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Tools to Study Alzheimer's Disease

The most common cause of dementia in older people, Alzheimer’s disease (AD), claims over 20,000 lives each year, a number that is expected to explode in the next few decades as our population ages. The postmortem diagnosis of AD depends on the existence of b-amyloid (Ab) plaques and intracellular neurofibrillary tangles (NFTs). Production of Ab, a protein essential to the development of AD, begins with cleavage of amyloid precursor protein (APP), which resides in the cell membrane. b-secretase cleavage of APP results in the secretion of amyloidogenic Ab, whereas b -secretase cleavage cleaves the precursor in the middle so that no Ab is formed. NFTs consist of accumulated hyperphosphorylated tau that forms paired helical filaments within the nerve cell body. AD results in drastic changes in quality of life for patients and their families, but the causes of the disease are not well understood, and there is no cure. Current treatments aim to improve AD symptoms, but do not address its underlying causes and do nothing to halt the progression of the disease. There is an urgent need for understanding the fundamental processes of Alzheimer’s degeneration in order to develop effective therapies for this debilitating condition.

The principal protein implicated in Alzheimer's disease is the transmembrane amyloid precursor protein (APP). Multiple APP isoforms, generated by alternative splicing, have been described with a 770 amino acid isoform being the largest and a 695 amino acid isoform being most prevalent in neuronal cells. Amyloid b (Ab) is produced by sequential cleavage of APP by proteins called secretases. Proteolysis of APP by b-secretase, which cleaves APP695 after Met-596, produces a large soluble n-terminal fragment (sAPPb) and a small membrane-bound c-terminal fragment (C 99). The C99 fragment is further processed by y-secretase cleavage within the trans-membrane region at Val-636, Ala-638 or Thr-639 to produce the three Ab isoforms of 40, 42, or 43 amino acids, designated x-40, x-42 or x-43. The Ab isoforms can induce neuronal apoptisis and aggregate into amyloid plaques. Progression of Alzheimer's disease is associated with increased levels of the x-42 and x-43 Ab peptides.

Tools to Study Alzheimer's Disease Protein of Interest

References

1. Bhat RV. Budd Haeberlein SL. Avila J. Glycogen synthase kinase 3: a drug target for CNS therapies. Journal of Neurochemistry. 89(6): 1313–7, 2004 Jun.
2. Goodenough S. Schafer M. Behl C. Estrogeninduced cell signalling in a cellular model of Alzheimer’s disease. Journal of Steroid Biochemistry & Molecular Biology. 84(2–3): 301–5, 2003 Feb.
3. Johnson GV. Bailey CD. The p38 MAP kinase signaling pathway in Alzheimer’s disease. Experimental Neurology. 183(2): 263–8, 2003 Oct.
4. King GD. Scott Turner R. Adaptor protein interactions: modulators of amyloid precursor protein metabolism and Alzheimer’s disease risk? Experimental Neurology. 185(2): 208–19, 2004 Feb.

1. Ogris, E., et al. 1999. A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. Journal of Biological Chemistry, 274(20): 14382–14391.
2. Tsai LH. Lee MS. Cruz J. Cdk5, a therapeutic target for Alzheimer’s disease? Biochimica et Biophysica Acta. 1697(1–2): 137–42, 2004 Mar 1

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