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p185neu is phosphorylated on tyrosine in human primary breast tumors which overexpress neu/erbB-2.

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.

journal_name

Oncogene

journal_title

Oncogene

authors

Wildenhain Y,Pawson T,Blackstein ME,Andrulis IL

subject

Has Abstract

pub_date

1990-06-01 00:00:00

pages

879-83

issue

6

eissn

0950-9232

issn

1476-5594

journal_volume

5

pub_type

杂志文章

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