Protein degradation and malfunction is a major cause of ageing and can be the result of attacks on proteins by other molecules.
One of these processes, called glycation, involves the spontaneous attack by sugars on proteins. If glycation gets out of hand many proteins are degraded or destroyed, proteins which are important for the proper functioning of the body. Protection against glycation declines with age leading to increasing glycation damage with increasing age. A critical enzyme involved in protection against glycation is "Glyoxalase 1". Using a model nematode system, Professor Paul Thornalley (University of Warwick) and his collaborators at the University of Heidelburg have shown for the first time that by enhancing levels of glyoxalase I the glycation process can be diminished and life can be extended by up to 40%. Similarly, by decreasing amounts of the enzyme they have shortened the lifespan of the nematodes. Professor Thornalley will present the results at the Society for Experimental Biology's Annual Main Meeting on Sunday 1st April.
"This work shows for the first time that this enzyme also protects proteins against damage by oxidation and nitration", says Professor Thornalley. The enzyme works by converting the damaging reactive products of glycation derived from glucose into harmless compounds. "This implies that glycation promotes multiple types of protein damage in ageing", says Prof Thornalley who will present his findings in the same session as plant scientist, Professor Dr Sudhir Sopory (International Center for Genetic Engineering and Biotechnology, New Delhi).
Professor Sopory has shown in tobacco and rice plants that increasing glyoxalase 1 enhances resistance to stress conditions, which demonstrates that the enzyme plays a similar role in both animal and plant systems in preventing protein damage.