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Mount Sinai Hospital  >
Pawson, Tony >

Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/9428

Title: p185neu is phosphorylated on tyrosine in human primary breast tumors which overexpress neu/erbB-2
Authors: Wildenhain, Y
Pawson, Tony
Blackstein, ME
Andrulis, IL
Keywords: Breast Neoplasms
Proto-Oncogene Proteins
Tyrosine
Issue Date: Jun-1990
Publisher: Nature Publishing Group
Citation: Oncogene. 1990 Jun;5(6):879-83
Abstract: A series of primary human breast tumors was analysed by immunoblotting with anti-neu antibodies. Overproduction of the neu protein-tyrosine kinase, p185neu, was observed in 23 of 56 malignant tumor samples. 29 of these tumors were also immunoblotted with antiphosphotyrosine antibodies. A single prominent phosphotyrosine-containing protein, which co-migrated with p185neu was identified in 11 of the 29 tumors examined. There was an exact concordance between the tumors with a 185kDa phosphotyrosine-containing protein, and those with elevated p185neu. These results indicate that overexpressed p185neu in primary human breast cancer is phosphorylated on tyrosine, most likely by autophosphorylation, and by inference is enzymatically activated as a protein-tyrosine kinase. Aberrant tyrosine phosphorylation may therefore be important in the development of a substantial fraction of breast cancers.
URI: http://www.nature.com
http://hdl.handle.net/1807/9428
ISSN: 0950-9232
Appears in Collections:Pawson, Tony
Pawson, Tony

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