The relevance of phosphorylated forms of estrogen receptor in human breast cancer in vivo.
Estrogen receptor (ER)alpha activity is regulated by phosphorylation at several sites. Recently several antibodies specific for individual phosphorylated sites within ERalpha have became available. Validation and use of these antibodies suggests that several forms of phosphorylated ERalpha can be detected in multiple ER+ human breast tumor samples, thus providing relevance for investigating the regulation and function of phosphorylated ERalpha in human breast cancer. Generally, the phosphorylated ERalpha isoforms are associated with parameters that suggest that they are markers of an intact estrogen dependent signaling pathway and better clinical outcome with respect to tamoxifen therapy. Profiling of phosphorylated ERalpha may provide better biomarkers of endocrine therapy response over and above those currently available.
Murphy
Leigh C
LC
Manitoba Institute of Cell Biology, University of Manitoba, Winnipeg, Manitoba, Canada. lcmurph@cc.umanitoba.ca
Skliris
Georgios P
GP
Rowan
Brian G
BG
Al-Dhaheri
Mariam
M
Williams
Christopher
C
Penner
Carla
C
Troup
Sandy
S
Begic
Sanela
S
Parisien
Michelle
M
Watson
Peter H
PH
D001706:Biopsy; D001943:Breast Neoplasms / Q000378:metabolism* / Q000473:pathology; D018572:Disease-Free Survival; D047628:Estrogen Receptor alpha / Q000235:genetics / Q000378:metabolism*; D005260:Female; D006801:Humans; D010766:Phosphorylation; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
C506487:ESR1 protein, human; D047628:Estrogen Receptor alpha; D020033:Protein Isoforms