scholarly journals Organization of amyloid-β protein precursor intracellular domain-associated protein-1 in the rat brain

2010 ◽  
Vol 518 (16) ◽  
pp. 3221-3236 ◽  
Author(s):  
Amanda L. Jacob ◽  
Bryen A. Jordan ◽  
Richard J. Weinberg
Keyword(s):  
Rat Brain ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Intracellular Domain ◽  
Protein Precursor ◽  
Β Protein

Amyloid β protein precursor accumulates in swollen neurites throughout rat brain with aging

1993 ◽  
Vol 153 (1) ◽  
pp. 73-76 ◽  
Author(s):  
Takeshi Kawarabayashi ◽  
Mikio Shoji ◽  
Haruyasu Yamaguchi ◽  
Makoto Tanaka ◽  
Yasuo Harigaya ◽  
...  
Keyword(s):  
Rat Brain ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Β Protein

Accumulation of amyloid β-protein precursor (APP) in Purkinje cells and increase of amino-terminal fragments of APP in cerebrum and cerebellum of aged rat brain

1994 ◽  
Vol 643 (1-2) ◽  
pp. 319-323 ◽  
Author(s):  
Yu Nakamura ◽  
Masatoshi Takeda ◽  
Hisayoshi Niigawa ◽  
Fuyuki Kametani ◽  
Shiro Hariguchi ◽  
...  
Keyword(s):  
Rat Brain ◽  
Purkinje Cells ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Aged Rat ◽  
Amino Terminal ◽  
Β Protein

Evidence that the Amyloid-β Protein Precursor Intracellular Domain, AICD, Derives From β-Secretase-Generated C-Terminal Fragment

2012 ◽  
Vol 30 (1) ◽  
pp. 145-153 ◽  
Author(s):  
Brice Flammang ◽  
Raphaëlle Pardossi-Piquard ◽  
Jean Sevalle ◽  
Delphine Debayle ◽  
Anne-Sophie Dabert-Gay ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Intracellular Domain ◽  
Protein Precursor ◽  
Terminal Fragment ◽  
Β Protein

scholarly journals Amyloid-β Oligomers Induce Only Mild Changes to Inhibitory Bouton Dynamics

2021 ◽  
Vol 5 (1) ◽  
pp. 153-160 ◽  
Author(s):  
Marvin Ruiter ◽  
Christine Lützkendorf ◽  
Jian Liang ◽  
Corette J. Wierenga
Keyword(s):  
Hippocampal Slices ◽  
Inhibitory Neuron ◽  
Amyloid Β ◽  
Inhibitory Neurons ◽  
Inhibitory Synapses ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Β Protein ◽  
Plaque Load ◽  
Early Alzheimer’S Disease

The amyloid-β protein precursor is highly expressed in a subset of inhibitory neuron in the hippocampus, and inhibitory neurons have been suggested to play an important role in early Alzheimer’s disease plaque load. Here we investigated bouton dynamics in axons of hippocampal interneurons in two independent amyloidosis models. Short-term (24 h) amyloid-β (Aβ)-oligomer application to organotypic hippocampal slices slightly increased inhibitory bouton dynamics, but bouton density and dynamics were unchanged in hippocampus slices of young-adult AppNL - F - G-mice, in which Aβ levels are chronically elevated. These results indicate that loss or defective adaptation of inhibitory synapses are not a major contribution to Aβ-induced hyperexcitability.

scholarly journals Phosphorylation of KLC1 modifies interaction with JIP1 and abolishes the enhanced fast velocity of APP transport by kinesin-1

2017 ◽  
Vol 28 (26) ◽  
pp. 3857-3869 ◽  
Author(s):  
Kyoko Chiba ◽  
Ko-yi Chien ◽  
Yuriko Sobu ◽  
Saori Hata ◽  
Shun Kato ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Amyloid Β ◽  
Tetratricopeptide Repeat ◽  
Amyloid Β Protein ◽  
The Novel ◽  
Anterograde Transport ◽  
Interacting Protein ◽  
Protein Precursor ◽  
Kinesin Light Chain ◽  
Β Protein

In neurons, amyloid β-protein precursor (APP) is transported by binding to kinesin-1, mediated by JNK-interacting protein 1b (JIP1b), which generates the enhanced fast velocity (EFV) and efficient high frequency (EHF) of APP anterograde transport. Previously, we showed that EFV requires conventional interaction between the JIP1b C-terminal region and the kinesin light chain 1 (KLC1) tetratricopeptide repeat, whereas EHF requires a novel interaction between the central region of JIP1b and the coiled-coil domain of KLC1. We found that phosphorylatable Thr466 of KLC1 regulates the conventional interaction with JIP1b. Substitution of Glu for Thr466 abolished this interaction and EFV, but did not impair the novel interaction responsible for EHF. Phosphorylation of KLC1 at Thr466 increased in aged brains, and JIP1 binding to kinesin-1 decreased, suggesting that APP transport is impaired by aging. We conclude that phosphorylation of KLC1 at Thr466 regulates the velocity of transport of APP by kinesin-1 by modulating its interaction with JIP1b.

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