, IGF-I was found to increase the cell surface expression of transferrin receptors by causing a small increase in the rate of exocytosis (from 0.11 to 0.17 min-1) and a decrease in the rate of endocytosis (from 0.33 to 0.24 min-1). It is concluded that the mechanisms for EGF and IGF-I action to increase the cell surface expression of the transferrin receptor are distinct. A kinetic model of the cycling of the transferrin receptor based on experimentally determined rate constants is presented. The model predicts that a consequence of IGF-I action on transferrin receptor cycling is to decrease the apparent Km for the uptake of diferric transferrin by cells. This prediction is confirmed by direct measurement of the accumulation of 59Fe-labeled diferric transferrin by A431 cells. These data demonstrate that the accumulation of iron by cultured cells is a complex function of the rate of cycling of the transferrin receptor and that this process is under acute regulation by growth factors.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=3498714&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/content/262/27/13126.full.pdf+html
dc.subjectCarcinoma, Squamous Cell
dc.subjectCell Membrane
dc.subjectEpidermal Growth Factor
dc.subjectExocytosis
dc.subjectHumans
dc.subjectInsulin-Like Growth Factor I
dc.subjectIron
dc.subjectKinetics
dc.subjectModels, Biological
dc.subjectReceptors, Transferrin
dc.subjectSomatomedins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleInsulin-like growth factor I and epidermal growth factor regulate the expression of transferrin receptors at the cell surface by distinct mechanisms
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume262
dc.source.issue27
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/906
dc.identifier.contextkey579795
html.description.abstract<p>The transferrin receptor cycles rapidly between cell surface and endosomal membrane compartments. Treatment of cultured cells with epidermal growth factor (EGF) or insulin-like growth factor I (IGF-I) at 37 degrees C causes a rapid redistribution of transferrin receptors from an intracellular compartment to the cell surface. The effects of EGF and IGF-I on the kinetics of the cycling of the transferrin receptor in A431 human epidermoid carcinoma cells were compared. The primary site of EGF action was found to be an increase in the rate of transferrin receptor exocytosis. The exocytotic rate constant was measured to be 0.11 min-1 in control cells and 0.33 min-1 in EGF-treated cells. In contrast, IGF-I was found to increase the cell surface expression of transferrin receptors by causing a small increase in the rate of exocytosis (from 0.11 to 0.17 min-1) and a decrease in the rate of endocytosis (from 0.33 to 0.24 min-1). It is concluded that the mechanisms for EGF and IGF-I action to increase the cell surface expression of the transferrin receptor are distinct. A kinetic model of the cycling of the transferrin receptor based on experimentally determined rate constants is presented. The model predicts that a consequence of IGF-I action on transferrin receptor cycling is to decrease the apparent Km for the uptake of diferric transferrin by cells. This prediction is confirmed by direct measurement of the accumulation of 59Fe-labeled diferric transferrin by A431 cells. These data demonstrate that the accumulation of iron by cultured cells is a complex function of the rate of cycling of the transferrin receptor and that this process is under acute regulation by growth factors.</p>
dc.identifier.submissionpathoapubs/906
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Biochemistry
dc.source.pages13126-34


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