GLORIA DIMCO1, RICHARD A. KNIGHT2, DAVID S. LATCHMAN2, ANASTASIS STEPHANOU2
1Medical Molecular Biology Unit, Institute of Child Health, University College London, London, UK
*Corresponding author e-mail: firstname.lastname@example.org
The STAT protein family members are among the best studies of the latent cytoplasmic signal-dependent transcription factors that play important roles in development, cell growth and homeostasis. Recently, we have reported that STAT1 and STAT3 have opposing effects in apoptosis in cardiac myocytes exposed to ischaemia/reperfusion injury, which are dependent on the C-terminal phosphorylation domains of these factors. However, very little is known about the factors that interact with phosphorylated STAT1 or STAT3 in the heart, which may mediate their antagonistic effects. Thus, in the present proposal we will use mass spectrometry MALDI-TOF-base proteomic technology to identify novel binding partners for the activated forms of STAT1 or STAT3 in the ischaemic heart. The proposed studies will enable us to characterize novel factors involved in STAT1 and STAT3 protein interactions and may lead to better understanding of the STAT-dependent transcriptional pathways in the stress-induced myocardium and cell cycle.
Keywords: STAT1, STAT1-GST, Emi1, IFNγ, cancer.