Alterations in cholinergic and non-cholinergic neurotransmitter receptor densities in transgenic Tg2576 mouse brain with β-amyloid plaque pathology

2003 ◽  
Vol 21 (7) ◽  
pp. 357-369 ◽  
Author(s):  
Margrit Klingner ◽  
Jenny Apelt ◽  
Ashok Kumar ◽  
Dietlind Sorger ◽  
Osama Sabri ◽  
...  
Keyword(s):  
Mouse Brain ◽  
Amyloid Plaque ◽  
Tg2576 Mouse ◽  
Neurotransmitter Receptor ◽  
Plaque Pathology ◽  
Β Amyloid ◽  
Cholinergic Neurotransmitter

Expression of β-secretase mRNA in transgenic Tg2576 mouse brain with Alzheimer plaque pathology

2000 ◽  
Vol 292 (2) ◽  
pp. 107-110 ◽  
Author(s):  
M Bigl ◽  
J Apelt ◽  
E.A Luschekina ◽  
C Lange-Dohna ◽  
S Roßner ◽  
...  
Keyword(s):  
Mouse Brain ◽  
Tg2576 Mouse ◽  
Plaque Pathology

Novel imaging agents for β-amyloid plaque based on the N-benzoylindole core

2011 ◽  
Vol 21 (18) ◽  
pp. 5594-5597 ◽  
Author(s):  
Yang Yang ◽  
Xin-Hong Duan ◽  
Jun-Yuan Deng ◽  
Bing Jin ◽  
Hong-Mei Jia ◽  
...  
Keyword(s):  
Amyloid Plaque ◽  
Imaging Agents ◽  
Β Amyloid

scholarly journals New Biochemical Insights to Unravel the Pathogenesis of Alzheimer's Lesions

1991 ◽  
Vol 18 (S3) ◽  
pp. 408-410 ◽  
Author(s):  
Alex E. Roher ◽  
Kenneth C. Palmer ◽  
John Capodilupo ◽  
Arun R. Wakade ◽  
Melvyn J. Ball
Keyword(s):  
Amyloid Plaque ◽  
Extracellular Proteins ◽  
High Yield ◽  
Chemical Fractionation ◽  
Core Proteins ◽  
Β Amyloid ◽  
Neuritic Sprouting

ABSTRACT:Purification of amyloid plaque core proteins (APCP) from Alzheimer's disease brains to complete homogeneity and in high yield permitted its chemical fractionation and characterization of its components. APCP is mainly made of β-amyloid (βA) and an assortment of glycoproteins (accounting for 20%) rich in carbohydrates compatible with N-and O-linked saccharides. When added to tissue culture of sympathetic and sensory neurons APCP and βA inhibited neuritic sprouting, a reversible phenomenon at low doses. Higher concentrations of both substances kill the neurons in culture. APCP is significantly more toxic than βA, suggesting the minor components may play an important role in increasing the toxicity of βA. If the observed toxic effects of APCP in situ are occurring in vivo during the course of AD, then the accumulation of these extracellular proteins could be largely responsible for some of the neuronal death observed in this neuropathology.

Targeted Intraparenchymal Delivery of Human NGF by Gene Transfer to the Primate Basal Forebrain for 3 Months Does Not Accelerate β-Amyloid Plaque Deposition

1998 ◽  
Vol 154 (2) ◽  
pp. 573-582 ◽  
Author(s):  
Mark H. Tuszynski ◽  
David E. Smith ◽  
Jeffrey Roberts ◽  
Heather McKay ◽  
Elliott Mufson
Keyword(s):  
Gene Transfer ◽  
Basal Forebrain ◽  
Amyloid Plaque ◽  
Plaque Deposition ◽  
Β Amyloid
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