Regulation of Amyloid Precursor Protein Processing by Low Density Lipoprotein Receptor-related Protein and Neurotrophin Receptors PDF Download
Are you looking for read ebook online? Search for your book and save it on your Kindle device, PC, phones or tablets. Download Regulation of Amyloid Precursor Protein Processing by Low Density Lipoprotein Receptor-related Protein and Neurotrophin Receptors PDF full book. Access full book title Regulation of Amyloid Precursor Protein Processing by Low Density Lipoprotein Receptor-related Protein and Neurotrophin Receptors by Amity F. Gann. Download full books in PDF and EPUB format.
Author: Amity F. Gann
Publisher:
ISBN:
Category :
Languages : en
Pages : 92
Get Book Here
Book Description
Author: Amity F. Gann
Publisher:
ISBN:
Category :
Languages : en
Pages : 92
Get Book Here
Book Description
Author: Melissa Holtman Tukey
Publisher:
ISBN:
Category : Alzheimer's disease
Languages : en
Pages : 140
Get Book Here
Book Description
Author: Lisa A. M. Conboy
Publisher:
ISBN:
Category : Alzheimer's disease
Languages : en
Pages : 197
Get Book Here
Book Description
![Role of the Low Density Lipoprotein Receptor-related Protein in the Metabolism of the [beta]-amyloid Precursor Protein PDF](https://books.google.com/books/content/images/frontcover/6xbcNwAACAAJ?fife=w80-h100)
Author: Paula Guillermina Ulery Torréns
Publisher:
ISBN:
Category :
Languages : en
Pages : 268
Get Book Here
Book Description
![The Mechanism of the Low-density Lipoprotein Receptor-related Protein (LRP) in the Production of Amyloid-[Beta] Peptide PDF](https://books.google.com/books/content/images/frontcover/MhqhDAEACAAJ?fife=w80-h100)
Author: Eunice Chungyu Chen
Publisher:
ISBN:
Category :
Languages : en
Pages : 46
Get Book Here
Book Description
Alzheimer's disease (AD) is the most common form of neurodegenerative disorder affecting the elderly, presenting symptoms such as memory impairment and dementia. AD is pathologically characterized by the development of extracellular senile plaques and intracellular neurofibrillary tangles (NFT). The plaques are composed of amyloid-[Beta] peptide (A[Beta]) and the NFTs are composed of a hyperphosphorylated form of the tau protein. A[Beta] is formed by sequential proteolytic processing of the amyloid precursor protein (APP) by [Beta]-, and [Gamma]-secretase. Accordingly, alterations in APP processing result in increased A[Beta] generation. The low-density lipoprotein receptor-related protein (LRP) is a large endocytic protein involved in diverse biological functions. It has been hypothesized that LRP plays a dual role in AD, playing a role in both the clearance and the production of A[Beta]. Previous studies have shown that the cytoplasmic tail alone is able to promote A[Beta] generation and promote APP processing. This study seeks to determine the area of the cytoplasmic tail responsible for pro-amyloidogenic activity and how it occurs. Our findings indicate that the last 37 amino acids of the tail, containing a dileucine motif, are sufficient. Additionally, LRP facilitates the generation of A[Beta] by trafficking APP and BACE1 to the lipid raft domains. This function of LRP may be altered due to the presence of a Kunitz protease inhibitor (KPI) domain on APP. The results of our study have therapeutic potential to reduce [Beta]-amyloid by understanding the function of LRP in the amyloidogenic processing of APP.
Author: David Eun-Kwang Kang
Publisher:
ISBN:
Category :
Languages : en
Pages : 390
Get Book Here
Book Description
Author: Heather Caroline Rice
Publisher:
ISBN:
Category :
Languages : en
Pages :
Get Book Here
Book Description
Despite intense interest in the proteolysis of Amyloid Precursor Protein (APP) in Alzheimer's disease (AD), how the normal processing and function of this type I receptor-like glycoprotein is regulated remains ill-defined. APP is reported to function in neurodevelopment, including migration of neuronal precursor cells into the cortical plate. In recent years, several candidate ligands for APP, including F-spondin, Reelin, â1 Integrin, Contactins, and Lingo-1 have been reported. However, a cognate ligand for APP that regulates its function or processing has yet to be widely confirmed in multiple laboratories.
Author: Emily Van Uden
Publisher:
ISBN:
Category :
Languages : en
Pages : 272
Get Book Here
Book Description
Author: Ulrike C. Müller
Publisher: Frontiers Media SA
ISBN: 2889453553
Category :
Languages : en
Pages : 295
Get Book Here
Book Description
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: C.L. Masters
Publisher: Springer Science & Business Media
ISBN: 3662011352
Category : Science
Languages : en
Pages : 277
Get Book Here
Book Description
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.
