William Kaelin, Sir Peter Ratcliffe and Gregg Semenza have been named the winners of the 2019 Nobel prize in medicine
Three scientists have shared this year’s Nobel prize in physiology or medicine for discovering how cells respond to varying oxygen levels in the body, one of the most essential adaptive processes for life.
William Kaelin Jr at Harvard University in Cambridge, Massachusetts; Sir Peter Ratcliffe at Oxford University and the Francis Crick Institute in London; and Gregg Semenza at Johns Hopkins University in Baltimore, Maryland won for “how cells sense and adapt to oxygen availability,” the Nobel committee said.
Beyond describing a fundamental physiological process that helps animals to thrive in some of the highest regions on Earth, the mechanism has given researchers new insights into treatments for anaemia, cancer and other diseases.
In work that spanned more than two decades, the researchers teased apart how low oxygen, known as hypoxia, drives up levels
This year’s Nobel laureates “have greatly expanded our knowledge of how physiological response makes life possible,” said Randall Johnson, professor of molecular physiology and pathology at Cambridge University.
A drug that boosts the body’s production of oxygen-carrying red blood cells by tapping into the molecular machinery identified by the winners has already been approved in China and is under consideration by regulators in Europe.
The three laureates will share the 9m Swedish kronor (£740,000) equally, according to the announcement from the Royal Swedish Academy of Sciences in Stockholm.
When the body is deprived of oxygen, there is a rise in the hormone erythropoietin (EPO) – this then boosts the production of red blood cells, which carry oxygen around the body.
But how does a drop in oxygen trigger this response? This year’s laureates found the answer.
They found that when oxygen levels drop, levels of a protein complex (dubbed HIF) increase. Under normal oxygen conditions, HIF is rapidly broken down – but under low oxygen conditions it builds up. Crucially this complex binds to segments of DNA near the gene for EPO.