Alzheimers Disease: An Investigation of an Amyloid Disease – Disorder Example

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"Alzheimer’ s Disease: An Investigation of an Amyloid Disease" is an engrossing example of a paper on the disorder. The main objective of the research undertaken is to investigate the molecular mechanism of Alzheimer’ s Disease (AD) as one of the conditions based on an abnormality in the amyloid functions. AD affects the cognitive function of the patient on the basis of ‘ cerebral atrophy, deposits of amyloid-β (Aβ ), neurofibrillary tangles, and neuronal cell loss (Amatsubo et al. , 2010, p. 25).   The condition can be defined as the most prevalent form of dementia that can be attributed to the pathogenic function of the amyloid-β protein recognized through the distinctive histopathologies of senile plaques and cerebral amyloid angiopathy.   Upon examination of the histological samples of AD, amyloid-β had been recorded in the areas and structures of the body known to be affected by the disease such as the hippocampal and frontotemporal cortices, specifically the neuronal processes and smooth muscle cells.   These areas had been observed with amyloid-β plaques and neuronal cell death (Lee et al. , 2007, p. 823).                       Amyloid-β (Aβ ) is the main protein responsible for the onset and continuous progression of the AD.   Aside from AD, other diseases known to be related to the action of amyloid-β are type 2 diabetes and Parkinson’ s disease.   Aβ is formed through the cleavage of the amyloid precursor protein.   The process results through the peptide-folding mechanism of the protein.   Oligomerization will then follow which can produce plaques of β -sheet due to continuous reaction of β and γ secretases.   The said reactions occur specifically in the isoforms Aβ 40 and Aβ 42.  At the point in the molecular reaction of these components, the Aβ can be considered toxic, thus, the detection of phases related to the formation of the said dodecamer of Aβ wherein plaques are established through molecular peptide-folding is the main focus in related studies (Berstein et al. , 2009, p.

326-7).   Basically, the Aβ is a by-product in the cleavage of a transmembrane protein which is essential in cellular processes but due to the process of molecular peptide-folding, the deposits of the toxic form of amyloid protein occur and result to diseases such as AD.   As the processes in the cell occur on a molecular level, the unmodified proteins are photoinduced resulting in cross-linking in the form of 42-residue form, a reactive phase that can develop into structures of higher level.   The said molecular form produces the plaques that can cause the expression of the cognitive symptoms of the disease (Berstein et al. , 2009, p.

328). The senile plaques and cerebral amyloid angiopathy, the main causes of AD, are due to the deposits of Aβ in different forms that can continuously occur with high risks of being aggregated into complex and stable forms (such as amyloid fibrils and plaques) that can pathologically affect the functioning of the body in the molecular and cellular level.   An increasing number of cells are affected by the generative degradation of the cognitive functions of patients with AD occurs (Berstein et al. , 2009; Lee et al. , 2007, p. 823).


Amatsubo, T., Yanagisawa, D., Morikawa, S. and Tagushi, H. and Tooyama, I. (2010). Amyloid Imaging Using High-Field Magnetic Resonance. Magn Reson Med Sci, 20 (3), p. 95-99.

Berstein, S. L., Dupuis, N.F., Lazo, N.D., Wyttenbach, T., Condron, M.M., Bitan, G., Teplow, D.B., Shea, J.E., Ruotolo, B.T., Robinson, C.V. and Bowers, M.T. (2009). Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer’s disease. Nat Chem., 1(4), p. 326-331.

Lee, H., Zhu, X., Castellani, R.J., Nunomura, A., Perry, G., and Smith., M.A. (2007). Amyloid-β in Alzheimer Disease: The Null versus the Alternate Hypotheses. JPET, 321, p.823-829.

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