Literature: A-K ; L-Z ; subject area
Compiled by: Julian Thorpe
Neurofibrillary Tangles
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Please Note: Due to time constraints, the text part of this page has not been updated for some time. However, references are added reasonably frequently. |
TEM Images
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| AD Tangle | FTD Tangle |
PiD Pick Body |
CBD Tangle 1 |
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|
CBD Tangle 2 |
Isolated Tau Filaments |
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 | Intracellular
neurofibrillary tangles (NFT)are - along with extracellular
deposits of beta-amyloid plaques
- one of the two histopathological hallmark
features of AD-affected brain tissue. Understanding how the
plaques and tangles are interrelated is difficult (and see
Inter-relationship of Plaques and Tangles
): some believe that plaques are directly toxic
to neurons, but NFTs often occur at sites distant to plaques.
"The number of neurofibrillary tangles is tightly linked to the
degree of dementia, suggesting that the formation of neurofibrillary
tangles more directly correlates with neuronal dysfunction
(than beta-amyloid plaques) " (from review article:
Brion, 1988 ).
A loss of synapses (Terry et al., 1991
) correlates with NFT formation (Arriagada et al., 1992
). The NFTs have also been shown to proceed in a well-defined
spatial and temporal fashion so that they are therefore useful in
defining AD stages ( Braak and Braak, 1991; Braak et al., 1994
). |
| Please also see Plaque
Relationship with Tangles
. |
| Recently a group of frontotemporal dementias
with parkinsonism linked to chromosome 17
(FTDP-17)
has been shown to be caused by
tau
gene mutations. Some of these mutations are
missense (producing altered tau proteins) while others affect pre-mRNA splicing (changing the balance between tau
isoforms).
These diseases usually occur in the complete absence of
beta-amyloid
deposits. The tau filaments have different
appearances with different mutations. It has been suggested
(Crowther and Goedert, 2000) that these mutations may reveal
important information regarding the large number of sporadic cases
of AD. |
| NFTs are composed of bundles of
paired helical
filaments
(PHF), the
major protein subunit of which is the microtubule-associated
protein (MAP),
tau
(Iqbal et al. 1989; Lee et al. 1991 ).
Can exist as extracellular (or 'ghost') tangles. FTIR and X-ray
diffraction studies have shown some evidence for secondary structure
such as beta sheets (Mandelkow et al., 1995) . See
Friedhoff et al. (2000) for a recent review of the
structure and conformation of tau protein and its assembly into PHFs. And please visit
Luc Buee's site
(at the 'Institut National de la Sante et
de la Recherche Medical') for detail on tau protein in relation
to neurodegeneration. |
| Tau in PHF
is in a different
form from that in normal neurones, being abnormally hyperphosphorylated,
ubiquitinated, proteolytically-processed and aggregated into
filaments (ubiquitination and proteolysis are probably secondary
events, reflecting the cell's attempt to eliminate the protein).
This hyperphosphorylated tau is unable to bind to
microtubules
and therefore unable to promote or maintain
microtubule assembly (Iqbal et al. 1998). Evidence
from many studies has indicated that hyperphosphorylation of
tau
is responsible for its loss of biological
activity, its resistance to proteolytic degradation, and probably
plays a key role in neurofibrillary degeneration in AD patients
(reviewed in Iqbal et al. 1998). Certain tau constructs
(comprising mainly the repeat, microtubule-binding region)
can associate into PHFs similar to AD PHFs. |
| It is still
unclear how hyperphosphorylation of tau occurs in AD brain
, but this probably reflects a combination of regulation at
the level of both increased kinase
and decreased phosphatase
activity (Gong et al. 2000). |
| It is also unclear whether microtubules
decay
because tau becomes detached from them or if
microtubules
decay for another reason, leaving the tau
free to interact with other proteins (including itself) and
produce PHFs. |
| Recently, evidence of an involvement of Pin1 in NFTs has been shown (Lu et al. 1999a). Elevated levels of Pin1 binding to the NFT-rich cytoplasm of AD-affected, compared with healthy, neurons were reported (at the light microscope level). These authors showed that Pin1 binds to only one phosphorylated threonine-proline motif in tau and that the protein co-purified with the PHFs. They suggested that the resultant depletion of available soluble Pin1 in the AD-affected neurones could contribute to cell death. We (Thorpe et al., 2001) have recently extended this work to the EM level and confirmed these results. |
(These journals include: Neurology, Neurobiology of Disease, Journal of Neurochemistry, Alzheimer's Disease Review)
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