Abstract

The objective of the proposed studies is to identify the critical molecular events that direct specific repression of PRL gene expression.
Aim 1 is to establish the importance of the alternative splice form of Pit-1 in the repression of PRL and to determine the molecular events that contribute to the splice choice.
Aim 2 is to determine if specific DNA elements in the PRL gene are the key determinants of why PRL gene expression is inhibited in GH3 cell-induced tumors, while GH gene expression is not.
Aim 3 will be to examine the interaction of proteins with the PRL and GH promoters, and to characterize the proteins that are involved in the specific repression of the PRL gene.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK043701-04
Application #
2444055
Study Section
Biochemical Endocrinology Study Section (BCE)
Program Officer
Sato, Sheryl M
Project Start
1994-07-11
Project End
1998-12-31
Budget Start
1997-07-25
Budget End
1998-12-31
Support Year
4
Fiscal Year
1997
Total Cost
Indirect Cost

  Institution

Name
University of Virginia
Department
Internal Medicine/Medicine
Type
Schools of Medicine
DUNS #
001910777
City
Charlottesville
State
VA
Country
United States
Zip Code
22904

  Publications

Tsekouras, Konstantinos; Siegel, Amanda P; Day, Richard N et al. (2015) Inferring diffusion dynamics from FCS in heterogeneous nuclear environments. Biophys J 109:7-17
Day, Richard N (2014) Measuring protein interactions using Förster resonance energy transfer and fluorescence lifetime imaging microscopy. Methods 66:200-7
Shaner, Nathan C; Lambert, Gerard G; Chammas, Andrew et al. (2013) A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum. Nat Methods 10:407-9
Siegel, Amanda P; Hays, Nicole M; Day, Richard N (2013) Unraveling transcription factor interactions with heterochromatin protein 1 using fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy. J Biomed Opt 18:25002
Day, Richard N; Davidson, Michael W (2012) Fluorescent proteins for FRET microscopy: monitoring protein interactions in living cells. Bioessays 34:341-50
Hum, Julia M; Siegel, Amanda P; Pavalko, Fredrick M et al. (2012) Monitoring biosensor activity in living cells with fluorescence lifetime imaging microscopy. Int J Mol Sci 13:14385-400
Sun, Yuansheng; Hays, Nicole M; Periasamy, Ammasi et al. (2012) Monitoring protein interactions in living cells with fluorescence lifetime imaging microscopy. Methods Enzymol 504:371-91
Sun, Yuansheng; Day, Richard N; Periasamy, Ammasi (2011) Investigating protein-protein interactions in living cells using fluorescence lifetime imaging microscopy. Nat Protoc 6:1324-40
Day, Richard N; Davidson, Michael W (2009) The fluorescent protein palette: tools for cellular imaging. Chem Soc Rev 38:2887-921
Day, Richard N; Booker, Cynthia F; Periasamy, Ammasi (2008) Characterization of an improved donor fluorescent protein for Forster resonance energy transfer microscopy. J Biomed Opt 13:031203

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