Amyloid Precursor Protein Might be a Receptor for Basic Fibroblast Growth Factor

Karaulanov, Emil; Gramatikoff, Kostadin; Milev, Peter

doi:10.3109/00207459208999793

Cited by 3 publications

(2 citation statements)

References 10 publications

(12 reference statements)

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“…APP has been shown to modulate cell growth, motility, neurite outgrowth and cell survival in transfected cell lines [42]. An in vivo study showed that rodents injected APP RNAi developed neuronal migration abnormalities [43].…”

Section: Other Functions Of Appmentioning

confidence: 99%

The role of APP in Alzheimer’s disease

Pung¹,

Wang²,

et al. 2013

AAD

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Alzheimer's disease (AD) is one of the most significant neurodegenerative disorders in terms of both severity and cost. Despite being defined over a century ago, there is currently no cure to this disease that affects an increasing elderly population. The amyloid precursor protein (APP) has been shown to play an important role in AD progression. The amyloid β peptide (Aβ), which accumulates in senile plaques, a central etiological AD factor, is a proteolytic product from APP by the enzymatic action of βand γ-secretases. In this review, we summarize the current knowledge of the processing and physiological functions of APP, and the involvement of APP and Aβ in AD. . (1999) Mutagenesis identifies new signals for β-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Aβ42.

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Section: Other Functions Of Appmentioning

confidence: 99%

The role of APP in Alzheimer’s disease

Pung¹,

Wang²,

et al. 2013

AAD

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“…APP exists either as a fulllength, transmembrane protein on the cell surface or a truncated soluble extracellular protein, protease nexin 2 (PN2). APP has been postulated to play a role in cell survival (13), neurite outgrowth (14,15), or to act as a cellular receptor (16).…”

Section: Introductionmentioning

confidence: 99%

Characterization of endogenous APP processing in a cell-free system

Brown

Potempska

Tummolo

et al. 1998

AGE

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We have developed a simple in vitro assay using tissue homogenates that allows detection and characterization of several endogenous proteolytic activities which convert Alzheimer's amyloid precursor protein (APP) to the smaller, carboxy-terminal fragments, postulated to be intermediates in the formation of 13-amyloid peptide (AI3). Incubation at 37 ~ C results in the degradation of transmembrane APP and formation of a mixture of carboxy-terminal containing peptides with mass values of 9-12 kDa. Epitope mapping and electrophoretic comparison with a truncated APP standard showed one of these peptides to contain the entire AI3 sequence. Analysis of pH dependence shows that formation of this carboxy-terminal product as well as another fragment, that is the likely product of 'secretase' activity, requires acidic pH. This suggests that cleavage of full-length APP to secreted forms may take place in an acidic intracellular compartment.

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