Literature: A-K ; L-Z ; subject area
Compiled by: Julian Thorpe
Neurofibrillary Tangles: Research Results
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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. |
General
 | The microtubule-associated protein (MAP), tau is the major protein subunit of NFTs (Iqbal et al. 1989; Lee et al. 1991). |
| Tau in PHF is in a different form from that in normal neurones, being abnormally hyperphosphorylated and aggregated into filaments. 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). |
| It is still unclear exactly 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). |
| Can exist as extracellular (or 'ghost') tangles. These may be separated into small bundles of abnormal straight filaments by invading astrocytic processes. |
| The recent finding that mutations in the tau gene are responsible for frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) has provided convincing evidence that tau protein plays a key role in neurodegeneration (Hutton et al., 1998 ) and suggests that distinct sets of tau isoforms expressed in different neuronal populations could lead to different pathologies (see review: Buee et al., 2000 ). |
Some Research Results (in chronological order)
| NFTs have been found in the adrenal medulla (pheochromocytoma cells) removed from a patient with no obvious AD (Izumiyama et al., 1990). . |
| Lichtenberg-Kraag et al. (1992) looked at the phosphorylation of tau from AD paired helical filaments (PHF), normal brain and recombinant isoforms. Their work suggested the involvement of a serine/proline kinase in the phosphorylation of tau which leads to PHF formation. |
| Hugon and co-workers (for overview see Hugon et al., 1995 ) studied the effects of glutamate (a major excitatory neurotransmitter in human brain but can also be a neurotoxin) on neuronal cultures. Glutamate has been implicated in many neurodegenerative disorders, including AD. It is able to produce an intracellular signal transduction in neurons which leads to protein phosphorylations. Their work showed that glutamate produced a rapid, transient modification of tau involving the phosphorylation of serine 202. This phosphorylation site is present in fetal and AD PHF tau. |
| Kosik and co-workers (for overview see Kosik et al., 1995 ) have found that a secreted fragment of APP can stimulate MAP kinase in a ras-dependent manner, leading to tau phosphorylation. Their results suggest an interaction of tau with actin in addition to microtubules . |
| Roses et al. (1996) suggest that apolipoprotein E (apoE) may have a role in the prevention of formation of PHFs. They localised apoE to the neuronal cytoplasm and suggested that apoE3 (and apoE2) prevented PHF formation by interacting with the microtubule binding domain of tau. In this way it also protects the site for microtubule stabilising interactions with beta-tubulin. |
| Grynspan et al. (1997) have published results which implicate calpain II (and a concomitant perturbation to the calcium balance within neurons) in NFTs (neuritic plaques, and neuropil threads) and AD pathogenesis. The calpain proteases can influence signalling pathways and regulate the organisation of the cytoskeleton . |
| Norlund et al. (1999) suggest that increased levels of transglutaminase-induced epsilon-(gamma-glutamyl)lysine bonds (in AD brain) lead to the formation of high molecular weight tau polymers. This would create the stable NFTs which are resistant to degradation and proteolytic digestion. (The NF-M and NF-H proteins were also found to contain increased levels of these bonds in AD brain.) |
| Interestingly, Holzer et al. (1999), have shown that in the peripheral nervous system - the sciatic nerve - hyperphosphorylation of tau in AD was not accompanied by PHF formation. |
| Alvarez et al. (1999) used cultured rat hippocampal cells to study the tau protein kinase II system (TPK II; involving cdk5 and p35). They showed that fibrillary beta-amyloid increased cdk5 activity, while a cdk5 inhibitor and an (cdk5) antisense probe protected the cells from beta-amyloid -induced neurotoxic damage. They therefore concluded that cdk5 plays a major role in the molecular path leading to the neurodegenerative process. |
| Vickers et al. (2000),in a review article, note that the the profound cytoskeletal alterations (including NFTs) associated with AD may result from a physically-injurious effect of beta-amyloid plaques because the earliest symptoms of neuronal pathology associated with the latter are similar to cellular changes observed after structural injury to axons. |
| Schwab et al. (2000) have shown (by immunohistochemistry) that casein kinase 1 delta (Cki delta) is associated with granulovacuolar bodies and tau-containing NFTs in AD (and a number of other neurodegenerative diseases). They suggested that this association with 'its apparent substrate' tau could be indicative of Cki delta's involvement in the abnormal processing of tau. |
| Thorpe et al. (2001) have demonstrated enhanced levels of Pin1 protein binding to NFTs in AD brain tissue. This confirms the (light microscopy) results of Lu et al. (1999). It is suggested that Pin1 depletion from the nucleus (when it is redirected to the NFTs in the cytoplasm) may ultimately contribute to neuronal cell death. |
| Ljungberg et al. (2002) have shown that truncated apoE forms tangle-like structures in a neuronal cell line. |
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