Christian de Duve (De Duve), Christian

genus. October 2, 1917
Belgian biochemist Christian Renц? De Duve was born in Thames Dittone (a suburb of London). His parents were Madeleine de Duve (Pangs) and Alphonse de Duve - Belgian citizens who found refuge in Britain during the First World War. In 1920, Mr.. family returned to Belgium and settled in Antwerp, here Christian was educated in French and Flemish. In 1934, Mr.. he entered the Catholic University of Louvain - a Jesuit school with a humanitarian slant. However, intrigued by medicine, soon moved to the middle, and then in a medical institution of higher learning in Louvain, where he worked in the physiological laboratory M. Bukkerta. He studied the processes of glucose utilization by cells. By 1941, when D. received a medical degree, he has firmly set out to elucidate the mechanism of action of insulin - a hormone that regulates the use of glucose in the body.
During the Second World War D. initially for some time served in the Belgian army, then was taken prisoner, escaped and returned to Louvain. Here he was a four-year university course and graduated chemist. By 1945, Mr.. D. In 1946, Mr.. Here he met with Charles V. and Gerty T. Cory. Also at Washington University he had opportunity cooperate with Earle U. Sutherland.
Returning to Belgium, D. he became a professor of biochemistry in medical school at the Catholic University of Louvain. Here he created a research laboratory. In an effort to understand the mechanism of action of insulin, D. conducted a series of experiments to study the properties of the enzyme of the liver cells involved in glucose metabolism - the process whereby it becomes the basic elements used by the body as an energy source. To explore biochemical properties cells, necessary was divide these cells on separate components by centrifugation. At the same time in different layers of the tube settled at different cells depending on their size, shape and density, and they could investigate separately. This method, . developed by Albert Claude and named by cell fractionation, . could provide several cell fractions: nucleus, . containing chromosomes; mitochondria, . playing role 'energy stations' cells; microsomes (subsequently named ribosomes) - plots education molekul proteins and supernatant - liquid part cells,
. D. and his colleagues at the University of Louvain improved this method so that it was possible to analyze the separated fractions. This new method, . called analytical cell fractionation, . possible to obtain additional data on the enzyme (enzymes - are proteins, . are catalysts for transformation of substances in the body) activity of individual fractions, . and especially the activity of organelles - intracellular structures, . carry out specific functions for the cell in general.,
. The first major achievement of the D
. was the discovery of new organelles - lysosomes. In 1949, Mr.. he and his colleagues discovered that the enzyme activity of liver cells of acid phosphatase, as contained in the mitochondrial fraction, on the fifth day after the fractionation was much higher than the first day. D. explained that the existence of another cytoplasmic organelles, the stability of the membrane which in laboratory conditions and delays in the manifestation of activity of enzymes. In the early 50-ies. D. and his team discovered another subcellular organelle containing the enzyme oxidase uric acid, this organelle was called peroxisomes.
Then D. and his colleagues undertook a study of these two new organelle - a problem worked on that and many other researchers. In 1983, summarizing the work, D. indicated that lysosomes - are small particles in the form of bubbles bounded by membrane. They contain many enzymes involved in the intracellular digestion of nutrients, foreign bodies, and sometimes the cell itself. In mammals, lysosomes are contained in large amounts in the cells of the liver and kidneys. As peroxisome, . widespread in plant and animal cells, . they, . apparently, . perform two metabolic functions: convert many molecules in the intracellular hydrogen peroxide, . which is subsequently reduced to water, . and contribute to the transformation of intracellular proteins in glucose,
. Neither lysosomes, or peroxisomes can not be, like mitochondria, the energy source for cells.
In 1951, Mr.. D. became professor of physiological chemistry in Louvain. In 1962. He was appointed professor of biological Cytology at Rockefeller University in New York. These positions allowed him to continue to study the functions of the two found their new organelles. In 1962. he and several colleagues founded the International Institute of Cellular and Molecular Pathology at the new Louvain Medical School in Brussels.
In 1974. D. together with Albert Claude and George E. Palade was awarded the Nobel Prize in Physiology or Medicine "for discoveries concerning the structural and functional organization of the cells'. In his Nobel lecture D. told about the purpose of the study of enzymes, quoting Hugo Hugo Theorell: 'The first stage is fully studied the spatial structure of all enzymes. On the second - to find out how enzymes are organized in cellular structures. Thus, a bridge across the gap between biochemistry and morphology '.
After receiving the Nobel Prize D. spent a lot of research, whose results have not yet found practical application. He studied, for example, properties and function of lysosomes and peroxisomes in normal conditions and in various diseases. Together with his colleagues, he established, . that the lack of lysosomal enzymes may be one of the pathogenetic factors of 20 different diseases, . under which disrupted the accumulation of glycogen - polysaccharide of high molecular, . formation of fats and polysaccharides - the main components of the basic substance of connective tissue,
. D. suggested that lysosomes and their enzymes may participate in the process of aging and decay of tissues. In addition, he and his colleagues studied the effects of drugs (like steroids) that suppress inflammatory reactions in tissues, and showed that they can influence the membrane of lysosomes. He and his colleagues are also trying to obtain substances that increase efficiency and reduce the effects of the drugs used for chemotherapy of leukemia.
In 1943, Mr.. D. married to Jeanine Herman, the daughter of a doctor. The family had two sons and two daughters. D. operates at two positions in New York and Brussels, dividing his time between the two laboratories. He enjoys bridge, skiing and tennis.
In addition to the Nobel Prize, Dr.. Pfizer was awarded the Prize of the Belgian Royal Academy of Medicine (1957), Prize Fund Franks Franks (1960), Special Award of Gardner Fund (1967) and the Heineken Prize of the Royal Netherlands Academy of Sciences (1973). He is a member of the Belgian Royal Academy of Medicine, Pontifical Academy of Sciences, the American Academy of Arts and Sciences and National Academy of Sciences, USA. He was awarded honorary degrees from more than 10 different American and European universities.