RESOUR> [NetGold] BIOCHEMISTRY: PRIONS : ARTICLE: Mad Cow Mechanism May Be Integral to Storing Memory

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Net Happenings - From Educational CyberPlayGround
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Date: Wed, 21 Jan 2004 15:45:31 -0500 (EST)
From: David P. Dillard <jwne@xxxxxxxxxx>
Reply-To: NetGold@xxxxxxxxxxxxxxx
To: NetGold <NetGold@xxxxxxxxxxxxxxx>
Subject: [NetGold] BIOCHEMISTRY: PRIONS : ARTICLE: Mad Cow Mechanism May Be
     Integral to Storing Memory

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@xxxxxxxxxx

Columbia University Contact: Annie Bayne
Phone: 212.305.3900
E-mail: as862@xxxxxxxxxxxx

Mad Cow Mechanism May Be Integral to Storing Memory
<http://www.whitehead.mit.edu/nap/features/nap_feature_memory.html>

"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
jwne@xxxxxxxxxxxxxxxx
<http://groups.yahoo.com/group/NetGold/>
<http://www.edu-cyberpg.com/ringleaders/davidd.html>
<http://www.kovacs.com/medref-l/medref-l.html>

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