Elevated content of the tyrosine kinase substrate phospholipase C-γ1 in primary human breast carcinomas

C. L. Arteaga, Mahlon Johnson, G. Todderud, R. J. Coffey, G. Carpenter, D. L. Page

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Abstract

Phospholipase C-γ1 (PLC-γ1) is a substrate for several receptor tyrosine kinases and its catalytic activity is increased by tyrosine phosphorylation. However, the biological significance of this molecule in normal or malignant human epithelial cell proliferation is unknown. We determined the relative content of PLC-γ1 in primary human mammary carcinomas and in nonmalignant mammary tissues. By Western blot and immunohistochemistry, considerably higher levels of PLC-γ1 protein were detectable in the majority of carcinomas and in one of two benign fibroadenomas compared to normal breast tissues. In 18 of 21 carcinomas that contained high levels of PLC-γ1, the presence of phosphotyrosine on PLC-γ1 could also be detected. All carcinomas in which tyrosine phosphorylated PLC-γ1 was present also expressed detectable levels of the epidermal growth factor receptor or erbB-2, two tyrosine kinases known to phosphorylate this enzyme. Thus, a high percentage of mammary carcinomas concomitantly display increased levels of receptor tyrosine kinases and a direct tyrosine phosphorylation substrate, thereby potentially amplifying two successive steps in a signal transduction pathway.

Original languageEnglish (US)
Pages (from-to)10435-10439
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number23
DOIs
StatePublished - Jan 1 1991

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Type C Phospholipases
Protein-Tyrosine Kinases
Breast Neoplasms
Tyrosine
Receptor Protein-Tyrosine Kinases
Carcinoma
Breast
TYK2 Kinase
Phosphorylation
Fibroadenoma
Phosphotyrosine
Epidermal Growth Factor Receptor
Signal Transduction
Western Blotting
Epithelial Cells
Immunohistochemistry
Cell Proliferation
Enzymes
Proteins

All Science Journal Classification (ASJC) codes

  • General

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Elevated content of the tyrosine kinase substrate phospholipase C-γ1 in primary human breast carcinomas. / Arteaga, C. L.; Johnson, Mahlon; Todderud, G.; Coffey, R. J.; Carpenter, G.; Page, D. L.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, No. 23, 01.01.1991, p. 10435-10439.

Research output: Contribution to journalArticle

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AU - Carpenter, G.

AU - Page, D. L.

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AB - Phospholipase C-γ1 (PLC-γ1) is a substrate for several receptor tyrosine kinases and its catalytic activity is increased by tyrosine phosphorylation. However, the biological significance of this molecule in normal or malignant human epithelial cell proliferation is unknown. We determined the relative content of PLC-γ1 in primary human mammary carcinomas and in nonmalignant mammary tissues. By Western blot and immunohistochemistry, considerably higher levels of PLC-γ1 protein were detectable in the majority of carcinomas and in one of two benign fibroadenomas compared to normal breast tissues. In 18 of 21 carcinomas that contained high levels of PLC-γ1, the presence of phosphotyrosine on PLC-γ1 could also be detected. All carcinomas in which tyrosine phosphorylated PLC-γ1 was present also expressed detectable levels of the epidermal growth factor receptor or erbB-2, two tyrosine kinases known to phosphorylate this enzyme. Thus, a high percentage of mammary carcinomas concomitantly display increased levels of receptor tyrosine kinases and a direct tyrosine phosphorylation substrate, thereby potentially amplifying two successive steps in a signal transduction pathway.

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