Medical News

[ 'Lifeless' Prions Capable Of Evolutionary Change And Adaptation Shown By Scripps Florida Scientists ]

'Lifeless' Prions Capable Of Evolutionary Change And Adaptation Shown By Scripps Florida Scientists

Scientists from The Scripps Research Institute have determined for the first time that prions, bits of infectious protein devoid of DNA or RNA that can cause fatal neurodegenerative disease, are capable of Darwinian evolution. The study from Scripps Florida in Jupiter shows that prions can develop large numbers of mutations at the protein level and, through natural selection, these mutations can eventually bring about such evolutionary adaptations as drug resistance, a phenomenon previously known to occur only in bacteria and viruses. These breakthrough findings also suggest that the normal prion protein - which occurs naturally in human cells - may prove to be a more effective therapeutic target than its abnormal toxic relation. The study was published in the December 31, 2009 issue of the journal Science Express, an advance, online edition of the prestigious journal Science.

CDC Assesses Potential Human Exposure To Prion Diseases Study Results Reported In The Journal Of The American Dietetic Association

Researchers from the Centers for Disease Control and Prevention (CDC) have examined the potential for human exposure to prion diseases, looking at hunting, venison consumption, and travel to areas in which prion diseases have been reported in animals. Three prion diseases in particular - bovine spongiform encephalopathy (BSE or "Mad Cow Disease"), variant Creutzfeldt-Jakob disease (vCJD), and chronic wasting disease (CWD) - were specified in the investigation. The results of this investigation are published in the June issue of the Journal of the American Dietetic Association. "While prion diseases are rare, they are generally fatal for anyone who becomes infected. More than anything else, the results of this study support the need for continued surveillance of prion diseases, " commented lead investigator Joseph Y.

ProMetic Life Sciences Inc. vCJD Infection: A Continuing Threat To Public Health

Variant Creutzfeldt-Jakob Disease ("vCJD") remains 'a very real and continuing threat to public health and recent developments strongly support predictions of second and third waves of long incubation vCJD' commented Dr Robert Rohwer, Director, Molecular Neurovirology Laboratory and Associate Professor of Neurology, University of Maryland, Baltimore, U.S., speaking at today's GovNet Communications' Patient Safety 2010 Conference held at the QEII Conference Centre in London, UK. Dr Rohwer went on to emphasize the urgency of implementing universal protective measures to arrest human to human transmission through blood transfusion and blood products. Dr Rohwer highlighted recent research and developments showing how vCJD transmission risk remains 'very real'. He discussed the 'significant challenges' associated with detecting the prion in blood and urged implementation of proven infectivity removal technologies to protect blood.

Prion Protein In Cell Culture

The fatal brain disease Creutzfeldt-Jakob in humans, BSE (bovine spongiform encephalopathy) in cattle and scrapie in sheep are so-called prion diseases, whereby one of the body's normal proteins, the prion protein PrPc misfolds into a pathogenic form: PrPSc. In spite of several years of extensive research, little is still known about what actually happens in this process. In spite of the fact that PrP is one of most intensely studied proteins in the human genome, its physiological function is still unknown. The pathogenic variant PrPSc arises as a result of changes in the structural folding of PrPc. We need to know more about how PrPc is expressed and treated in cells in order to understand how the misfolding of PrPc occurs and why cells die as a result. In the course of the work connected with his PhD, Christoffer Lund has therefore carried out detailed studies of cell cultures of normal PrP in sheep.

Prestigious Dementia Research Honor For Two UCSF Scientists

Two UCSF scientists have been selected for the American Academy of Neurology's prestigious Potamkin Prize, for their "outstanding achievements" in research on dementias. Bruce Miller, MD, W. & Mary Margaret Clausen Distinguished Professor of Neurology, and Lennart Mucke, MD, Joseph B. Martin Distinguished Professor of Neuroscience and director of the Gladstone Institute of Neurological Disease, will receive the honor for their major contributions to the understanding of the causes of, and treatment strategies for, frontotemporal lobar degeneration, Alzheimer's disease and related diseases. They will receive the prize on April 15, 2010 at the AAN's annual meeting. The $100, 000 prize is to be used for continuing research on dementias. As director of UCSF's Memory and Aging Center, Miller oversees a program that provides clinical care and conducts clinical research on all forms of dementia.

Fast: [10]

Medical News © Nanda
Designer Damodar