Proteins phosphorylated on tyrosine in human breast cancer

S. Bretti, A. P M Cappa, P. M. Comoglio, M. F. Di Renzo

Research output: Contribution to journalArticle

Abstract

Proteins phosphorylated on tyrosine are detectable by antibodies against phosphotyrosine (P-Tyr) in cells transformed by oncogene-encoded tyrosine kinases. In this work, P-Tyr antibodies were used to investigate the existence of abnormal levels of tyrosine phosphoproteins in human breast cancers. Three human breast cancer cell lines and 37 human breast cancer specimens were examined by Western blot analysis and in vitro kinase assays. In the SK-BR-3 cell line three major phosphoproteins of approximate Mr of 185,000 (p185), 135,000 (p135) and 110,000 (p110) were detected. P185 was identified as the HER-2 gene-encoded protein. In the MCF-7 and CG-5 cell lines, a protein of approximate Mr of 170,000 (p170), together with a p135 and a p110, were found to be phosphorylated on tyrosine. P135 and p110, were also found to be abnormally phosphorylated on tyrosine in 50% of the breast cancer samples tested. In all samples the HER-2 protein was detectable at various levels but was not found to be phosphorylated.

Original languageEnglish
Pages (from-to)134-138
Number of pages5
JournalCancer Journal (United States)
Volume3
Issue number3
Publication statusPublished - 1990

Fingerprint

Tyrosine
Breast Neoplasms
Phosphotyrosine
Phosphoproteins
Cell Line
Proteins
erbB-2 Genes
Antibodies
Oncogenes
Protein-Tyrosine Kinases
Phosphotransferases
Western Blotting

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

Proteins phosphorylated on tyrosine in human breast cancer. / Bretti, S.; Cappa, A. P M; Comoglio, P. M.; Di Renzo, M. F.

In: Cancer Journal (United States), Vol. 3, No. 3, 1990, p. 134-138.

Research output: Contribution to journalArticle

@article{5b67c07050b947fbbee5ee31a116fdc8,
title = "Proteins phosphorylated on tyrosine in human breast cancer",
abstract = "Proteins phosphorylated on tyrosine are detectable by antibodies against phosphotyrosine (P-Tyr) in cells transformed by oncogene-encoded tyrosine kinases. In this work, P-Tyr antibodies were used to investigate the existence of abnormal levels of tyrosine phosphoproteins in human breast cancers. Three human breast cancer cell lines and 37 human breast cancer specimens were examined by Western blot analysis and in vitro kinase assays. In the SK-BR-3 cell line three major phosphoproteins of approximate Mr of 185,000 (p185), 135,000 (p135) and 110,000 (p110) were detected. P185 was identified as the HER-2 gene-encoded protein. In the MCF-7 and CG-5 cell lines, a protein of approximate Mr of 170,000 (p170), together with a p135 and a p110, were found to be phosphorylated on tyrosine. P135 and p110, were also found to be abnormally phosphorylated on tyrosine in 50{\%} of the breast cancer samples tested. In all samples the HER-2 protein was detectable at various levels but was not found to be phosphorylated.",
author = "S. Bretti and Cappa, {A. P M} and Comoglio, {P. M.} and {Di Renzo}, {M. F.}",
year = "1990",
language = "English",
volume = "3",
pages = "134--138",
journal = "Cancer Journal from Scientific American",
issn = "1528-9117",
publisher = "Association Pour le Developpement de la Communication Cancerologique",
number = "3",

}

TY - JOUR

T1 - Proteins phosphorylated on tyrosine in human breast cancer

AU - Bretti, S.

AU - Cappa, A. P M

AU - Comoglio, P. M.

AU - Di Renzo, M. F.

PY - 1990

Y1 - 1990

N2 - Proteins phosphorylated on tyrosine are detectable by antibodies against phosphotyrosine (P-Tyr) in cells transformed by oncogene-encoded tyrosine kinases. In this work, P-Tyr antibodies were used to investigate the existence of abnormal levels of tyrosine phosphoproteins in human breast cancers. Three human breast cancer cell lines and 37 human breast cancer specimens were examined by Western blot analysis and in vitro kinase assays. In the SK-BR-3 cell line three major phosphoproteins of approximate Mr of 185,000 (p185), 135,000 (p135) and 110,000 (p110) were detected. P185 was identified as the HER-2 gene-encoded protein. In the MCF-7 and CG-5 cell lines, a protein of approximate Mr of 170,000 (p170), together with a p135 and a p110, were found to be phosphorylated on tyrosine. P135 and p110, were also found to be abnormally phosphorylated on tyrosine in 50% of the breast cancer samples tested. In all samples the HER-2 protein was detectable at various levels but was not found to be phosphorylated.

AB - Proteins phosphorylated on tyrosine are detectable by antibodies against phosphotyrosine (P-Tyr) in cells transformed by oncogene-encoded tyrosine kinases. In this work, P-Tyr antibodies were used to investigate the existence of abnormal levels of tyrosine phosphoproteins in human breast cancers. Three human breast cancer cell lines and 37 human breast cancer specimens were examined by Western blot analysis and in vitro kinase assays. In the SK-BR-3 cell line three major phosphoproteins of approximate Mr of 185,000 (p185), 135,000 (p135) and 110,000 (p110) were detected. P185 was identified as the HER-2 gene-encoded protein. In the MCF-7 and CG-5 cell lines, a protein of approximate Mr of 170,000 (p170), together with a p135 and a p110, were found to be phosphorylated on tyrosine. P135 and p110, were also found to be abnormally phosphorylated on tyrosine in 50% of the breast cancer samples tested. In all samples the HER-2 protein was detectable at various levels but was not found to be phosphorylated.

UR - http://www.scopus.com/inward/record.url?scp=0025360087&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025360087&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0025360087

VL - 3

SP - 134

EP - 138

JO - Cancer Journal from Scientific American

JF - Cancer Journal from Scientific American

SN - 1528-9117

IS - 3

ER -