They 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.
Prions are a modified form of normal proteins, the prion proteins, which become infectious and accumulate in the nervous system causing fatal neurodegenerative disease. Variant CJD results from eating contaminated beef products from cattle infected with mad cow disease. To date, 155 cases of confirmed and probable vCJD in the world have been reported, and it is unclear how many others are carrying the infection.
George Stamatis | EurekAlert!
Amputees can learn to control a robotic arm with their minds
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The miniaturization of the current technology of storage media is hindered by fundamental limits of quantum mechanics. A new approach consists in using so-called spin-crossover molecules as the smallest possible storage unit. Similar to normal hard drives, these special molecules can save information via their magnetic state. A research team from Kiel University has now managed to successfully place a new class of spin-crossover molecules onto a surface and to improve the molecule’s storage capacity. The storage density of conventional hard drives could therefore theoretically be increased by more than one hundred fold. The study has been published in the scientific journal Nano Letters.
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