Gene Expression (incl. Microarray and other genome-wide approaches) Cancer Genetics Proteomics and Intermolecular Interactions (excl. Medical Proteomics) Breast cancer Proteomic analysis Mass spectrometry
Progesterone receptor (PR) isoforms, PRA and PRB, act in a progesterone-independent and dependent manner to differentially modulate the biology of breast cancer cells. Here we show that the differences in PRA and PRB structure facilitate the binding of common and distinct protein interacting partners affecting the downstream signaling events of each PR-isoform. Tet-inducible HA-tagged PRA or HA-tagged PRB constructs were expressed in T47DC42 (PR/ER negative) breast cancer cells. Affinity purification coupled with stable isotope labeling of amino acids in cell culture (SILAC) mass spectrometry technique was performed to comprehensively study PRA and PRB interacting partners in both unliganded and liganded conditions. To validate our findings, we applied both forward and reverse SILAC conditions to effectively minimize experimental errors. These datasets will be useful in investigating PRA- and PRB-specific molecular mechanisms and as a database for subsequent experiments to identify novel PRA and PRB interacting proteins that differentially mediated different biological functions in breast cancer.
Details
Title
Triple SILAC identified progestin-independent and dependent PRA and PRB interacting partners in breast cancer
Authors
Prangwan Pateetin (Author) - Chulalongkorn University
Gyorgy Hutvagner (Author) - University of Technology Sydney
Sarah Bajan (Author) - University of the Sunshine Coast, Queensland, School of Health and Behavioural Sciences - Legacy
Matthew P Padula (Author) - University of Technology Sydney
Eileen M McGowan (Author) - University of Technology Sydney
Viroj Boonyaratanakornkit (Author) - Chulalongkorn University