Mϋnch, G. (2005) Glycation and physiological mechanisms of its prevention in Alzheimer's disease. In: Sames, Klaus, Sethe, Sebastian, and Stolzing, Alexandra, (eds.) Extending the Lifespan: biotechnical, gerontological and social problems. LIT Verlag, Mϋnster, Germany, pp. 103-106.

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Abstract

Alzheimer's disease (AD) is a multifactorial disease that involves progressive synaptic loss and neuronal death. This neurodegeneration has been linked to the presence of extracellular plaques of amyloid beta (Aβ) peptide and to the occurrence of intracellular deposits (tangles) that are composed predominantly of microtubule-associated-protein tau (MAP-tau). It is noteworthy that the proteins in these deposits are frequently modified by Advanced Glycation Endproducts (AGEs). AGEs are found in many aging and pathological tissues but are particularly prevalent in AD. Evidence suggests that AGE-crosslinked aggregates may contribute to the pathophysiology of AD by a variety of mechanisms.

Item ID:	14419
Item Type:	Book Chapter (Research - B1)
ISBN:	978-3-8258-8563-2
Keywords:	AGE-crosslinking; Alzheimer's disease; glycation
Date Deposited:	23 Dec 2010 02:01
FoR Codes:	11 MEDICAL AND HEALTH SCIENCES > 1109 Neurosciences > 110902 Cellular Nervous System @ 100%
SEO Codes:	92 HEALTH > 9201 Clinical Health (Organs, Diseases and Abnormal Conditions) > 920111 Nervous System and Disorders @ 100%
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