Title |
Targeting aspartate aminotransferase in breast cancer
|
---|---|
Published in |
Breast Cancer Research, October 2008
|
DOI | 10.1186/bcr2154 |
Pubmed ID | |
Authors |
Joshua Marshall Thornburg, Kristin K Nelson, Brian F Clem, Andrew N Lane, Sengodagounder Arumugam, Allan Simmons, John W Eaton, Sucheta Telang, Jason Chesney |
Abstract |
Glycolysis is increased in breast adenocarcinoma cells relative to adjacent normal cells in order to produce the ATP and anabolic precursors required for survival, growth and invasion. Glycolysis also serves as a key source of the reduced form of cytoplasmic nicotinamide adenine dinucleotide (NADH) necessary for the shuttling of electrons into mitochondria for electron transport. Lactate dehydrogenase (LDH) regulates glycolytic flux by converting pyruvate to lactate and has been found to be highly expressed in breast tumours. Aspartate aminotransferase (AAT) functions in tandem with malate dehydrogenase to transfer electrons from NADH across the inner mitochondrial membrane. Oxamate is an inhibitor of both LDH and AAT, and we hypothesised that oxamate may disrupt the metabolism and growth of breast adenocarcinoma cells. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United Kingdom | 2 | 1% |
United States | 2 | 1% |
Czechia | 1 | <1% |
Mexico | 1 | <1% |
Germany | 1 | <1% |
Unknown | 191 | 96% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 55 | 28% |
Researcher | 34 | 17% |
Student > Bachelor | 15 | 8% |
Student > Master | 13 | 7% |
Professor | 8 | 4% |
Other | 25 | 13% |
Unknown | 48 | 24% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 47 | 24% |
Biochemistry, Genetics and Molecular Biology | 41 | 21% |
Chemistry | 17 | 9% |
Medicine and Dentistry | 16 | 8% |
Pharmacology, Toxicology and Pharmaceutical Science | 7 | 4% |
Other | 16 | 8% |
Unknown | 54 | 27% |