You are seeing this message because your Web browser does not support basic Web standards. Find out more about why this message is appearing and what you can do to make your experience on this site better.


ABOUT JAMA
Advanced Search

Welcome   | My Account | E-mail Alerts | Access Rights | Sign In


  Vol. 283 No. 4, January 26, 2000 TABLE OF CONTENTS
  JAMA
  •  Online Features
  Quick Uptakes
 This Article
 •Full text
 •PDF
 •Send to a friend
 • Save in My Folder
 •Save to citation manager
 •Permissions
 Citing Articles
 •Contact me when this article is cited
 Related Content
 •Similar articles in JAMA

Prion Diseases Linked

Rebecca Voelker

JAMA. 2000;283:470.

Since this article does not have an abstract, we have provided the first 150 words of the full text and any section headings.

A new study offers the most compelling evidence to date that infectious proteins that cause bovine spongiform encephalopathy (BSE), or "mad cow" disease, also cause disease in humans.

The December 20, 1999, issue of the Proceedings of the National Academy of Sciences described laboratory experiments with transgenic mice that harbored genes for bovine prion protein, the culprit in BSE. When inoculated with prions from diseased cows or from humans with new-variant Creutzfeldt-Jakob disease (nvCJD), the mice developed the same neurologic symptoms during the same period of time—about 250 days. But when researchers inoculated transgenic mice with prions from sheep with scrapie, a related disease, a different pattern of illness occurred.

"These findings argue unequivocally that BSE and nvCJD are the same strain of prion," said Stephen DeArmond, MD, PhD, senior author and chief of neuropathology at the University of California at San Francisco. The emergence of nvCJD in . . . [Full Text of this Article]







HOME | CURRENT ISSUE | PAST ISSUES | TOPIC COLLECTIONS | CME | SUBMIT | SUBSCRIBE | HELP
CONDITIONS OF USE | PRIVACY POLICY | CONTACT US | SITE MAP
 
© 2000 American Medical Association. All Rights Reserved.