BIOCHEMISTRY: PRIONS : ARTICLE: Mad Cow Mechanism May Be Integral to
Storing Memory

Whitehead Institute Contacts: Kelli Whitlock or David Cameron
Phone: 617.258.5183
E-mail: newsroom @ wi.mit.edu

Columbia University Contact: Annie Bayne
Phone: 212.305.3900
E-mail: as862 @ columbia.edu

Mad Cow Mechanism May Be Integral to Storing Memory

"CAMBRIDGE, Mass. (Dec. 24, 2003) Scientists have discovered a new
process for how memories might be stored, a finding that could help
explain one of the least-understood activities of the brain. Whats
more, the key player in this process is a protein that acts just
like a prion a class of proteins that includes the deadly agents
involved in neurodegenerative conditions such as mad cow disease.

The study, published as two papers in the Dec. 26 issue of the
journal Cell, suggests that this protein does its good work while in
a prion state, contradicting a widely held belief that a protein
that has prion activity is toxic or at least doesnt function
properly.

For a while weve known quite a bit about how memory works, but weve
had no clear concept of what the key storage device is, says
Whitehead Institute for Biomedical Research Director Susan
Lindquist, who coauthored the study with neurobiologist Eric Kandel
at Columbia University. This study suggests what the storage device
might be but its such a surprising suggestion to find that a prion-
like activity may be involved.

Central to a proteins function is its shape, and most proteins
maintain only one shape throughout their lifetime. Prions, on the
other hand, are proteins that can suddenly alter their shape, or
misfold. But more than just misfolding themselves, they influence
other proteins of the same type to do the same. In all known cases,
the proteins in these misfolded clusters cease their normal function
and either die or are deadly to the cell and ultimately to the
organism.

For this reason, Kausik Si, a postdoc in Kandels lab, was surprised
to find that a protein related to maintaining long-term memory
contained certain distinct prion signatures. The protein, CPEB,
resides in central-nervous-system synapses, the junctions that
connect neurons in the brain. Memories are contained within that
intricate network of approximately 1 trillion neurons and their
synapses. With experience and learning, new junctions form and
others are strengthened. CPEB synthesizes proteins that strengthen
such synapses as memories are formed, enabling the synapses to
retain those memories over long periods.

For the study, the team extracted the CPEB protein from a sea slug.
This lowly creature has achieved high status in neurobiology because
its neurons are so big, they can be manipulated and turned into
unusually powerful investigative tools. The researchers fused this
CPEB to other proteins that would serve as reporters of activity,
and then observed its behavior in a variety of yeast models. The
researchers discovered that CPEB altered its form and caused other
proteins to follow functioning exactly like a prion. A second
unexpected finding was that CPEB carried out its normal function
protein synthesis when it was in its prion state.

This is remarkable not just because the protein executes a positive
function in its prion-like state, says Lindquist, who also is
professor of biology at the Massachusetts Institute of Technology.
It also indicates that prions arent just oddballs of nature but
might participate in fundamental processes."

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The full article may be read at the URL above.

A list or resources and links related to this research report is
provided at the end of this document.

Sincerely,
David Dillard
Temple University
(215) 204 - 4584

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