||Last Updated: Nov 17th, 2006 - 22:35:04
Prions' physical properties lead to different physiological effects
Brittleness is often seen as a sign of fragility. But in the case of infectious proteins called prions, brittleness makes for a tougher, more menacing pathogen. Howard Hughes Medical Institute researcher have discovered that brittle prion particles break more readily into new "seeds," which spread infection much more quickly.
Jun 29, 2006, 02:24
Seven UK cases of Creutzfeldt-Jakob disease associated with transplanted human tissue
Seven cases of Creutzfeldt-Jakob disease (CJD) associated with transplanted human tissue have occurred in the UK over a period of 33 years, reveals a study published ahead of print in the Journal of Neurology Neurosurgery and Psychiatry.
Apr 20, 2006, 16:50
First Successful Blood Test for 'Mad Cow' Disease Prions
Researchers at the University of Texas Medical Branch at Galveston (UTMB) have found a way to detect in blood the malformed proteins that cause "mad cow disease," the first time such "prions" have been detected biochemically in blood.
Aug 29, 2005, 23:22
Variant prion protein causes infection but no symptoms
Abnormal prion proteins are little understood disease agents involved in causing horrific brain-wasting diseases such as Creutzfeldt-Jacob disease in people, mad cow disease in cattle and chronic wasting disease in deer and elk. Now, new research suggests that a variant form of abnormal prion protein--one lacking an "anchor" into the cell membrane--may be unable to signal cells to start the lethal disease process, according to scientists at the Rocky Mountain Laboratories (RML), part of the National Institute of Allergy and Infectious Diseases (NIAID) of the National Institutes of Health.
Jun 3, 2005, 16:40
First mucosal prion vaccine tested in mice
NYU School of Medicine scientists have created the first active vaccine that can significantly delay and possibly prevent the onset of a brain disease in mice that is similar to mad cow disease. The new findings, published online this week in the journal Neuroscience, could provide a platform for the development of a vaccine to prevent a group of fatal brain diseases caused by unusual infectious particles called prions.
May 13, 2005, 20:08
Blocking apoptosis fails to stop prion damage in mouse brains
Researchers knew that prions, the misfolded proteins that cause mad cow disease and other brain disorders, were killing off a class of important brain cells in a transgenic mouse model. But when they found a way to rescue those cells, they were astonished to discover the mice still became sick.
Dec 23, 2004, 13:07
Mad cow prions piggyback on iron-storing proteins after surviving digestive juices
A new study from the Department of Pathology at Case Western Reserve University School of Medicine shows that the infectious version of prion proteins, the main culprits behind the human form of mad cow disease or variant Creutzfeldt-Jakob Disease (vCJD), are not destroyed by digestive enzymes found in the stomach. Furthermore, the study finds that the infectious prion proteins, also known as prions, cross the normally stringent intestinal barrier by riding piggyback on ferritin, a protein normally absorbed by the intestine and abundantly present in a typical meat dish. The study appears in the Dec. 15 issue of the Journal of Neuroscience.
Dec 16, 2004, 18:50
Testing Transepithelial Prion Protein Transport In Vitro
The discovery of the "mad cow" variant of Creutzfeldt–Jakob disease (CJD) as a foodborne illness not only created a worldwide scare but also focused attention on the mechanisms of transmission of the infective agent, the scrapie prion protein (PrPSc).
Dec 15, 2004, 18:45