scholarly journals Effects of Amyloid Precursor Protein 17 Peptide on the Protection of Diabetic Encephalopathy and Improvement of Glycol Metabolism in the Diabetic Rat

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Heng Meng ◽  
Duo Zhang ◽  
Haishan Yang
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Plaques ◽  
Precursor Protein ◽  
Diabetic Rat ◽  
Therapeutic Effects ◽  
Diabetic Encephalopathy ◽  
Peptide Group ◽  
Experimental Approaches ◽  
Active Fragment ◽  
The Brain

Researchers have proposed that amyloid precursor protein 17 peptide (APP17 peptide), an active fragment of amyloid precursor protein (APP) in the nervous system, has therapeutic effects on neurodegeneration. Diabetic encephalopathy (DE) is a neurological disease caused by diabetes. Here we use multiple experimental approaches to investigate the effect of APP17 peptide on changes in learning behavior and glycol metabolism in rats. It was found that rats with DE treated by APP17 peptide showed reversed behavioral alternation. The [18F]-FDG-PET images and other results all showed that the APP17 peptide could promote glucose metabolism in the brain of the DE rat model. Meanwhile, the insulin signaling was markedly increased as shown by increased phosphorylation of Akt and enhanced GLUT4 activation. Compared with the DE group, the activities of SOD, GSH-Px, and CAT in the rat hippocampal gyrus were increased, while MDA decreased markedly in the DE + APP17 peptide group. No amyloid plaques in the cortex and the hippocampus were detected in either group, indicating that the experimental animals in the current study were not suffering from Alzheimer’s disease. These results indicate that APP17 peptide could be used to treat DE effectively.

β-amyloid plaques in amyloid precursor protein knock-in mice

2000 ◽  
Vol 21 ◽  
pp. 223
Author(s):  
Andreas Popp ◽  
Elke Hartmann ◽  
Ina Hagelschuer ◽  
A.G. Bayer ◽  
Karen Duff ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Amyloid Plaques ◽  
Precursor Protein ◽  
Β Amyloid

Lewy bodies in the brain of two members of a family with the 717 (Val to Ile) mutation of the amyloid precursor protein gene

1994 ◽  
Vol 172 (1-2) ◽  
pp. 77-79 ◽  
Author(s):  
P.L. Lantos ◽  
I.M.K. Ovenstone ◽  
J. Johnson ◽  
C.A. Clelland ◽  
Penelope Roques ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Protein Gene ◽  
Lewy Bodies ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Gene ◽  
The Brain

scholarly journals Transmissible Endosomal Intoxication: A Balance between Exosomes and Lysosomes at the Basis of Intercellular Amyloid Propagation

Biomedicines ◽  
2020 ◽  
Vol 8 (8) ◽  
pp. 272
Author(s):  
Anaïs Bécot ◽  
Charlotte Volgers ◽  
Guillaume van Niel
Keyword(s):  
Amyloid Precursor Protein ◽  
Neurodegenerative Diseases ◽  
Multivesicular Body ◽  
Precursor Protein ◽  
Aβ Peptides ◽  
Amyloid Aβ ◽  
Β Amyloid ◽  
Novel Concept ◽  
The Brain

In Alzheimer′s disease (AD), endolysosomal dysfunctions are amongst the earliest cellular features to appear. Each organelle of the endolysosomal system, from the multivesicular body (MVB) to the lysosome, contributes to the homeostasis of amyloid precursor protein (APP) cleavage products including β-amyloid (Aβ) peptides. Hence, this review will attempt to disentangle how changes in the endolysosomal system cumulate to the generation of toxic amyloid species and hamper their degradation. We highlight that the formation of MVBs and the generation of amyloid species are closely linked and describe how the molecular machineries acting at MVBs determine the generation and sorting of APP cleavage products towards their degradation or release in association with exosomes. In particular, we will focus on AD-related distortions of the endolysomal system that divert it from its degradative function to favour the release of exosomes and associated amyloid species. We propose here that such an imbalance transposed at the brain scale poses a novel concept of transmissible endosomal intoxication (TEI). This TEI would initiate a self-perpetuating transmission of endosomal dysfunction between cells that would support the propagation of amyloid species in neurodegenerative diseases.

Sign in / Sign up

Export Citation Format

Share Document