Ultrastructural localization of amyloid β/A4 protein precursor in the normal rat brain

1993 ◽  
Vol 63 (1) ◽  
pp. 173-180 ◽  
Author(s):  
Tsuneo Yamazaki ◽  
Haruyasu Yamaguchi ◽  
Takeshi Kawarabayashi ◽  
Shunsaku Hirai
Keyword(s):  
Rat Brain ◽  
Amyloid Β ◽  
Ultrastructural Localization ◽  
Protein Precursor ◽  
Normal Rat

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

scholarly journals Ultrastructural Localization of Nitrotyrosine within the Caudate-Putamen Nucleus and the Globus Pallidus of Normal Rat Brain

2000 ◽  
Vol 20 (13) ◽  
pp. 4798-4808 ◽  
Author(s):  
Elizabeth A. Bolan ◽  
K. Noelle Gracy ◽  
June Chan ◽  
Rosario R. Trifiletti ◽  
Virginia M. Pickel
Keyword(s):  
Rat Brain ◽  
Globus Pallidus ◽  
Ultrastructural Localization ◽  
Caudate Putamen ◽  
Normal Rat

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

Angiogenesis Induced by Photodynamic Therapy in Normal Rat Brain¶

2004 ◽  
Vol 79 (6) ◽  
pp. 494 ◽  
Author(s):  
Feng Jiang ◽  
Zheng Gang Zhang ◽  
Mark Katakowski ◽  
Adam M Robin ◽  
Michelle Faber ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Rat Brain ◽  
Normal Rat

scholarly journals High Glycogen Levels in Brains of Rats with Minimal Environmental Stimuli: Implications for Metabolic Contributions of Working Astrocytes

2002 ◽  
Vol 22 (12) ◽  
pp. 1476-1489 ◽  
Author(s):  
Nancy F. Cruz ◽  
Gerald A. Dienel
Keyword(s):  
Rat Brain ◽  
Sensory Stimulation ◽  
Enzyme Inactivation ◽  
Biologically Active ◽  
Metabolic Labeling ◽  
Tissue Sampling ◽  
Normal Rat ◽  
Sampling Procedures ◽  
Very High

The concentration of glycogen, the major brain energy reserve localized mainly in astrocytes, is generally reported as about 2 or 3 μmol/g, but sometimes as high as 3.9 to 8 μmol/g, in normal rat brain. The authors found high but very different glycogen levels in two recent studies in which glycogen was determined by the routine amyloglucosidase procedure in 0.03N HCl digests either of frozen powders (4.8 to 6 μmol/g) or of ethanol-insoluble fractions (8 to 12 μmol/g). To evaluate the basis for these discrepant results, glycogen was assayed in parallel extracts of the same samples. Glycogen levels in ethanol extracts were twice those in 0.03N HCl digests, suggesting incomplete enzyme inactivation even with very careful thawing. The very high glycogen levels were biologically active and responsive to physiologic and pharmacological challenge. Glycogen levels fell after brief sensory stimulation, and metabolic labeling indicated its turnover under resting conditions. About 95% of the glycogen was degraded under in vitro ischemic conditions, and its “carbon equivalents” recovered mainly as glc, glc-P, and lactate. Resting glycogen stores were reduced by about 50% by chronic inhibition of nitric oxide synthase. Because neurotransmitters are known to stimulate glycogenolysis, stress or sensory activation due to animal handling and tissue-sampling procedures may stimulate glycogenolysis during an experiment, and glycogen lability during tissue sampling and extraction can further reduce glycogen levels. The very high glycogen levels in normal rat brain suggest an unrecognized role for astrocytic energy metabolism during brain activation.

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.

Sign in / Sign up

Export Citation Format

Share Document