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PMID: 6207534 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Antibodies to two defined regions of the transforming protein pp60src interact specifically with the epidermal growth factor receptor kinase system.

Lax I, Bar-Eli M, Yarden Y, Libermann TA, Schlessinger J

Abstract

Antibodies generated against two synthetic peptides corresponding to two defined regions on the transforming protein of Rous sarcoma virus, pp60src, interact specifically with the epidermal growth factor (EGF)-receptor kinase. An antibody directed against a synthetic peptide corresponding to the major phosphorylation site of pp60src interacts specifically with EGF receptor and immunoprecipitates a functional EGF-receptor kinase. The second antibody, which binds close to a region on the src molecule that is required for its kinase activity, also binds to EGF-receptor kinase and prevents the autophosphorylation of the receptor molecules. Neither antibody binds to intact cells, but they do recognize various forms of the solubilized receptor. It is concluded that at least two cytoplasmic domains of the EGF receptor are antigenically and presumably also structurally related to specific domains on pp60src.

MeSH Terms
Amino Acid Sequence Antibodies Antigen-Antibody Complex Carcinoma, Squamous Cell Cell Line Cell Membrane/metabolism Enzyme-Linked Immunosorbent Assay Epidermal Growth Factor/metabolism Epitopes/analysis ErbB Receptors Humans Oncogene Protein pp60(v-src) Phosphorylation Protein Kinases/immunology Receptors, Cell Surface/metabolism Viral Proteins/immunology
Chemicals
Antibodies Antigen-Antibody Complex Epitopes Receptors, Cell Surface Viral Proteins Epidermal Growth Factor Protein Kinases ErbB Receptors Oncogene Protein pp60(v-src)
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Lax I
Bar-Eli M
Yarden Y
Libermann T A
Schlessinger J
References (29)
29 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1984-10-00
Pages
5911-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC391828
Subset
IM
Grants
NCI NIH HHS · CA-25820 · United States
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