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Science 21 November 1997:
Vol. 278. no. 5342, pp. 1404 - 1405
DOI: 10.1126/science.278.5342.1404b
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Research News

MEETING BRIEFS:
Protective Role for Prion Protein?

Marcia Barinaga

In spite of the body of work implicating rogue proteins called "prions" in a variety of fatal brain diseases, including the United Kingdom's bovine spongiform encephalopathy (BSE or "mad cow disease"), the story has some gaping holes. One of the largest: No one knows the function of the normal prion protein, known as PrPc. Data presented at the 27th annual meeting of the Society for Neuroscience in New Orleans last month may help remedy that. The new findings suggest that PrPc protects neurons by binding copper ions. When they run free, these reactive ions are highly toxic to cells. If the normal prion protein does help sequester the ions, the abnormal prion folding and clumping thought to cause BSE and other prion diseases could cause nerve cell death by interfering with this protective function.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)