Journal
BREAST CANCER RESEARCH AND TREATMENT
Volume 118, Issue 3, Pages 443-453Publisher
SPRINGER
DOI: 10.1007/s10549-008-0267-z
Keywords
Phosphorylation; Estrogen receptor; Breast cancer; Tissue microarrays; Immunohistochemistry; Validation; Tissue collection time; Endocrine therapy
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Funding
- Manitoba Health Research Council (MHRC)
- CancerCare Manitoba Foundation (CCMF)
- MHRC studentship
- Canadian Institute of Health Research (CIHR)
- Canadian Breast Cancer Research Alliance (CBCRA)
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Estrogen receptor a (ER alpha) activity is regulated by phosphorylation at several sites. Recently several antibodies specific for individual phosphorylated sites within ERa have became available. Such antibodies potentially provide invaluable tools to gain insight into the relevance in vivo of phosphorylated ERa in human breast tumors. However, validation of these antibodies for immunohistochemistry in particular is necessary in the first instance. In this study we have investigated the usefulness of several antibodies generated to specific phosphorylated sites within ERa for immunohistochemistry of formalin-fixed, paraffin-embedded human breast cancer biopsy samples. As well, these data demonstrate for the first time, the detection of multiple phosphorylated ERa forms in breast cancer (P-S104/106-ER alpha, P-S118-ER alpha, P-S167-ER alpha, P-S282-ER alpha, P-S294-ER alpha, P-T311-ER alpha, and P-S559-ER alpha) suggesting the possibility that profiling of phosphorylated ERa isoforms might be useful in selecting subgroups of breast cancer patients that would benefit from endocrine therapy.
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