The effect of corticosteroids on amyloid β precursor protein/amyloid precursor-like protein expression and processing in vivo

1999 ◽  
Vol 276 (1) ◽  
pp. 61-64 ◽  
Author(s):  
Grant Budas ◽  
Christine M Coughlan ◽  
Jonathan R Seckl ◽  
Kieran C Breen
1998 ◽  
Vol 245 (2) ◽  
pp. 111-115 ◽  
Author(s):  
M. Bornebroek ◽  
Peter A. Kr. von dem Borne ◽  
Joost Haan ◽  
Joost C. M. Meijers ◽  
William E. Van Nostrand ◽  
...  

Thyroid ◽  
2006 ◽  
Vol 16 (12) ◽  
pp. 1207-1213 ◽  
Author(s):  
Stephen A. O'Barr ◽  
Jin S. Oh ◽  
Chan Ma ◽  
Gregory A. Brent ◽  
James J. Schultz

2018 ◽  
Vol 19 (7) ◽  
pp. 2109 ◽  
Author(s):  
Yong Tang ◽  
Rui Xiong ◽  
An-Guo Wu ◽  
Chong-Lin Yu ◽  
Ya Zhao ◽  
...  

Amyloid-β (Aβ) is commonly recognized as the most important factor that results in neuronal cell death and accelerates the progression of Alzheimer’s disease (AD). Increasing evidence suggests that microglia activated by Aβ release an amount of neurotoxic inflammatory cytokines that contribute to neuron death and aggravate AD pathology. In our previous studies, we found that lychee seed fraction (LSF), an active fraction derived from the lychee seed, could significantly improve the cognitive function of AD rats and inhibit Aβ-induced neuroinflammation in vitro, and decrease neuronal injuries in vivo and in vitro. In the current study, we aimed to isolate and identify the specific components in LSF that were responsible for the anti-neuroinflammation effect using preparative high performance liquid chromatography (pre-HPLC), liquid chromatography-mass spectrometry (LC-MS), and nuclear magnetic resonance (NMR) methods. To this end, we confirmed two polyphenols including catechin and procyanidin A2 that could improve the morphological status of BV-2 cells and suppress the release, mRNA levels, and protein expression of pro-inflammatory cytokines such as tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β), and interleukin-6 (IL-6) through downregulating the nuclear factor-κB (NF-κB) signaling pathway using ELISA, RT-PCR, and Western blotting methods. Furthermore, catechin and procyanidin A2 could inhibit Aβ-induced apoptosis in BV-2 cells by upregulating Bcl-2 and downregulating Bax protein expression. Therefore, the current study illustrated the active substances in lychee seed, and first reported that catechin and procyanidin A2 could suppress neuroinflammation in Aβ-induced BV-2 cells, which provides detailed insights into the molecular mechanism of catechin and procyanidin A2 in the neuroprotective effect, and their further validations of anti-neuroinflammation in vivo is also essential in future research.


1993 ◽  
Vol 293 (1) ◽  
pp. 27-30 ◽  
Author(s):  
J Ghiso ◽  
E Matsubara ◽  
A Koudinov ◽  
N H Choi-Miura ◽  
M Tomita ◽  
...  

The amyloid fibrils deposited in Alzheimer's neuritic plaque cores and cerebral blood vessels are mainly composed of aggregated forms of a unique peptide, 39-42 amino acids long, named amyloid beta (A beta). A similar, although soluble, A beta (‘sA beta’) has been identified in cerebrospinal fluid, plasma and cell supernatants, indicating that it is normally produced by proteolytic processing of its precursor protein, amyloid precursor protein (APP). Using direct binding experiments we have isolated and characterized an 80 kDa circulating protein that specifically interacts with a synthetic peptide identical with A beta. The protein was unmistakably identified as SP-40,40 or ApoJ, a cytolytic inhibitor and lipid carrier, by means of amino acid sequence and immunoreactivity with specific antibodies. Immunoprecipitation with anti-SP-40,40 retrieved soluble A beta from cerebrospinal fluid, indicating that the interaction occurs in vivo.


PLoS ONE ◽  
2010 ◽  
Vol 5 (7) ◽  
pp. e11609 ◽  
Author(s):  
Luca Giliberto ◽  
Cristina d'Abramo ◽  
Christopher Michael Acker ◽  
Peter Davies ◽  
Luciano D'Adamio

Science ◽  
2019 ◽  
Vol 363 (6423) ◽  
pp. eaao4827 ◽  
Author(s):  
Heather C. Rice ◽  
Daniel de Malmazet ◽  
An Schreurs ◽  
Samuel Frere ◽  
Inge Van Molle ◽  
...  

Amyloid-β precursor protein (APP) is central to the pathogenesis of Alzheimer’s disease, yet its physiological function remains unresolved. Accumulating evidence suggests that APP has a synaptic function mediated by an unidentified receptor for secreted APP (sAPP). Here we show that the sAPP extension domain directly bound the sushi 1 domain specific to the γ-aminobutyric acid type B receptor subunit 1a (GABABR1a). sAPP-GABABR1a binding suppressed synaptic transmission and enhanced short-term facilitation in mouse hippocampal synapses via inhibition of synaptic vesicle release. A 17–amino acid peptide corresponding to the GABABR1a binding region within APP suppressed in vivo spontaneous neuronal activity in the hippocampus of anesthetized Thy1-GCaMP6s mice. Our findings identify GABABR1a as a synaptic receptor for sAPP and reveal a physiological role for sAPP in regulating GABABR1a function to modulate synaptic transmission.


2009 ◽  
Vol 5 (4S_Part_4) ◽  
pp. P116-P117
Author(s):  
Takami Tomiyama ◽  
Shogo Matsuyama ◽  
Hiroyuki Iso ◽  
Hiroshi Takuma ◽  
Tomohiro Umeda ◽  
...  

2017 ◽  
Vol 38 (10) ◽  
pp. 1715-1726 ◽  
Author(s):  
Livius V d’Uscio ◽  
Tongrong He ◽  
Anantha V Santhanam ◽  
Zvonimir S Katusic

The exact physiological function of amyloid-β precursor protein (APP) in endothelial cells is unknown. Endothelium-specific APP-deficient (eAPP−/−) mice were created to gain new insights into the role of APP in the control of vascular endothelial function. Endothelium-dependent relaxations to acetylcholine were significantly impaired in basilar arteries of global APP knockout (APP−/−) and eAPP−/− mice ( P < 0.05). In contrast, endothelium-independent relaxations to nitric oxide (NO)-donor diethylamine-NONOate were unchanged. Western blot analysis revealed that protein expression of endothelial nitric oxide synthase (eNOS) was significantly downregulated in large cerebral arteries of APP−/− mice and eAPP−/− mice as compared to respective wild-type littermates ( P < 0.05). Furthermore, basal levels of cyclic guanosine monophosphate (cGMP) were also significantly reduced in large cerebral arteries of APP-deficient mice ( P < 0.05). In contrast, protein expression of prostacyclin synthase as well as levels of cyclic adenosine monophosphate (cAMP) was not affected by genetic inactivation of APP in endothelial cells. By using siRNA to knockdown APP in cultured human brain microvascular endothelial cells we also found a significant downregulation of eNOS mRNA and protein expressions in APP-deficient endothelium ( P < 0.05). These findings indicate that under physiological conditions, expression of APP in cerebral vascular endothelium plays an important protective function by maintaining constitutive expression of eNOS .


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