Alzheimer's Disease and Frontotemporal Dementias

A Review with Particular Reference to Pin1 Protein



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Compiled by: Julian Thorpe



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.

The disruption of the cytoskeleton is a key feature of AD, so here is some general background:
The cytoskeleton is a complex mixture of proteins which together act to maintain cell shape and facilitate the movement of particles and organelles within the cytoplasm. The overall cytoskeletal structure is very dynamic as the component proteins may go through rapid cycles of polymerisation and disassembly. These proteins may be broadly grouped into 3 types:

1. Microfilaments:

5-7nm thick filaments of F-actin which function as contractile elements when associated with the complementary contractile protein myosin (to form actinomyosin ). May also be laterally associated with other proteins and sometimes anchored to membranes.

2. Intermediate filaments:
N.B. See  Intermediate filaments of neural/glial cells for more detail on intermediate filaments specific to neurons and glial cells, research results, etc.
So named because of their intermediate size (c. 10nm) between the microfilaments and microtubules.
Contain a characteristic central alpha-helical domain that forms coiled-coil rods. The latter can assemble into filaments.
Responsible for cell shape maintenance and conferring some strength and rigidity.
The protein subunits of intermediate filaments show considerable diversity and tissue specificity.


Type I and II:keratins of epithelial cells.
Type III: vimentin (mesenchymal cells); desmin (muscle); glial fibrillary acidic protein (astroglia); peripherin (peripheral neurons)
Type IV: neurofilaments of neuronal cell types
Type V: nuclear lammins.

3. Microtubules:

They are c. 25nm in width and composed of tubulin .
Involved in the maintenance of cell shape and in the movement of organelles, cell products and chromosomes during cell division. They are also the components of cilia and flagella.
Play a crucial role in neuronal development as neuritic outgrowth is dependent upon microtubule assembly ( Yamada et al., 1970 ).
Microtubules and their associated proteins also form the basis of axonal transport.
The microtubules are associated with other proteins such as dynein and kinesin and also the MAPs ( microtubule-associated proteins ). Of the latter MAP1A and 1B (c. 350kD) and MAP2A and 2B (270kD) form projections from microtubules within brain cells. MAP2 is a distinguishing protein within axonal processes of neurones.
The MAP tau is as an elongated molecule (about 35-50 nm long, dependent on the isoform) without recognizable secondary structure ( Mandelkow et al., 1995). Its role may be likened to that of  'ties' which hold the microtubular tracks in place. There is a mixture of up to 6 isoforms in the human brain which are generated from a single gene by alternative splicing. Range in size from 352-441 amino acids ( Goedert et al., 1989). 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 ). It appears to be enriched in axons, probably playing a role in axonal development, and it is the inappropriate hyperphosphorylation of this protein in AD which contributes towards neurofibrillary tangle development.

N.B. Please visit the website of the 'Institut National de la Sante et de la Recherche Medical' for detail on tau protein in relation to neurodegeneration

Some Related References


N.B. Free Medical Journals online now at :
(These journals include: Neurology, Neurobiology of Disease, Journal of Neurochemistry, Alzheimer's Disease Review)

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Ackerley, S, Thornhill, P, Grierson, AJ, Brownlees, J, Anderton, BH, Leigh, PN, Shaw, CE, Miller, CCJ (2003) Neurofilament heavy chain side arm phosphorylation regulates axonal transport of neurofilaments. JOURNAL OF CELL BIOLOGY 161: 489-495

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Aletta_Jm, Shelanski_Ml, Greene_La. (1989) Phosphorylation Of The Peripherin 58-Kda Neuronal Intermediate Filament Protein - Regulation By Nerve Growth-Factor And Other Agents. JOURNAL OF BIOLOGICAL CHEMISTRY, 1989, Vol.264, No.8, pp.4619- 4627

Anderson, SJ, Barker, PE, Hadfield, MG (2002) Cytonectin expression in Alzheimer disease. JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY 61: 230-236

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Angelastro_JM, Ho_CL, Frappier_T, Liem_RKH, Greene_LA. (1998) Peripherin is tyrosine-phosphorylated at its carboxyl-terminal tyrosine. JOURNAL OF NEUROCHEMISTRY, 1998, Vol.70, No.2, pp.540-549

Arai, H, Ishiguro, K, Ohno, H, Moriyama, M, Itoh, N, Okamura, N, Matsui, T, Morikawa, Y, Horikawa, E, Kohno, H, Sasaki, H, Imahori, K (2000) CSF phosphorylated tau protein and mild cognitive impairment: a prospective study. EXPERIMENTAL NEUROLOGY 166: 201-203

Arai, Y, Yamazaki, M,  Mori, O, Muramatsu, H, Asano, G and Katayama, Y (2001) alpha-Synuclein-positive structures in cases with sporadic  Alzheimer's disease: morphology and its relationship to tau aggregation. BRAIN RESEARCH 888: 287-296

Arendt_T, Holzer_M, Fruth_R, Bruckner_MK, Gartner_U. (1998) Phosphorylation of tau, A beta-formation, and apoptosis after in vivo inhibition of PP-1 and PP-2A. NEUROBIOLOGY OF AGING, 1998, Vol.19, No.1, pp.3-13

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David, DC, Layfield, R, Serpell, L, Narain, Y, Goedert, M, Spillantini, MG (2002)
Proteasomal degradation of tau protein

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Dehmelt, L, Halpain, S (2005) The MAP2/Tau family of microtubule-associated proteins.  GENOME BIOLOGY 6: 195-204

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Eidenmuller, J, Fath, T, Hellwig, A, Reed, J, Sontag, E and Brandt, R (2000) Structural and functional implications of tau hyperphosphorylation: Information from phosphorylation-mimicking mutated tau proteins. BIOCHEMISTRY 39: 13166-13175

Eidenmuller, J, Fath, T, Maas, T, Pool, M, Sontag, E and Brandt, R (2001) Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein. BIOCHEMICAL JOURNAL 357: 759-767

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Esposito, G, Viglino, P, Novak, M and Cattaneo, A (2000) The solution structure of the C-terminal segment of tau protein. JOURNAL OF PEPTIDE SCIENCE 6: 550-559

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Mol Biol Cell.

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