| Self-phosphorylation of epidermal growth factor receptor is an intermolecular reaction. | |
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MedLine Citation:
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PMID: 9335547 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The binding of epidermal growth factor (EGF) to epidermal growth factor receptor (EGF receptor) results in the dimerization and self-phosphorylation of the receptor. Both of these responses were followed as a function of time and the concentration of EGF receptor. Dimerization of EGF receptor was monitored by immunoblotting the protein after it had been cross-linked with glutaraldehyde. The capacity for self-phosphorylation was followed by measuring the relative level of incorporation of [32P]phosphate into EGF receptor on autoradiograms of the same immunoblots used for the assay of its dimerization. When these two properties were followed as a function of time, it was found that dimerization preceded the appearance of the capacity for self-phosphorylation. Both dimeric and monomeric forms of EGF receptor were self-phosphorylated in the presence of EGF, but the dimeric form was phosphorylated preferentially to the monomeric form. When the dimerization and the capacity for self-phosphorylation were followed as a function of the concentration of dimeric EGF receptor, it was observed that the self-phosphorylation of dimeric EGF receptor increased as the concentration of dimeric EGF receptor increased. An equation including terms representing both intramolecular and intermolecular rates of self-phosphorylation was fit to the plots of self-phosphorylation as a function of concentration of EGF receptor. These fits demonstrate that intramolecular self-phosphorylation within dimers of EGF receptor is insignificant and that self-phosphorylation is an intermolecular process between dimers of EGF receptor. |
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Authors:
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J M Sherrill |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Biochemistry Volume: 36 ISSN: 0006-2960 ISO Abbreviation: Biochemistry Publication Date: 1997 Oct |
Date Detail:
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Created Date: 1997-11-20 Completed Date: 1997-11-20 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 12890-6 Citation Subset: IM |
Affiliation:
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Department of Chemistry and Biochemistry 0506, University of California at San Diego, 9500 Gilman Drive, La Jolla, California 92093-0506, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphate
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metabolism* Carcinoma, Squamous Cell Cross-Linking Reagents Dimerization Epidermal Growth Factor / metabolism* Glutaral Humans Kinetics Phosphorus Radioisotopes Phosphorylation Radioisotope Dilution Technique Receptor, Epidermal Growth Factor / chemistry*, isolation & purification, metabolism* Tumor Cells, Cultured |
| Grant Support | |
ID/Acronym/Agency:
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GM-33962/GM/NIGMS NIH HHS; T32-GM07313/GM/NIGMS NIH HHS; T32-GM08326/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cross-Linking Reagents; 0/Phosphorus Radioisotopes; 111-30-8/Glutaral; 56-65-5/Adenosine Triphosphate; 62229-50-9/Epidermal Growth Factor; EC 2.7.10.1/Receptor, Epidermal Growth Factor |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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