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Crosstalk between EGFR and Extranuclear Steroid Receptors
Author(s) -
MIGLIACCIO ANTIMO,
CASTORIA GABRIELLA,
DOMENICO MARINA DI,
CIOCIOLA ALESSANDRA,
LOMBARDI MARIA,
DE FALCO ANTONIETTA,
NANAYAKKARA MERLIN,
BOTTERO DANIELA,
DE STASIO ROSINA,
VARRICCHIO LILIAN,
AURICCHIO FERDINANDO
Publication year - 2006
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1386.006
Subject(s) - lncap , proto oncogene tyrosine protein kinase src , epidermal growth factor , tyrosine kinase , cancer research , estrogen receptor , microbiology and biotechnology , tyrosine phosphorylation , phosphorylation , biology , receptor , androgen receptor , growth factor receptor , endocrinology , signal transduction , chemistry , medicine , cancer cell , prostate cancer , biochemistry , cancer , breast cancer
Epidermal growth factor (EGF) stimulates DNA synthesis and cytoskeletal rearrangement in human breast cancer (MCF‐7) and human prostate cancer (LNCaP) cells. Both effects are inhibited by estrogen (ICI 182,780) and androgen (Casodex) antagonists. This supports the view that crosstalk exists between EGF and estradiol (ER) and androgen (AR) receptors and suggests that these receptors are directly involved in the EGF action. Our recent work shows that EGF stimulates ER phosphorylation on tyrosine and promotes the association of a complex between EGFR, AR/ER, and the kinase Src. The complex assembly triggers Src activity, epidermal growth factor receptor (EGFR) phosphorylation on tyrosine, and the EGF‐dependent signaling pathway activation. In these cells, the AR/ER/Src complex is required for the EGF action, as the growth factor effects are abolished upon receptor silencing by specific SiRNAs and steroid antagonists or Src inhibition by the kinase inhibitor PP2.