For a while now I've been contemplating the subject of my blog. So far it has been split into two broad sections of learning and yearning. I have decided to change my blog into a more scientifically oriented area.
With that said, I will provide medical information for all types of situations. More geared to the mind and brain, information about disorders and psychology will be given.
Today I will be writing about Mad Cow Disease.
ScienceDaily (Jan. 11, 2011) — Scientists at the University of Kentucky have discovered that plasminogen, a protein used by the body to break up blood clots, speeds up the progress of prion diseases such as mad cow disease.As you can see, this study is very recent.
This finding makes plasminogen a promising new target for the development of drugs to treat prion diseases in humans and animals, says study senior author Chongsuk Ryou, a researcher at the UK Sanders-Brown Center on Aging and professor of microbiology, immunology and molecular genetics in the UK College of Medicine.
"I hope that our study will aid in developing therapy for prion diseases, which will ultimately improve the quality of life of patients suffering from prion diseases," Ryou said. "Since prion diseases can lay undetected for decades, delaying the ability of the disease-associated prion protein to replicate by targeting the cofactor of the process could be a monumental implication for treatment."
The study was reported in the December issue of The FASEB Journal, published by the Federation of American Societies for Experimental Biology.
Ryou's team used simple test-tube reactions to multiply disease-associated prion proteins. The reactions were conducted in the presence or absence of plasminogen. They also found that the natural replication of the prions was stimulated by plasminogen in animal cells.
"Rogue prions are one of nature's most interesting, deadly and least understood biological freak shows," says Dr. Gerald Weissmann, editor-in-chief of The FASEB Journal. "They are neither virus nor bacteria, but they kill or harm you just the same. By showing how prions hijack our own clot-busting machinery, this work points to a new target for anti-prion therapy."
According to the U.S. National Institute of Allergy and Infectious Diseases, prion diseases are a related group of rare, fatal brain diseases that affect animals and humans. The diseases are characterized by certain misshapen protein molecules that appear in brain tissue. Normal forms of these prion protein molecules reside on the surface of many types of cells, including brain cells, but scientists do not understand what normal prion protein does. On the other hand, scientists believe that abnormal prion protein, which clumps together and accumulates in brain tissue, is the likely cause of the brain damage that occurs. Scientists do not have a good understanding of what causes the normal prion protein to take on the misshapen abnormal form.
Prion diseases are also known as transmissible spongiform encephalopathies, and include bovine spongiform encephalopathy ("mad cow" disease) in cattle; Creutzfeldt-Jakob disease in humans; scrapie in sheep; and chronic wasting disease in deer and elk. These proteins may be spread through certain types of contact with infected tissue, body fluids, and possibly, contaminated medical instruments.
The co-author of the study is Charles E. Mays, formerly a graduate student in the Ryou labI'm sure we all remember that time when Mad Cow disease was of extreme relevance. But little did we know that research is still conducted on the subject.
Even though the disease has settled down considerably, study is still focused to develop medicine that can improve the quality of life for patients suffering from related diseases.
Prions can turn a normal protein into a misfolded form. One prion in mammals promotes progressive neurodegenerative disorders like "mad cow" disease that often prove fatal. But how this process happens remains an open question for scientists.Prions have been found to exist in a wide range of organisms. Those in brewer's yeast, which researchers like Liebman study, provide critical insight into how prions work.Prion proteins in yeast aggregate, while non-prion proteins do not. Aggregation of new prions happens spontaneously -- but, in the natural world, very slowly.Anita Manogaran, a former UIC research assistant professor in biological sciences, working with Liebman, sped-up prion formation to identify genes important in the process. The researchers were also able to monitor different stages of prion appearance by tagging prion proteins with another protein that fluoresces green. Cells in the process of forming prions had fluorescent rings, which could give rise to cells with prions."We learned there are some genes important for the generation of prions," Liebman said.Some 400 yeast genes were screened for the ability to prevent the new appearance of yeast prion proteins."Through a number of screens, we came down to a much smaller number (of genes) that inhibited prion appearance," Liebman said. These genes fell into two classes -- one that could still make the rings, which is the hallmark of the beginning of prion aggregation. But the other class of genes had trouble forming rings, Liebman said.Liebman and Manogaran also looked beyond new prion formation to see if these same genes had an effect on toxicity associated with a protein that causes Huntington's disease -- a fatal human neurodegenerative disorder."We found that genes that could make rings also were more toxic in the presence of the Huntington's disease protein," Liebman said. "If no rings were made, they were less toxic."The full implications of the findings are not yet understood, Liebman cautioned."The more we understand about these mechanisms and the genes that are involved, the more we'll be able to understand the new appearance of prion disease -- like Creutzfeldt-Jakob and 'mad cow' -- and Huntington's disease. The more we understand what affects toxicity, the more we'll understand why these are toxic."The findings were reported in the May 19 issue of PLoS Genetics.Manogaran, now at the University of Wisconsin-Milwaukee, UIC research assistant Joo Hong and former UIC undergraduate student Joan Hufana worked with Liebman on the project. Other co-authors of the paper include Jens Tyedmers of the University of Heidelberg and Susan Lindquist of the Massachusetts Institute of Technology.
As you can see here, more findings are being made. Thank you for reading. Please, if I may, what are your thoughts of researching diseases that are not of extreme relevance? Do you think they are an efficient way to use money? In these economic times, is it necessary to spend the money on such diseases?