General Hospital, in Charlestown. University of California, Irvine, neurobiologist
Frank M. LaFerla has been investigating
this connection. He recently reported that
chronic copper exposure accelerates tau
phosphorylation—possibly through kinase
activation—and amyloid-β production in
mice (J. Neurochem. 2009, 108, 1550).
Industry Exhibition and Conference
2010 China International Coal Chemical
Date : 25-27th,August 2010 Venue: National Convention Center, Beijing,China
Sponsor: China Petroleum and Chemical Industry Association (CPCIA)
Why you should attend this event?
GLYCOSYLATION, which attaches sugars
to tau, also appears to promote hyperphosphorylation and has been detected in
Alzheimer’s cases, Leonard Petrucelli, a
molecular neuroscientist at Mayo Clinic’s
Jacksonville, Fla., facility, notes in a review
about tau ( Mol. Neurodegener. 2009,
4, 13).
Another factor that can increase phosphorylation is aging-associated oxidative
damage to kinases, Lee notes. Oxidation
can also damage tau directly, making it
less able to bind to microtubules and more
prone to aggregate, he adds.
Furthermore, cells become less able to
dispose of damaged tau as they age. As tau
aggregates accumulate, they may block the
intracellular transport of other biomolecules needed for the proper functioning of
neurons, Petrucelli says.
In sum, there are numerous ways for
tau to go bad and to disrupt its neuronal
host. Complicating the situation further,
tau trouble doesn’t develop in isolation. In
many Alzheimer’s patients, for example, tau
pathology is likely preceded and indeed exacerbated by amyloid-β pathology, suggests
Einar M. Sigurdsson, a neuroscientist at
New York University School of Medicine. In
turn, tau pathology may make neurons more
vulnerable to damage by amyloid-β.
Sigurdsson thinks accumulation of
amyloid-β inside or outside neurons
damages synapses, which start to retract.
Hyperphosphorylated tau then begins to
build up inside the afflicted neurons, and
the synapses deteriorate further. The cells
eventually die, leaving behind insoluble tau
tangles that serve as a kind of tombstone
for the vanished neurons, Wilcock says.
Amyloid-β and tau appear to share some
characteristics. Amyloid-β plaques were
for many years thought to be the most
harmful form of amyloid-β. But an increasingly popular notion posits that amyloid
plaques may represent the end result of
the brain’s effort to collect and sequester smaller but more toxic aggregates of
amyloid-β, such as oligomers. Likewise,
some researchers believe that soluble aggregates of tau oligomers are more likely
to lead to neuronal dysfunction and death
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Organizing Committee
Contact: Michael Zhao , Zada Huang
Tel:+86-10-84292984 64298374
Fax:+86-10-84292987
E-mail: zhj@ccpitchem.org.cn
www.ciccec.com
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