Scientists unravel evolutionary origins of prion disease gene.Byline: ANI Washington, Sept 29 (ANI): Scientists claim to have unravelled the evolutionary origin of the prion gene that is responsible for causing diseases such as bovine spongiform encephalopathy bovine spongiform encephalopathy: see prion. (BSE See Bombay Stock Exchange. BSE See Boston Stock Exchange (BSE). ), also known as "mad cow disease mad cow disease: see prion. mad cow disease or bovine spongiform encephalopathy (BSE) Fatal neurodegenerative disease of cattle. Symptoms include behavioral changes (e.g. ." Diseased prion proteins are responsible for the fatal neurodegenerative Creutzfeldt-Jakob disease (CJD) in humans, and BSE, scrapie scrapie: see prion. and chronic wasting disease Noun 1. chronic wasting disease - a wildlife disease (akin to bovine spongiform encephalitis) that affects deer and elk animal disease - a disease that typically does not affect human beings (CWD) in livestock. The researchers say that the new study may provide insights into the origins and underlying constraints of the conformational changes associated with prion diseases. "The prion protein was discovered over twenty years ago and has been studied intensively. Nobody, however, knew its evolutionary origin and much confusion surrounds its physiological function," said principal investigator Gerold Schmitt-Ulms (Centre for Research in Neurodegenerative Diseases; Department of Laboratory Medicine and Pathobiology pathobiology /patho·bi·ol·o·gy/ (-bi-ol´ah-je) pathology. path·o·bi·ol·o·gy n. The study or practice of pathology with greater emphasis on the biological than on the medical aspects. , U of T) The team's analysis suggests that the prion gene is descended from the more ancient ZIP family of metal ion transporters. The members of ZIP protein family are well known for their ability to transport zinc and other metals across cell membranes. Schmitt-Ulms has found that prion and ZIP proteins contain extensive stretches of similar amino acid sequence. The researchers next documented that the respective segments within ZIP and prion proteins are computationally predicted to acquire a highly similar three-dimensional structure. Finally, the team uncovered multiple additional commonalities between ZIP and prion proteins, which led them to conclude these molecules, are evolutionarily related. The study was published in the online journal PLoS ONE. (ANI) Copyright 2009 Asian News International The Asian News International (ANI) agency provides multimedia news to China and 50 bureaus in India. It covers virtually all of South Asia since its foundation and presently claims, on its official website, to be the leading South Asia-wide news agency. (ANI) - All Rights Reserved. Provided by Syndigate.info an Albawaba.com company |
|
||||||||||||||

Printer friendly
Cite/link
Email
Feedback
Reader Opinion