Investigating The Role Of The Amyloid Precursor Protein In The Pathogenesis Of Alzheimers Disease
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Author | : Roger Lefort |
Publisher | : |
Total Pages | : |
Release | : 2011 |
Genre | : |
ISBN | : |
We also found that dimerization of APP is sufficient to promote the amyloidogenic pathway, by increasing levels of the Î2-secretase BACE1, resulting in increased AÎ2 production. Finally, we found that dimerization of APP triggered caspase-dependent cleavage of APP and the formation of a second neurotoxic fragment, termed C31, which also mimics the effects of AÎ2 in hippocampal neurons. Taken together, our data provides support for the occurrence of a positive pathogenic feedback loop involving AÎ2, APP and C31 in neurons.
Author | : C.L. Masters |
Publisher | : Springer Science & Business Media |
Total Pages | : 277 |
Release | : 2013-04-17 |
Genre | : Science |
ISBN | : 3662011352 |
This book summarizes the last ten years' research on Alzheimer's disease. Genetic mutations in the gene which codes for amyloid precursor protein (APP) have now been shown to cause Alzheimer's disease in some families. Other genetic loci are now being discovered which relate to Alzheimer's disease in some families. Understanding the normal structure and function of the APP gene product will eventually provide avenues for developing specific therapeutic strategies targeted at the amyloid deposition in the Alzheimer's disease brain. Drugs which can inhibit or dissolve the amyloid, affect the synthesis and proteolysis of APP, or which regulate the activity of the APP gene all hold the promise of eventually yielding an effective treatment for Alzheimer's disease.
Author | : Ulrike C. Müller |
Publisher | : Frontiers Media SA |
Total Pages | : 295 |
Release | : 2017-12-28 |
Genre | : |
ISBN | : 2889453553 |
The amyloid precursor protein APP plays a key role in the pathogenesis of Alzheimer’s disease (AD), as proteolytical cleavage of APP gives rise to the Aβ peptide which is deposited in the brains of Alzheimer patients. Despite this, our knowledge of the normal cell biological and physiological functions of APP and the closely related APLPs is limited. This may have hampered our understanding of AD, since evidence has accumulated that not only the production of the Aβ peptide but also the loss of APP-mediated functions may contribute to AD pathogenesis. Thus, it appears timely and highly relevant to elucidate the functions of the APP gene family from the molecular level to their role in the intact organism, i.e. in the context of nervous system development, synapse formation and adult synapse function, as well as neural homeostasis and aging. Why is our understanding of the APP functions so limited? APP and the APLPs are multifunctional proteins that undergo complex proteolytical processing. They give rise to an almost bewildering array of different fragments that may each subserve specific functions. While Aβ is aggregation prone and neurotoxic, the large secreted ectodomain APPsα - produced in the non-amyloidogenic α-secretase pathway - has been shown to be neurotrophic, neuroprotective and relevant for synaptic plasticity, learning and memory. Recently, novel APP cleavage pathways and enzymes have been discovered that have gained much attention not only with respect to AD but also regarding their role in normal brain physiology. In addition to the various cleavage products, there is also solid evidence that APP family proteins mediate important functions as transmembrane cell surface molecules, most notably in synaptic adhesion and cell surface signaling. Elucidating in more detail the molecular mechanisms underlying these divers functions thus calls for an interdisciplinary approach ranging from the structural level to the analysis in model organisms. Thus, in this research topic of Frontiers we compile reviews and original studies, covering our current knowledge of the physiological functions of this intriguing and medically important protein family.
Author | : Oliver Wilkes |
Publisher | : |
Total Pages | : 0 |
Release | : 2022 |
Genre | : |
ISBN | : |
Author | : Elise Nguyen Le |
Publisher | : |
Total Pages | : 0 |
Release | : 2022 |
Genre | : |
ISBN | : |
Author | : Thimmaiah Govindaraju |
Publisher | : Royal Society of Chemistry |
Total Pages | : 531 |
Release | : 2022-01-04 |
Genre | : Medical |
ISBN | : 1839162740 |
Alzheimer’s disease is an increasingly common form of dementia and despite rising interest in discovery of novel treatments and investigation into aetiology, there are no currently approved treatments that directly tackle the causes of the condition. Due to its multifactorial pathogenesis, current treatments are directed against symptoms and even precise diagnosis remains difficult as the majority of cases are diagnosed symptomatically and usually confirmed only by autopsy. Alzheimer’s Disease: Recent Findings in Pathophysiology, Diagnostic and Therapeutic Modalities provides a comprehensive overview from aetiology and neurochemistry to diagnosis, evaluation and management of Alzheimer's disease, and latest therapeutic approaches. Intended to provide an introduction to all aspects of the disease and latest developments, this book is ideal for students, postgraduates and researchers in neurochemistry, neurological drug discovery and Alzheimer’s disease.
Author | : Weiming Xia |
Publisher | : CRC Press |
Total Pages | : 240 |
Release | : 2004-12-16 |
Genre | : Science |
ISBN | : 0203492188 |
In the search for an effective treatment for Alzheimer's disease, APP is a unique model protein that illustrates the wide array of basic and sophisticated characterization techniques available. Exploring a variety of biological techniques to clarify the structure and function of this transmembrane protein, this text presents each method with detail
Author | : James Daly |
Publisher | : |
Total Pages | : 282 |
Release | : 1998 |
Genre | : Alzheimer's disease |
ISBN | : |
Author | : Rudy Castellani |
Publisher | : Biota Publishing |
Total Pages | : 166 |
Release | : 2013-10-31 |
Genre | : Health & Fitness |
ISBN | : 1615047417 |
Alzheimer’s Disease is characterized pathologically by two principal hallmark lesions: the senile plaque and the neurofibrillary tangle. Since the identification of each over 100 years ago, the major protein components have been elucidated. This has led in turn to the elaboration of metabolic cascades involving amyloid-β production in the case of the senile plaque, and phosphorylated-tau protein in the case of the neurofibrillary tangle. The pathogenesis and histogenesis of each have been the source of extensive investigation and some controversy in recent years, as both cascades have been implicated in the pathogenesis of Alzheimer’s Disease, relied upon in the diagnostic criteria for Alzheimer’s Disease at autopsy, and targeted for therapeutic intervention. With the accumulation of data and expansion of knowledge of the molecular biology of Alzheimer’s Disease, it appears that the enthusiasm for successful intervention has been premature. In this book, we detail the discovery and characterization of the major pathological lesions, their associated molecular biology, their relationship to clinical disease, and potential fundamental errors in understanding that may be leading scientific investigators in unintended directions.
Author | : A.D. Roses |
Publisher | : Springer Science & Business Media |
Total Pages | : 208 |
Release | : 2012-12-06 |
Genre | : Medical |
ISBN | : 3642801099 |
There is now considerable genetic evidence that the type 4 allele of the apolipoprotein E gene is a major susceptibility factor associated with late-onset Alzheimer's disease, the common form of the disease defined as starting after sixty years of age. The role of apolipoprotein E in normal brain metabolism and in the pathogenesis of Alzheimer's disease are new and exciting avenues of research. This book, written by the most outstanding scientists in this new filed, is the first presentation of results concerning the implications of apolipoprotein E on the genetics, cell biology, neuropathology, biochemistry, and therapeutic management of Alzheimer's disease.