Download e-book for iPad: Alzheimer's Disease: Advances in Genetics, Molecular and by Sangram S. Sisodia, Rudolph E. Tanzi

By Sangram S. Sisodia, Rudolph E. Tanzi

ISBN-10: 0387351345

ISBN-13: 9780387351346

ISBN-10: 0387351353

ISBN-13: 9780387351353

This booklet examines each significant point of Alzheimer sickness – medical, epidemiologic, structural, chemical, genetic, molecular, and healing. This version contains extended assurance of the cellular-level exploration of comparable dementing issues, with in-depth presentation of prion illnesses, Pick's ailment, fronto-temporal problems, transgenic versions, and biochemistry of presenilins. remedy of signs with healing medicines is mentioned, in addition to results of and difficulties inherent in medical trials for advert. The extensive insurance of advert during this publication merits clinicians, educators, investigators, and healthiness administrators.

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Additional info for Alzheimer's Disease: Advances in Genetics, Molecular and Cellular Biology

Sample text

It was reported that F-spondin, a neuronally secreted signaling glycoprotein that may function in neuronal development and repair, binds to the extracellular domain of APP as well as APLP1 and APLP2 (Ho and Sudhof, 2004). This binding reduces β-secretase cleavage of APP and nuclear transactivation of AICD (see below), suggesting therefore that F-spondin may be a ligand that regulates APP processing. As mentioned above, γ -secretase processing of APP also releases an intracellular domain of APP, termed AICD (Figure 1).

However since this reflects a decrease in Aβ40 and an increase in Aβ42, these results do not necessarily imply that absolute amounts of Aβ are elevated (Walker et al. 2005). If Aβ42 is an inefficiently generated Aβ species, one could reconcile the data, at least conceptually, by proposing that PS mutations cause partial loss of function of the γ -secretase complex (hypomorphs), resulting in a protease that is biochemically inefficient. This interpretation is not necessarily in contradiction with rescue experiments in PS1 knock out mice showing that transgenic expression of FAD mutant PS1, can (partially) rescue the embryonic lethal phenotype (Qian et al.

2005). Taken together, these findings are consistent with the prediction that γ -secretase cleavage of APP occurs in lipid rafts. Further investigations are needed to address how the components of the γ -secretase and APP are recruited into raft microdomains, and clarify whether genetic mutations in APP, PS1, and PS2 modulate Aβ42 production by affecting the localization and processing of APP in lipid rafts. 3. 1 Trophic properties While a number of physiological roles have been attributed to APP, some unique to certain isoforms, the in vivo function(s) of the molecule remain unclear.

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Alzheimer's Disease: Advances in Genetics, Molecular and Cellular Biology by Sangram S. Sisodia, Rudolph E. Tanzi


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