Перулік молекулалық биолог Эрнесто Бустаманте

Peruvian molecular biologist

Ernesto Bustamante (born May 19, 1950) is a scientist known for his expertise and contributions to the field of molecular biology. He is currently also a politician and member of the Parliament of Peru.

He served as professor of biochemistry at Cayetano Heredia University (Lima, Peru) during eight years (1977–1984). He also was visiting professor, research professor, visiting researcher, or research scholar at the following institutions: Johns Hopkins University School of Medicine (Baltimore, Maryland, USA) [1979, 1980, 1981, 1984], Universidad de Chile Facultad de Ciencias (Santiago, Chile) [1980, 1981], and more recently at the School of Medicine of the University of North Carolina at Chapel Hill (Chapel Hill, North Carolina, USA) [2002–2005]. Bustamante was a fellow from the Ford Foundation, The Commonwealth Fund of New York, Eli Lilly and Company's Pre doctoral Fellowship in Biology, E. I. DuPont de Nemours & Co., and The Rockefeller Foundation. In 2002 he was awarded competitively a Breast Cancer Concept Award by the U. S. Department of Defense as recommended by the Congressionally directed Medical Research Programs. He has published over thirty peer reviewed original research articles (Google Scholar) in the specialty of mitochondrial bioenergetics and molecular biology. His largest contribution to biochemistry and cell biology was to demonstrate that the mitochondrial hexokinase is the enzyme responsible for driving the high rates of glycolysis that occur under aerobic conditions characteristic of rapidly growing malignant tumor cells. Since then, aerobic glycolysis by malignant tumors is utilized clinically to diagnose and monitor treatment responses of cancers by imaging uptake of 2 18F 2 deoxyglucose (a radioactive modified hexokinase substrate) with positron emission tomography (PET). In 2005, he published a research article that demonstrates that the functional association of glucokinase (a hexokinase isoform) to mitochondrial metabolism and intracellular signaling of apoptosis in normal liver is actually not mediated by a physical association of this enzyme with mitochondria or either their inner membrane or outer membrane as proposed by others.