Laurie Russell, Ph.D.
Professor
Biology
Courses Taught
General Physiology, Principles of Genetics, Molecular Biology, Cellular and Molecular Genetics
Education
- Ph.D., Washington University in St. Louis
Research Interests
Russell's recent research has focused on the regulation of mitochondrial proliferation and metabolism in the heart, with an emphasis on the role of the transcriptional coactivator peroxisome proliferator-activated receptor g coactivator-1a (PGC-1a) and its interaction with nuclear respiratory factor 1 (NRF-1). Using an inducible, cardiac-specific PGC-1a transgene, she showed that overexpression of PGC-1a induces mitochondrial biogenesis in neonatal mice, but causes cardiomyopathy in adult mice (Circ. Res. 94:525-533, 2004). More recent work has employed overexpression of PGC-1a and NRF-1 in primary cardiac myocytes cultures to delineate NRF-1-dependent pathways downstream of PGC-1a.
Publications and Media Placements
Bennett MJ, Russell LK, Tokunaga C, Narayan SB, Tan L, Seegmiller A, Boriack RL, and Strauss AW. Reye-like syndrome resulting from novel missense mutations in mitochondrial medium- and short- chain L-3-hydroxy-acyl-CoA dehydrogenase. Molecular Genetics and Metabolism 89:74-79 (2006).
Russell LK, Mansfield CM, Lehman JJ, Kovacs A, Courtois M, Saffitz JE, Medeiros DM, Valencik ML, McDonald JA, and Kelly DP. Cardiac-Specific Induction of the Transcriptional Coactivator Peroxisome Proliferator-Activated Receptor g Coactivator-1a Promotes Mitochondrial Biogenesis and Reversible Cardiomyopathy in a Developmental Stage-Dependent Manner. Circulation Research 94: 525 â€" 533 (2004).
Barycki JJ, O’Brien LK, Strauss AW, and Banaszak LJ. Glutamate 170 of the catalytic dyad of human L-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme. Journal of Biological Chemistry 276, 36718-36726 (2001).
Barycki JJ, O’Brien LK, Strauss AW, and Banaszak LJ. Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. Journal of Biological Chemistry 275, 27186-27196 (2000).
Barycki JJ, O'Brien LK, Strauss AW, and Banaszak LJ. Pig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: sequence analysis and crystal structure determination. Protein Science 8, 2010-2018 (1999).
Barycki JJ, O'Brien LK, Bratt JM, Zhang R, Sanishvili R, Strauss AW, and Banaszak LJ. Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxycyl-CoA dehydrogenase provide insights into catalytic mechanism. Biochemistry 38, 5786-5798 (1999).