Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
enabled [disable] Abstract
Number of results

Results found: 3

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

Search:
in the keywords:  BSE
help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
1
Content available remote

Bovine spongiform encephalopathy Update

100%
EN
Bovine spongiform encephalopathy (BSE) is a zoonosis being the origin of variant Creutzfeldt-Jakob disease and an important cattle disease in its own right. Countries have been slow to learn the importance of protecting, not only their cattle populations, but also their human populations. Since 2000, several additional European countries have reported BSE in native-born stock and this has led to a concern about the BSE status of countries that have imported cattle and cattle products from infected countries. Extensive feed and offal bans and application of newly-developed, ?Rapid? tests for prion protein in central nervous tissue of targeted, high-risk animals and slaughter cattle over 30 months old now provides the tools whereby the public are fully protected and BSE can be eradicated.
EN
Prion diseases (for example: scrape of sheep, BSE, CJD of humans) are among the most notable central nervous system degenerative disorders caused by the accumulation of modified cellular protein. The conversion of PrP(C) (the normal cellular protein) into PrP(Sc) (the abnormal disease-causing isoform) involves a conformation change whereby the ?-helical content diminishes and the amount of ? sheet increases. PrP (Sc) is partially resistant to proteases, temperature, high and low pH. Because the incidence of prion diseases is due to several factors, various efforts need to be taken to reduce the scale and consequences of the disease. They include post-mortem and in vivo diagnosis and prophylactics, i.e. monitoring of animals and feed control.
EN
Prions are devoid of nucleic acids and they are composed mainly or exclusively of protein PrPSC, that is a conformational variant of the normal cellular prion protein PrPC, encoded by a chromosomal gene. Conversion of PrPC into PrPSC is a posttranslational process which is accompanied by the acquisition of high b-sheet content. Human prion diseases may be of sporadic, genetic or infectious origin. Human activity caused a 'mad cow disease' epidemic, iatrogenic Creutzfeldt-Jakob disease (CJD), and lately, a new variant of CJD, which is thought to be a result of transmission of bovine prions to humans. Prion diseases are always fatal, and there is a need to develop effective methods of prevention and therapy for these disorders.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.