“Rice Responsible For Asians' Alcohol Flush Reaction - Redorbit.com” plus 1 more |
| Rice Responsible For Asians' Alcohol Flush Reaction - Redorbit.com Posted: 20 Jan 2010 10:54 AM PST Posted on: Wednesday, 20 January 2010, 13:33 CST The mutation responsible for the alcohol flush reaction, an unpleasant response to alcohol that is relatively common in people of Asian descent, may have occurred following the domestication of rice. Researchers writing in the open access journal BMC Evolutionary Biology traced the history of the version of the gene responsible, finding that the ADH1B*47His allele appeared around the same time that rice was first cultivated in southern China. Bing Su, from the Chinese Academy of Sciences, China, worked with a team of researchers to study 38 populations (2,275 individuals) including Han Chinese, Tibetan and other ethnic populations across China. He said, "Our molecular dating suggests that the emergence of the ADH1B*47His allele occurred about 10,000-7,000 years ago. The geographic distribution of the allele in East Asia is also consistent with the unearthed culture relic sites of rice domestication in China, suggesting that distribution of the alcohol flush mutation can be explained by the origin and expansion of the Neolithic rice culture. This is one of the few cases reported demonstrating the genetic adaptation of human populations to the dramatic changes in agriculture and diet during Neolithic times". Rice was fermented to gain the benefits of ethanol's combined analgesic, disinfectant and profound mind-altering effects. In addition, fermentation can help to preserve and enhance the nutritional value of food and drink. Su and his colleagues believe that the flushing response may be an adaptation to counter the negative effects of alcohol consumption. They write, "Individuals carrying ADH1B*47His have a lower risk for alcoholism, as the unpleasant reaction they experience can influence drinking behavior and so protect them from overconsumption. The allele can also protect their organs from the damage caused by alcohol consumption". --- On the Net: Five Filters featured article: Chilcot Inquiry. Available tools: PDF Newspaper, Full Text RSS, Term Extraction. |
| Iowa State University researcher discovers Ebola's deadly secret - Science Centric Posted: 20 Jan 2010 05:10 AM PST Research at Iowa State University has led scientists to uncover how the deadly Zaire Ebola virus decoys cells and eventually kills them. A research team led by Gaya Amarasinghe, an assistant professor of biochemistry, biophysics and molecular biology, had previously solved the structure of a critical part of an Ebola protein known as VP35, which is involved in host immune suppression. Amarasinghe and his research team now know how VP35 is able to do it. When most viruses invade a cell, they start to make RNA in order to replicate. When the healthy host cell senses the replicating RNA, the host cell starts to activate anti-viral defences that halt replication and eventually help clear the viral infections. What Amarasinghe and his group have discovered is that Ebola virus encoded VP35 protein actually masks the replicating viral ribonucleic acid (RNA), so the cell doesn't recognise that there is an invading virus. One of the reasons Ebola, in particular the strain isolated from Zaire, is so deadly is that the host cells don't have any immune response when the virus enters the cell, said Amarasinghe. 'The question with Ebola has always been 'Why can't host cells mount an immune response against the Ebola virus, like they do against other viruses?'' he said. 'The answer is, 'If the cell doesn't know that there's an infection, it cannot build up any response.' So our work really gets at the mechanism Ebola infection and immune evasion.' The collaborative approach taken by Amarasinghe enabled him to team up with virologist Christopher Basler at the Mt. Sinai School of Medicine, New York City, to investigate how the structural findings match up with how these proteins function inside the cell. 'Our initial structure that we solved in 2008 was key to expanding our knowledge, but the structure was just part of the equation, and when we put it together with the functional studies, everything made sense,' Amarasinghe said. The current research describing the protein-RNA complex structure, which was solved by using non-infectious VP35 protein, and associated functional studies is published in the current issue of the journal Nature Structural and Molecular Biology and is available as an advanced online publication. These findings build on Amarasinghe's research published in the journal Proceedings of the National Academy of Sciences of the United States of America last January. In his current research, Amarasinghe focused on a specific part of the Zaire Ebola VP35 protein that he thought looked unusual. As testing results came in, he found that the suspect region of the protein was binding with, or neutralising, the part of the host cell that triggers the immune system in the cell. 'The interesting thing about the Ebola virus is that it doesn't let cells even get started to defend themselves,' he said. 'This hides the (viral) RNA from being recognised by the host cell. This is a powerful immune evasion mechanism.' Source: Iowa State UniversityFive Filters featured article: Chilcot Inquiry. Available tools: PDF Newspaper, Full Text RSS, Term Extraction. |
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